[{"month":"07","external_id":{"pmid":["42399561"]},"oa_version":"Published Version","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1038/s41564-026-02403-6","open_access":"1"}],"type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["2058-5276"]},"year":"2026","citation":{"ista":"Navarro PP, Vettiger A, Hajdu R, Ananda VY, López-Tavares A, Schmid EW, Walter JC, Loose M, Chao LH, Bernhardt TG. 2026. The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. Nature Microbiology.","apa":"Navarro, P. P., Vettiger, A., Hajdu, R., Ananda, V. Y., López-Tavares, A., Schmid, E. W., … Bernhardt, T. G. (2026). The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. <i>Nature Microbiology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41564-026-02403-6\">https://doi.org/10.1038/s41564-026-02403-6</a>","mla":"Navarro, Paula P., et al. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site against Osmotic Rupture.” <i>Nature Microbiology</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41564-026-02403-6\">10.1038/s41564-026-02403-6</a>.","ama":"Navarro PP, Vettiger A, Hajdu R, et al. The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. <i>Nature Microbiology</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41564-026-02403-6\">10.1038/s41564-026-02403-6</a>","short":"P.P. Navarro, A. Vettiger, R. Hajdu, V.Y. Ananda, A. López-Tavares, E.W. Schmid, J.C. Walter, M. Loose, L.H. Chao, T.G. Bernhardt, Nature Microbiology (2026).","chicago":"Navarro, Paula P., Andrea Vettiger, Roman Hajdu, Virly Y. Ananda, Alejandro López-Tavares, Ernst W. Schmid, Johannes C. Walter, Martin Loose, Luke H. Chao, and Thomas G. Bernhardt. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site against Osmotic Rupture.” <i>Nature Microbiology</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41564-026-02403-6\">https://doi.org/10.1038/s41564-026-02403-6</a>.","ieee":"P. P. Navarro <i>et al.</i>, “The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture,” <i>Nature Microbiology</i>. Springer Nature, 2026."},"oa":1,"date_created":"2026-07-12T22:02:19Z","ddc":["570"],"article_type":"original","date_updated":"2026-07-13T09:22:49Z","OA_place":"publisher","publisher":"Springer Nature","doi":"10.1038/s41564-026-02403-6","dataavailabilitystatement":"The data, plasmids and strains that support the findings of this study are available from the corresponding authors by request. Representative tomograms are deposited in EMDB: EMD-27479 (wild-type), EMD-53351 (∆ponB), EMD-53357(∆lpoB) and EMD-53363 (∆ponA). Corresponding raw movie frames and stacks of tilt series are deposited as EMPIAR-11090 (wild type), EMPIAR-13502 (∆ponB), EMPIAR-13513 (∆lpoB) and EMPIAR-13512 (∆ponA), and will be released upon publication. Other data related to this manuscript (for example, AFM, light microscopy, growth curves and so on) can be found on Zenodo at https://doi.org/10.5281/zenodo.20841819 (ref. 101). Source data are provided with this paper. Scripts used in this study were deposited on GitHub at https://github.com/NavarroVettiger/Navarro-et-al_2022 and https://github.com/virlyananda/EM-ImageProcessing.","_id":"22269","researchdata_availability":"yes","day":"03","abstract":[{"lang":"eng","text":"The divisome apparatus synthesizes septal peptidoglycan (PG) during bacterial division. In Escherichia coli, the class A penicillin-binding protein (aPBP) called PBP1b has been implicated in division, but its role in the process has remained unclear. Here we show using in situ cryo-electron tomography, genetics and other imaging methods that PBP1b is required to produce a wedge-like density of PG at the division site and that loss of this structure weakens the division site, making it hypersusceptible to osmotic lysis. Surprisingly, the activator LpoB needed for general PBP1b function was not required for its role in division. Of the two PBP1b isoforms produced in cells, we show that the one with an extended cytoplasmic N terminus localizes to and functions at the division site, probably via recruitment by the FtsA component of the divisome. The conservation of aPBPs with extended cytoplasmic N termini suggests that other Gram-negative bacteria may use similar mechanisms for division site reinforcement."}],"quality_controlled":"1","supplementarymaterial":"yes","fulldoi":"https://doi.org/10.1038/s41564-026-02403-6","has_accepted_license":"1","das_tickbox":"1","pmid":1,"date_published":"2026-07-03T00:00:00Z","author":[{"full_name":"Navarro, Paula P.","last_name":"Navarro","first_name":"Paula P."},{"full_name":"Vettiger, Andrea","last_name":"Vettiger","first_name":"Andrea"},{"id":"ffab949d-133f-11ed-8f02-94de21ace503","full_name":"Hajdu, Roman","last_name":"Hajdu","first_name":"Roman"},{"first_name":"Virly Y.","full_name":"Ananda, Virly Y.","last_name":"Ananda"},{"full_name":"López-Tavares, Alejandro","last_name":"López-Tavares","first_name":"Alejandro"},{"last_name":"Schmid","full_name":"Schmid, Ernst W.","first_name":"Ernst W."},{"first_name":"Johannes C.","last_name":"Walter","full_name":"Walter, Johannes C."},{"full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","orcid":"0000-0001-7309-9724","first_name":"Martin"},{"full_name":"Chao, Luke H.","last_name":"Chao","first_name":"Luke H."},{"first_name":"Thomas G.","full_name":"Bernhardt, Thomas G.","last_name":"Bernhardt"}],"publication_status":"epub_ahead","article_processing_charge":"Yes (in subscription journal)","OA_type":"hybrid","acknowledgement":"We thank all members of the Bernhardt, Rudner, Navarro and Vettiger Laboratories for support and helpful conversations. We thank C. Genoud, J. Daraspe, A. Mucciolo and D. de Bellis at the Electron Microscopy Facility of the University of Lausanne and E. Jeanvoine for providing access to workstations for cryo-ET image processing; S. Sterling, C. Borsa, J. Podgorski, P. Vinh Dip, E. Brignole and A. Osherov at the MIT.nano cryo-EM facility, K. Song and C. Xu at the University of Massachusetts cryo-EM facility, and R. Walsh and Z. Li at the cryo-EM at Harvard Medical School facility for providing access to the cryo-EM microscopes and for all their help, advice and maintenance of cryo-EM equipment. AFM was performed at the Harvard University Center for Nanoscale Systems (CNS), a member of the National Nanotechnology Coordinated Infrastructure Network (NNCI), which is supported by the National Science Foundation under NSF award no. ECCS-2025158. We thank N. S. Colella for excellent advice on AFM data acquisition and analysis; the MicRoN imaging core at Harvard Medical School for excellent advice on live cell imaging and maintenance of fluorescence microscopes; B. Krautz for creating the cartoon illustrations (www.sciencecommunicated.com); and L. Miles and R. Aeschimann for assistance with strain construction. A.V. was supported by an EMBO long-term postdoctoral fellowship ALTF_89-2019, the Swiss National Science Foundation (SNSF) Postdoc.Mobility fellowship P500PB_203143. P.P.N. was a recipient of early postdoc.mobility and postdoc.mobility fellowships (P2BSP3_188112 and P400PB_199252). This work was also supported by funding from the National Institutes of Health (R35GM142553 to L.H.C. and R01AI083365 to T.G.B.), investigator funds from the Howard Hughes Medical Institute (T.G.B.), an SNSF project grant (320030-236243 to A.V.), an SNSF Starting Grant (TMSGI3_218251 to P.P.N.), an SNSF Project grant (320030-236069 to P.P.N), an SNSF SPARK grant (CRSK-3_237167 to P.P.N.), cryo-EM funds from the Faculty of Biology and Medicine at University of Lausanne to P.P.N. and the Foundation Pierre Mercier pour la Science (to P.P.N.).","title":"The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture","language":[{"iso":"eng"}],"department":[{"_id":"MaLo"},{"_id":"GradSch"}],"status":"public","publication":"Nature Microbiology"},{"year":"2026","project":[{"_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","name":"IST-BRIDGE: International postdoctoral program","grant_number":"101034413","call_identifier":"H2020"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb"}],"type":"journal_article","corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"scopus_import":"1","oa_version":"None","month":"04","external_id":{"pmid":["41990175"]},"article_type":"original","date_updated":"2026-09-03T09:36:24Z","date_created":"2026-04-26T22:01:46Z","citation":{"chicago":"Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu, Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>. AAAS, 2026. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>.","ieee":"B. L. Springstein <i>et al.</i>, “Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape,” <i>Science</i>, vol. 392, no. 6795. AAAS, 2026.","mla":"Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>, vol. 392, no. 6795, eaea6343, AAAS, 2026, doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>.","apa":"Springstein, B. L., Javoor, M., Megrian, D., Hajdu, R., Hanke, D. M., Zens, B., … Loose, M. (2026). Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. AAAS. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>","ista":"Springstein BL, Javoor M, Megrian D, Hajdu R, Hanke DM, Zens B, Weiss GL, Schur FK, Loose M. 2026. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. Science. 392(6795), eaea6343.","ama":"Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. 2026;392(6795). doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>","short":"B.L. Springstein, M. Javoor, D. Megrian, R. Hajdu, D.M. Hanke, B. Zens, G.L. Weiss, F.K. Schur, M. Loose, Science 392 (2026)."},"issue":"6795","fulldoi":"https://doi.org/10.1126/science.aea6343","abstract":[{"text":"Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal system named CorMR with a function in cell shape control rather than DNA segregation. Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed that CorM formed dynamically unstable, antiparallel double-stranded filaments that were recruited to the membrane by CorR through an amphipathic helix conserved in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which excluded them from the poles and division plane. Comparative genomics indicated that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity, highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.","lang":"eng"}],"day":"16","quality_controlled":"1","_id":"21762","doi":"10.1126/science.aea6343","publisher":"AAAS","ec_funded":1,"department":[{"_id":"MaLo"},{"_id":"FlSc"},{"_id":"GradSch"},{"_id":"EM-Fac"}],"publication":"Science","article_number":"eaea6343","status":"public","related_material":{"record":[{"id":"22744","relation":"dissertation_contains","status":"public"}]},"language":[{"iso":"eng"}],"publication_status":"published","author":[{"last_name":"Springstein","full_name":"Springstein, Benjamin L","orcid":"0000-0002-3461-5391","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","first_name":"Benjamin L"},{"first_name":"Manjunath","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","last_name":"Javoor"},{"first_name":"Daniela","last_name":"Megrian","full_name":"Megrian, Daniela"},{"first_name":"Roman","last_name":"Hajdu","full_name":"Hajdu, Roman","id":"ffab949d-133f-11ed-8f02-94de21ace503"},{"last_name":"Hanke","full_name":"Hanke, Dustin M.","first_name":"Dustin M."},{"last_name":"Zens","orcid":"0000-0002-9561-1239","id":"45FD126C-F248-11E8-B48F-1D18A9856A87","full_name":"Zens, Bettina","first_name":"Bettina"},{"last_name":"Weiss","full_name":"Weiss, Gregor L.","first_name":"Gregor L."},{"orcid":"0000-0003-4790-8078","last_name":"Schur","full_name":"Schur, Florian Km","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian Km"},{"first_name":"Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"intvolume":"       392","title":"Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape","OA_type":"closed access","acknowledgement":"We thank all members of the Loose lab at ISTA for helpful discussions; M. Kojic for critical reading of the manuscript; A. Herrero (Sevilla University) for sharing her extensive BACTH plasmid library and other plasmids, as well as cyanobacterial strains; T. Dagan and F. Nies (both Kiel University) for sharing cyanobacterial strains and plasmids and for valuable discussions; N. Sapay and A. Michon for providing the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix screen of cyanobacterial CorR proteins; V.-V. Hodirnau for support in cryo-ET data collection; and J. Hansen for advice about cryo-EM data processing.\r\nThis work was supported by the Scientific Service Units (SSU) of ISTA through resources provided by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp), the Electron Microscopy Facility (EMF), and the Lab Support Facility (LSF). This work was funded by the European Union’s Horizon 2020 research and innovation program (Marie Skłodowska-Curie grant 101034413 to B.L.S.); the European Research Council (ERC) of the European Union (grant ActinID 101076260 to F.K.M.S.); the Swiss National Science Foundation (starting grant TMSGI3_226208 to G.L.W.); and the Jean-Jacques et Letitia Lopez-Loreta Foundation (G.L.W.).","article_processing_charge":"No","date_published":"2026-04-16T00:00:00Z","volume":392,"pmid":1,"acknowledged_ssus":[{"_id":"Bio"},{"_id":"ScienComp"},{"_id":"EM-Fac"},{"_id":"LifeSc"}]},{"date_published":"2025-08-29T00:00:00Z","pmid":1,"volume":11,"author":[{"last_name":"Wilmes","full_name":"Wilmes, Stephan","first_name":"Stephan"},{"first_name":"Jesse","last_name":"Tönjes","full_name":"Tönjes, Jesse"},{"last_name":"Drechsler","full_name":"Drechsler, Maik","first_name":"Maik"},{"last_name":"Ruf","full_name":"Ruf, Anita","first_name":"Anita"},{"first_name":"Jan Hannes","last_name":"Schäfer","full_name":"Schäfer, Jan Hannes"},{"full_name":"Lürick, Anna","last_name":"Lürick","first_name":"Anna"},{"last_name":"Januliene","full_name":"Januliene, Dovile","first_name":"Dovile"},{"last_name":"Apelt","full_name":"Apelt, Steven","first_name":"Steven"},{"first_name":"Daniele","full_name":"Di Iorio, Daniele","last_name":"Di Iorio"},{"first_name":"Seraphine V.","full_name":"Wegner, Seraphine V.","last_name":"Wegner"},{"first_name":"Martin","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","orcid":"0000-0001-7309-9724"},{"first_name":"Arne","last_name":"Moeller","full_name":"Moeller, Arne"},{"first_name":"Achim","last_name":"Paululat","full_name":"Paululat, Achim"},{"first_name":"Daniel","full_name":"Kümmel, Daniel","last_name":"Kümmel"}],"publication_status":"published","title":"Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned","intvolume":"        11","acknowledgement":"We thank A.-M. Lawrence-Dörner and B. Berkenfeld for technical assistance and the members of the Kümmel Lab for constructive feedback. We are grateful to C. Ungermann and L. Langemeyer for insightful discussions and to F. Barr for providing plasmids encoding Fuzzy, Inturned, Rab23, and Rsg1. The template clone Flag-ciBAR1 was a gift from K.-I. Takemaru (Addgene, plasmid #200440). We thank the Bloomington Drosophila Stock center (BDSC) and DSHB for providing fly stocks and antibodies. This work was supported by the German Research Foundation (DFG) through the grants SFB1557-P10 (D.K.), SFB1557-P11 (A.M.), and SFB1577-P6, PA517/12-2, PA517/14-1, PA517/15-1, and PA517/16-1 (A.P.). Cryo-EM data were collected at the infrastructure of the University of Osnabrück, funded by the DFG (project number 455249646). J.-H.S. was supported by the Friedrich-Ebert Foundation. M.L. acknowledges funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement number 101045340).","OA_type":"gold","article_processing_charge":"Yes","language":[{"iso":"eng"}],"department":[{"_id":"MaLo"}],"publication":"Science Advances","status":"public","page":"eadx2893","OA_place":"publisher","doi":"10.1126/sciadv.adx2893","file_date_updated":"2025-09-15T07:23:12Z","publisher":"AAAS","_id":"20351","PlanS_conform":"1","abstract":[{"text":"Rab GTPases organize intracellular trafficking and provide identity to organelles. Their spatiotemporal activation by guanine nucleotide exchange factors (GEFs) is tightly controlled to ensure fidelity. Our structural and functional comparison of the tri-longin domain RabGEFs Mon1-Ccz1 and Fuzzy-Inturned reveals the molecular basis for their target specificity. Both complexes rely on a conserved sequence motif of their substrate GTPases for the catalytic mechanism, while secondary interactions allow discrimination between targets. We also find that dimeric Mon1-Ccz1 from fungi and the metazoan homologs with the additional third subunit RMC1/Bulli bind membranes through electrostatic interactions via distinct interfaces. Protein-lipid interaction studies and functional characterization in flies reveal an essential function of RMC1/Bulli as mediator of GEF complex membrane recruitment. In the case of Fuzzy-Inturned, reconstitution experiments demonstrate that the BAR (Bin-Amphiphysin-Rvs) domain protein CiBAR1 can support membrane recruitment of the GEF. Collectively, our study demonstrates the molecular basis for the adaptation of TLD-RabGEFs to different cellular functions.","lang":"eng"}],"day":"29","quality_controlled":"1","fulldoi":"https://doi.org/10.1126/sciadv.adx2893","has_accepted_license":"1","issue":"35","oa":1,"citation":{"chicago":"Wilmes, Stephan, Jesse Tönjes, Maik Drechsler, Anita Ruf, Jan Hannes Schäfer, Anna Lürick, Dovile Januliene, et al. “Mechanistic Adaptation of the Metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.” <i>Science Advances</i>. AAAS, 2025. <a href=\"https://doi.org/10.1126/sciadv.adx2893\">https://doi.org/10.1126/sciadv.adx2893</a>.","ieee":"S. Wilmes <i>et al.</i>, “Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned,” <i>Science Advances</i>, vol. 11, no. 35. AAAS, p. eadx2893, 2025.","apa":"Wilmes, S., Tönjes, J., Drechsler, M., Ruf, A., Schäfer, J. H., Lürick, A., … Kümmel, D. (2025). Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. <i>Science Advances</i>. AAAS. <a href=\"https://doi.org/10.1126/sciadv.adx2893\">https://doi.org/10.1126/sciadv.adx2893</a>","mla":"Wilmes, Stephan, et al. “Mechanistic Adaptation of the Metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.” <i>Science Advances</i>, vol. 11, no. 35, AAAS, 2025, p. eadx2893, doi:<a href=\"https://doi.org/10.1126/sciadv.adx2893\">10.1126/sciadv.adx2893</a>.","ista":"Wilmes S, Tönjes J, Drechsler M, Ruf A, Schäfer JH, Lürick A, Januliene D, Apelt S, Di Iorio D, Wegner SV, Loose M, Moeller A, Paululat A, Kümmel D. 2025. Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science Advances. 11(35), eadx2893.","ama":"Wilmes S, Tönjes J, Drechsler M, et al. Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. <i>Science Advances</i>. 2025;11(35):eadx2893. doi:<a href=\"https://doi.org/10.1126/sciadv.adx2893\">10.1126/sciadv.adx2893</a>","short":"S. Wilmes, J. Tönjes, M. Drechsler, A. Ruf, J.H. Schäfer, A. Lürick, D. Januliene, S. Apelt, D. Di Iorio, S.V. Wegner, M. Loose, A. Moeller, A. Paululat, D. Kümmel, Science Advances 11 (2025) eadx2893."},"file":[{"relation":"main_file","file_name":"2025_ScienceAdvance_Wilmes.pdf","file_id":"20355","date_updated":"2025-09-15T07:23:12Z","creator":"dernst","checksum":"a3de801f3c6c1deadd7099d965db799a","access_level":"open_access","file_size":3434827,"content_type":"application/pdf","success":1,"date_created":"2025-09-15T07:23:12Z"}],"date_created":"2025-09-14T22:01:32Z","ddc":["570"],"isi":1,"article_type":"original","date_updated":"2025-09-30T14:40:27Z","month":"08","external_id":{"isi":["001559806100033"],"pmid":["40864718"]},"scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"oa_version":"Published Version","DOAJ_listed":"1","type":"journal_article","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication_identifier":{"eissn":["2375-2548"]},"project":[{"_id":"bd6ae2ca-d553-11ed-ba76-a4aa239da5ee","name":"Synthetic and structural biology of Rab GTPase networks","grant_number":"101045340"}],"year":"2025"},{"scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"oa_version":"Published Version","external_id":{"isi":["001154500400001"],"pmid":["38134934"]},"month":"01","project":[{"name":"Interaction and feedback between cell mechanics and fate specification in vertebrate gastrulation","grant_number":"742573","call_identifier":"H2020","_id":"260F1432-B435-11E9-9278-68D0E5697425"}],"year":"2024","publication_identifier":{"issn":["0960-9822"],"eissn":["1879-0445"]},"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","corr_author":"1","type":"journal_article","file":[{"relation":"main_file","date_updated":"2024-01-16T10:53:31Z","file_id":"14813","file_name":"2024_CurrentBiology_Arslan.pdf","checksum":"51220b76d72a614208f84bdbfbaf9b72","creator":"dernst","success":1,"date_created":"2024-01-16T10:53:31Z","access_level":"open_access","content_type":"application/pdf","file_size":5183861}],"date_created":"2024-01-14T23:00:56Z","oa":1,"citation":{"ieee":"F. N. Arslan, E. B. Hannezo, J. Merrin, M. Loose, and C.-P. J. Heisenberg, “Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts,” <i>Current Biology</i>, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024.","chicago":"Arslan, Feyza N, Edouard B Hannezo, Jack Merrin, Martin Loose, and Carl-Philipp J Heisenberg. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell Contacts.” <i>Current Biology</i>. Elsevier, 2024. <a href=\"https://doi.org/10.1016/j.cub.2023.11.067\">https://doi.org/10.1016/j.cub.2023.11.067</a>.","ama":"Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts. <i>Current Biology</i>. 2024;34(1):171-182.e8. doi:<a href=\"https://doi.org/10.1016/j.cub.2023.11.067\">10.1016/j.cub.2023.11.067</a>","short":"F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current Biology 34 (2024) 171–182.e8.","mla":"Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell Contacts.” <i>Current Biology</i>, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8, doi:<a href=\"https://doi.org/10.1016/j.cub.2023.11.067\">10.1016/j.cub.2023.11.067</a>.","apa":"Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., &#38; Heisenberg, C.-P. J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts. <i>Current Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cub.2023.11.067\">https://doi.org/10.1016/j.cub.2023.11.067</a>","ista":"Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. 2024. Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 34(1), 171–182.e8."},"date_updated":"2025-09-04T11:39:10Z","article_type":"original","isi":1,"ddc":["570"],"_id":"14795","doi":"10.1016/j.cub.2023.11.067","file_date_updated":"2024-01-16T10:53:31Z","publisher":"Elsevier","has_accepted_license":"1","fulldoi":"https://doi.org/10.1016/j.cub.2023.11.067","issue":"1","quality_controlled":"1","abstract":[{"text":"Metazoan development relies on the formation and remodeling of cell-cell contacts. Dynamic reorganization of adhesion receptors and the actomyosin cell cortex in space and time plays a central role in cell-cell contact formation and maturation. Nevertheless, how this process is mechanistically achieved when new contacts are formed remains unclear. Here, by building a biomimetic assay composed of progenitor cells adhering to supported lipid bilayers functionalized with E-cadherin ectodomains, we show that cortical F-actin flows, driven by the depletion of myosin-2 at the cell contact center, mediate the dynamic reorganization of adhesion receptors and cell cortex at the contact. E-cadherin-dependent downregulation of the small GTPase RhoA at the forming contact leads to both a depletion of myosin-2 and a decrease of F-actin at the contact center. At the contact rim, in contrast, myosin-2 becomes enriched by the retraction of bleb-like protrusions, resulting in a cortical tension gradient from the contact rim to its center. This tension gradient, in turn, triggers centrifugal F-actin flows, leading to further accumulation of F-actin at the contact rim and the progressive redistribution of E-cadherin from the contact center to the rim. Eventually, this combination of actomyosin downregulation and flows at the contact determines the characteristic molecular organization, with E-cadherin and F-actin accumulating at the contact rim, where they are needed to mechanically link the contractile cortices of the adhering cells.","lang":"eng"}],"day":"08","title":"Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts","intvolume":"        34","article_processing_charge":"Yes (via OA deal)","acknowledgement":"We are grateful to Edwin Munro for their feedback and help with the single particle analysis. We thank members of the Heisenberg and Loose labs for their help and feedback on the manuscript, notably Xin Tong for making the PCS2-mCherry-AHPH plasmid. Finally, we thank the Aquatics and Imaging & Optics facilities of ISTA for their continuous support, especially Yann Cesbron for assistance with the laser cutter. This work was supported by an ERC\r\nAdvanced Grant (MECSPEC) to C.-P.H.","author":[{"first_name":"Feyza N","id":"49DA7910-F248-11E8-B48F-1D18A9856A87","last_name":"Arslan","orcid":"0000-0001-5809-9566","full_name":"Arslan, Feyza N"},{"id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6005-1561","last_name":"Hannezo","full_name":"Hannezo, Edouard B","first_name":"Edouard B"},{"full_name":"Merrin, Jack","id":"4515C308-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-5145-4609","last_name":"Merrin","first_name":"Jack"},{"full_name":"Loose, Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin"},{"first_name":"Carl-Philipp J","id":"39427864-F248-11E8-B48F-1D18A9856A87","full_name":"Heisenberg, Carl-Philipp J","orcid":"0000-0002-0912-4566","last_name":"Heisenberg"}],"publication_status":"published","acknowledged_ssus":[{"_id":"Bio"},{"_id":"PreCl"}],"date_published":"2024-01-08T00:00:00Z","volume":34,"pmid":1,"publication":"Current Biology","status":"public","page":"171-182.e8","ec_funded":1,"department":[{"_id":"CaHe"},{"_id":"EdHa"},{"_id":"MaLo"},{"_id":"NanoFab"}],"language":[{"iso":"eng"}]},{"ddc":["570"],"isi":1,"article_type":"review","date_updated":"2025-09-04T11:45:31Z","citation":{"short":"P. Radler, M. Loose, European Journal of Cell Biology 103 (2024).","ama":"Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. <i>European Journal of Cell Biology</i>. 2024;103(1). doi:<a href=\"https://doi.org/10.1016/j.ejcb.2023.151380\">10.1016/j.ejcb.2023.151380</a>","apa":"Radler, P., &#38; Loose, M. (2024). A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. <i>European Journal of Cell Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ejcb.2023.151380\">https://doi.org/10.1016/j.ejcb.2023.151380</a>","mla":"Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.” <i>European Journal of Cell Biology</i>, vol. 103, no. 1, 151380, Elsevier, 2024, doi:<a href=\"https://doi.org/10.1016/j.ejcb.2023.151380\">10.1016/j.ejcb.2023.151380</a>.","ista":"Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. 103(1), 151380.","ieee":"P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches,” <i>European Journal of Cell Biology</i>, vol. 103, no. 1. Elsevier, 2024.","chicago":"Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.” <i>European Journal of Cell Biology</i>. Elsevier, 2024. <a href=\"https://doi.org/10.1016/j.ejcb.2023.151380\">https://doi.org/10.1016/j.ejcb.2023.151380</a>."},"oa":1,"date_created":"2024-01-18T08:16:43Z","file":[{"relation":"main_file","file_id":"17265","date_updated":"2024-07-16T12:07:20Z","file_name":"2024_EJCB_Radler.pdf","checksum":"5d170abbc87585205c010657e4552360","creator":"dernst","date_created":"2024-07-16T12:07:20Z","success":1,"file_size":9995304,"content_type":"application/pdf","access_level":"open_access"}],"corr_author":"1","type":"journal_article","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication_identifier":{"issn":["0171-9335"]},"project":[{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"}],"year":"2024","month":"03","external_id":{"pmid":["38218128"],"isi":["001166216800001"]},"oa_version":"Published Version","scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"language":[{"iso":"eng"}],"department":[{"_id":"MaLo"}],"status":"public","article_number":"151380","publication":"European Journal of Cell Biology","date_published":"2024-03-01T00:00:00Z","pmid":1,"volume":103,"publication_status":"published","author":[{"first_name":"Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","full_name":"Radler, Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 "},{"last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin"}],"article_processing_charge":"Yes","acknowledgement":"We acknowledge members of the Loose laboratory at ISTA for helpful discussions—in particular M. Kojic for his insightful comments. This work was supported by the Austrian Science Fund (FWF P34607) to M.L.","title":"A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches","intvolume":"       103","day":"01","abstract":[{"text":"Bacteria divide by binary fission. The protein machine responsible for this process is the divisome, a transient assembly of more than 30 proteins in and on the surface of the cytoplasmic membrane. Together, they constrict the cell envelope and remodel the peptidoglycan layer to eventually split the cell into two. For Escherichia coli, most molecular players involved in this process have probably been identified, but obtaining the quantitative information needed for a mechanistic understanding can often not be achieved from experiments in vivo alone. Since the discovery of the Z-ring more than 30 years ago, in vitro reconstitution experiments have been crucial to shed light on molecular processes normally hidden in the complex environment of the living cell. In this review, we summarize how rebuilding the divisome from purified components – or at least parts of it - have been instrumental to obtain the detailed mechanistic understanding of the bacterial cell division machinery that we have today.","lang":"eng"}],"quality_controlled":"1","fulldoi":"https://doi.org/10.1016/j.ejcb.2023.151380","issue":"1","has_accepted_license":"1","publisher":"Elsevier","doi":"10.1016/j.ejcb.2023.151380","file_date_updated":"2024-07-16T12:07:20Z","_id":"14834","keyword":["Cell Biology","General Medicine","Histology","Pathology and Forensic Medicine"]},{"oa_version":"None","scopus_import":"1","external_id":{"pmid":["38443575"],"isi":["001183270800021"]},"month":"03","year":"2024","project":[{"_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607","name":"In vitro reconstitution of bacterial cell division"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication_identifier":{"eissn":["2058-5276"]},"type":"journal_article","date_created":"2024-03-17T23:00:58Z","citation":{"ieee":"P. Nußbaum <i>et al.</i>, “Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division,” <i>Nature Microbiology</i>, vol. 9, no. 3. Springer Nature, pp. 698–711, 2024.","chicago":"Nußbaum, Phillip, Danguole Kureisaite-Ciziene, Dom Bellini, Chris Van Der Does, Marko Kojic, Najwa Taib, Anna Yeates, et al. “Proteins Containing Photosynthetic Reaction Centre Domains Modulate FtsZ-Based Archaeal Cell Division.” <i>Nature Microbiology</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41564-024-01600-5\">https://doi.org/10.1038/s41564-024-01600-5</a>.","short":"P. Nußbaum, D. Kureisaite-Ciziene, D. Bellini, C. Van Der Does, M. Kojic, N. Taib, A. Yeates, M. Tourte, S. Gribaldo, M. Loose, J. Löwe, S.V. Albers, Nature Microbiology 9 (2024) 698–711.","ama":"Nußbaum P, Kureisaite-Ciziene D, Bellini D, et al. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. <i>Nature Microbiology</i>. 2024;9(3):698-711. doi:<a href=\"https://doi.org/10.1038/s41564-024-01600-5\">10.1038/s41564-024-01600-5</a>","apa":"Nußbaum, P., Kureisaite-Ciziene, D., Bellini, D., Van Der Does, C., Kojic, M., Taib, N., … Albers, S. V. (2024). Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. <i>Nature Microbiology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41564-024-01600-5\">https://doi.org/10.1038/s41564-024-01600-5</a>","mla":"Nußbaum, Phillip, et al. “Proteins Containing Photosynthetic Reaction Centre Domains Modulate FtsZ-Based Archaeal Cell Division.” <i>Nature Microbiology</i>, vol. 9, no. 3, Springer Nature, 2024, pp. 698–711, doi:<a href=\"https://doi.org/10.1038/s41564-024-01600-5\">10.1038/s41564-024-01600-5</a>.","ista":"Nußbaum P, Kureisaite-Ciziene D, Bellini D, Van Der Does C, Kojic M, Taib N, Yeates A, Tourte M, Gribaldo S, Loose M, Löwe J, Albers SV. 2024. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. Nature Microbiology. 9(3), 698–711."},"date_updated":"2026-04-07T12:27:57Z","isi":1,"article_type":"original","_id":"15118","publisher":"Springer Nature","doi":"10.1038/s41564-024-01600-5","issue":"3","fulldoi":"https://doi.org/10.1038/s41564-024-01600-5","quality_controlled":"1","day":"04","abstract":[{"lang":"eng","text":"Cell division in all domains of life requires the orchestration of many proteins, but in Archaea most of the machinery remains poorly characterized. Here we investigate the FtsZ-based cell division mechanism in Haloferax volcanii and find proteins containing photosynthetic reaction centre (PRC) barrel domains that play an essential role in archaeal cell division. We rename these proteins cell division protein B 1 (CdpB1) and CdpB2. Depletions and deletions in their respective genes cause severe cell division defects, generating drastically enlarged cells. Fluorescence microscopy of tagged FtsZ1, FtsZ2 and SepF in CdpB1 and CdpB2 mutant strains revealed an unusually disordered divisome that is not organized into a distinct ring-like structure. Biochemical analysis shows that SepF forms a tripartite complex with CdpB1/2 and crystal structures suggest that these two proteins might form filaments, possibly aligning SepF and the FtsZ2 ring during cell division. Overall our results indicate that PRC-domain proteins play essential roles in FtsZ-based cell division in Archaea."}],"article_processing_charge":"No","acknowledgement":"We thank X. Ye (ISTA) for providing the His–SUMO expression plasmid pSVA13429. pCDB302 was a gift from C. Bahl (Addgene plasmid number 113673; http://n2t.net/addgene:113673; RRID Addgene_113673). We thank B. Ahsan, G. Sharov, G. Cannone and S. Chen from the Medical Research Council (MRC) LMB Electron Microscopy Facility for help and support. We thank Scientific Computing at the MRC LMB for their support. We thank L. Trübestein and N. Krasnici of the protein service unit of the ISTA Lab Support Facility for help with the SEC coupled with multi-angle light scattering experiments. We thank D. Grohmann and R. Reichelt from the Archaea Centre at the University of Regensburg for providing the P. furiosus cell material. P.N. and S.-V.A. were supported by a Momentum grant from the Volkswagen (VW) Foundation (grant number 94933). D.K.-C. and D.B. were supported by the VW Stiftung ‘Life?’ programme (to J.L.; grant number Az 96727) and by the MRC, as part of UK Research and Innovation (UKRI), MRC file reference number U105184326 (to J.L.). N.T. and S.G. acknowledge support from the French Government’s Investissement d’Avenir program, Laboratoire d’Excellence ‘Integrative Biology of Emerging Infectious Diseases’ (grant number ANR-10-LABX-62-IBEID), and the computational and storage services (Maestro cluster) provided by the IT department at Institut Pasteur. M.K. and M.L. were supported by the Austrian Science Fund (FWF) Stand-Alone P34607. For the purpose of open access, the MRC Laboratory of Molecular Biology has applied a CC BY public copyright licence to any author accepted manuscript version arising.","title":"Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division","intvolume":"         9","publication_status":"published","author":[{"last_name":"Nußbaum","full_name":"Nußbaum, Phillip","first_name":"Phillip"},{"last_name":"Kureisaite-Ciziene","full_name":"Kureisaite-Ciziene, Danguole","first_name":"Danguole"},{"last_name":"Bellini","full_name":"Bellini, Dom","first_name":"Dom"},{"first_name":"Chris","last_name":"Van Der Does","full_name":"Van Der Does, Chris"},{"first_name":"Marko","orcid":"0000-0001-7244-8128","full_name":"Kojic, Marko","last_name":"Kojic","id":"73e7ecd4-dc85-11ea-9058-88a16394b160"},{"last_name":"Taib","full_name":"Taib, Najwa","first_name":"Najwa"},{"first_name":"Anna","full_name":"Yeates, Anna","last_name":"Yeates"},{"first_name":"Maxime","full_name":"Tourte, Maxime","last_name":"Tourte"},{"last_name":"Gribaldo","full_name":"Gribaldo, Simonetta","first_name":"Simonetta"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","first_name":"Martin"},{"first_name":"Jan","full_name":"Löwe, Jan","last_name":"Löwe"},{"first_name":"Sonja Verena","last_name":"Albers","full_name":"Albers, Sonja Verena"}],"acknowledged_ssus":[{"_id":"LifeSc"}],"pmid":1,"date_published":"2024-03-04T00:00:00Z","volume":9,"page":"698-711","status":"public","publication":"Nature Microbiology","department":[{"_id":"MaLo"}],"language":[{"iso":"eng"}],"related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"20741"}]}},{"oa_version":"Published Version","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"scopus_import":"1","external_id":{"pmid":["38506228"],"isi":["001266917100005"]},"month":"04","year":"2024","project":[{"_id":"2564DBCA-B435-11E9-9278-68D0E5697425","name":"International IST Doctoral Program","grant_number":"665385","call_identifier":"H2020"},{"name":"Peptide receptors for auxin canalization in Arabidopsis","grant_number":"I06123","_id":"bd76d395-d553-11ed-ba76-f678c14f9033"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"corr_author":"1","type":"journal_article","date_created":"2024-04-19T09:54:59Z","file":[{"access_level":"open_access","file_size":25845948,"content_type":"application/pdf","success":1,"date_created":"2025-01-09T08:41:16Z","creator":"dernst","checksum":"6dc023f0cc7052ad3cf0a42589d2e30f","file_name":"2024_JourCellScience_Gnyliukh.pdf","file_id":"18792","date_updated":"2025-01-09T08:41:16Z","relation":"main_file"}],"citation":{"ieee":"N. Gnyliukh <i>et al.</i>, “Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana,” <i>Journal of Cell Science</i>, vol. 137, no. 8. The Company of Biologists, 2024.","chicago":"Gnyliukh, Nataliia, Alexander J Johnson, MK Nagel, Aline Monzer, David Babic, Annamaria Hlavata, SS Alotaibi, E Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Arabidopsis Thaliana.” <i>Journal of Cell Science</i>. The Company of Biologists, 2024. <a href=\"https://doi.org/10.1242/jcs.261720\">https://doi.org/10.1242/jcs.261720</a>.","short":"N. Gnyliukh, A.J. Johnson, M. Nagel, A. Monzer, D. Babic, A. Hlavata, S. Alotaibi, E. Isono, M. Loose, J. Friml, Journal of Cell Science 137 (2024).","ama":"Gnyliukh N, Johnson AJ, Nagel M, et al. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. <i>Journal of Cell Science</i>. 2024;137(8). doi:<a href=\"https://doi.org/10.1242/jcs.261720\">10.1242/jcs.261720</a>","ista":"Gnyliukh N, Johnson AJ, Nagel M, Monzer A, Babic D, Hlavata A, Alotaibi S, Isono E, Loose M, Friml J. 2024. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal of Cell Science. 137(8), jcs. 261720.","mla":"Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Arabidopsis Thaliana.” <i>Journal of Cell Science</i>, vol. 137, no. 8, jcs. 261720, The Company of Biologists, 2024, doi:<a href=\"https://doi.org/10.1242/jcs.261720\">10.1242/jcs.261720</a>.","apa":"Gnyliukh, N., Johnson, A. J., Nagel, M., Monzer, A., Babic, D., Hlavata, A., … Friml, J. (2024). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. <i>Journal of Cell Science</i>. The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.261720\">https://doi.org/10.1242/jcs.261720</a>"},"oa":1,"date_updated":"2025-09-04T13:49:45Z","article_type":"original","isi":1,"ddc":["570"],"_id":"15330","publisher":"The Company of Biologists","file_date_updated":"2025-01-09T08:41:16Z","doi":"10.1242/jcs.261720","OA_place":"publisher","fulldoi":"https://doi.org/10.1242/jcs.261720","has_accepted_license":"1","issue":"8","quality_controlled":"1","day":"01","abstract":[{"lang":"eng","text":"Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth and development by controlling plasma membrane protein composition and cargo uptake. CME relies on the precise recruitment of regulators for vesicle maturation and release. Homologues of components of mammalian vesicle scission are strong candidates to be part of the scission machinery in plants, but the precise roles of these proteins in this process are not fully understood. Here, we characterised the roles of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein 2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin, in the CME by combining high-resolution imaging of endocytic events in vivo and characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive similarly late during CME and physically interact, genetic analysis of the sh3p123 triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis. These observations imply that despite the presence of many well-conserved endocytic components, plants have acquired a distinct mechanism for CME."}],"acknowledgement":"Nataliia Gnyliukh was partially funded by the European Union’s Horizon 2020 research and\r\ninnovation program (2018-2020) under the Marie Sklodowska-Curie Grant (agreement no.\r\n665385). Taif University Researchers Supporting Project: TURSP-HC2022/02. and Austrian\r\nScience Fund (FWF): I 6123-B.We thank Prof. Eileen Lafer and Liping Wang for their suggestions regarding the optimisation of protein expression and purification. We thank Prof. Sebastian Y. Bednarek for the useful comments and constructive criticism of the project. We thank Maciek Adamowski for providing genetic material. This research was supported by the Scientific Service Units (SSU) of IST-Austria through resources provided by the Electron microscopy (EMF), Lab Support Facility (LSF) (particularly Dorota Jaworska) and the Bioimaging Facility (BIF).","article_processing_charge":"Yes (via OA deal)","OA_type":"hybrid","title":"Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana","intvolume":"       137","author":[{"last_name":"Gnyliukh","id":"390C1120-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-2198-0509","full_name":"Gnyliukh, Nataliia","first_name":"Nataliia"},{"first_name":"Alexander J","last_name":"Johnson","orcid":"0000-0002-2739-8843","id":"46A62C3A-F248-11E8-B48F-1D18A9856A87","full_name":"Johnson, Alexander J"},{"first_name":"MK","last_name":"Nagel","full_name":"Nagel, MK"},{"first_name":"Aline","full_name":"Monzer, Aline","id":"2DB5D88C-D7B3-11E9-B8FD-7907E6697425","last_name":"Monzer"},{"last_name":"Babic","id":"db566d23-f6e0-11ea-865d-e6f270e968e7","full_name":"Babic, David","first_name":"David"},{"first_name":"Annamaria","full_name":"Hlavata, Annamaria","id":"36062FEC-F248-11E8-B48F-1D18A9856A87","last_name":"Hlavata"},{"first_name":"SS","full_name":"Alotaibi, SS","last_name":"Alotaibi"},{"last_name":"Isono","full_name":"Isono, E","first_name":"E"},{"first_name":"Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin"},{"first_name":"Jiří","full_name":"Friml, Jiří","orcid":"0000-0002-8302-7596","last_name":"Friml","id":"4159519E-F248-11E8-B48F-1D18A9856A87"}],"publication_status":"published","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"Bio"}],"volume":137,"date_published":"2024-04-01T00:00:00Z","pmid":1,"status":"public","publication":"Journal of Cell Science","article_number":"jcs.261720","department":[{"_id":"MaLo"},{"_id":"JiFr"},{"_id":"CaBe"}],"ec_funded":1,"language":[{"iso":"eng"}],"related_material":{"record":[{"status":"public","id":"14591","relation":"earlier_version"}]}},{"has_accepted_license":"1","fulldoi":"https://doi.org/10.1038/s44318-024-00207-0","issue":"20","abstract":[{"lang":"eng","text":"Conserved signaling cascades monitor protein-folding homeostasis to ensure proper cellular function. One of the evolutionary conserved key players is IRE1, which maintains endoplasmic reticulum (ER) homeostasis through the unfolded protein response (UPR). Upon accumulation of misfolded proteins in the ER, IRE1 forms clusters on the ER membrane to initiate UPR signaling. What regulates IRE1 cluster formation is not fully understood. Here, we show that the ER lumenal domain (LD) of human IRE1α forms biomolecular condensates in vitro. IRE1α LD condensates were stabilized both by binding to unfolded polypeptides as well as by tethering to model membranes, suggesting their role in assembling IRE1α into signaling-competent stable clusters. Molecular dynamics simulations indicated that weak multivalent interactions drive IRE1α LD clustering. Mutagenesis experiments identified disordered regions in IRE1α LD to control its clustering in vitro and in cells. Importantly, dysregulated clustering of IRE1α mutants led to defects in IRE1α signaling. Our results revealed that disordered regions in IRE1α LD control its clustering and suggest their role as a common strategy in regulating protein assembly on membranes."}],"day":"15","quality_controlled":"1","_id":"18073","OA_place":"publisher","doi":"10.1038/s44318-024-00207-0","file_date_updated":"2025-01-13T08:43:20Z","publisher":"Embo Press","department":[{"_id":"MaLo"},{"_id":"JiFr"}],"publication":"EMBO Journal","page":"4668-4698","status":"public","language":[{"iso":"eng"}],"publication_status":"published","author":[{"full_name":"Kettel, Paulina","last_name":"Kettel","first_name":"Paulina"},{"last_name":"Marosits","full_name":"Marosits, Laura","first_name":"Laura"},{"first_name":"Elena","full_name":"Spinetti, Elena","last_name":"Spinetti"},{"last_name":"Rechberger","full_name":"Rechberger, Michael","first_name":"Michael"},{"id":"e3fdddd5-f6e0-11ea-865d-ca99ee6367f4","last_name":"Giannini","full_name":"Giannini, Caterina","first_name":"Caterina"},{"first_name":"Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 ","full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Niedermoser","full_name":"Niedermoser, Isabell","first_name":"Isabell"},{"first_name":"Irmgard","full_name":"Fischer, Irmgard","last_name":"Fischer"},{"full_name":"Versteeg, Gijs A.","last_name":"Versteeg","first_name":"Gijs A."},{"last_name":"Loose","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin"},{"full_name":"Covino, Roberto","last_name":"Covino","first_name":"Roberto"},{"full_name":"Karagöz, G. Elif","last_name":"Karagöz","first_name":"G. Elif"}],"title":"Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering","intvolume":"        43","OA_type":"gold","acknowledgement":"We thank late Thomas Peterbauer at the Max Perutz Labs Biooptics Light Microscopy Facility for his help and support. We are grateful to Kitti Csalyi and Thomas Sauer at Max Perutz Labs Biooptics FACS facility for their help. We thank Grzegorz Scibisz and Sertan Atilla for their support with the expression and purification of mCherry-IRE1α LD-10His. We are grateful to Aleksandra S Anisimova with her help in the generation of stable cell lines and the statistical analyses of the data. We thank Venja Vieweger for her help with the characterization of the WLLI and D123P IRE1 mutants in cells. We are thankful to Monika Kubickova for the help with the AUC experiments. We acknowledge CF BIC of CIISB, Instruct-CZ Centre, supported by MEYS CR (LM2023042)) and European Regional Development Fund-Project, UP CIISB“ (No. CZ.02.1.01/0.0/0.0/18_046/0015974). We thank the members of the Karagöz lab for the critical reading and editing of the manuscript. We are thankful to our colleagues Diego Acosta-Alvear, Vladislav Belyy, Jirka Peschek, Yasin Dagdas, Javier Martinez, Sascha Martens and Alwin Köhler for their invaluable input on the manuscript. We are grateful to Life Science Editors, especially Katrina Woolcock for her useful edits and comments on the manuscript. We acknowledge funding from Austrian Science Fund (FWF-SFB F79 and FWF-W 1261) to GEK. PK acknowledges the support of the Max Perutz PhD fellowship. GAV is funded by Stand-Alone grants (P30231-B, P30415-B, P36572), Special Research Grant (SFB grant F79), and Doctoral School grant (DK grant W1261) from the Austrian Science Fund (FWF). ES and RC acknowledge support and funding by the Frankfurt Institute of Advanced Studies, the LOEWE Center for Multiscale Modelling in Life Sciences of the state of Hesse, the Collaborative Research Center 1507 “Membrane-associated Protein Assemblies, Machineries, and Supercomplexes” (Project ID 450648163), and the International Max Planck Research School on Cellular Biophysics (to RC), the Center for Scientific Computing of the Goethe University and the Jülich Supercomputing Centre for computational resources and support.","article_processing_charge":"Yes","pmid":1,"volume":43,"date_published":"2024-10-15T00:00:00Z","year":"2024","type":"journal_article","publication_identifier":{"issn":["0261-4189"],"eissn":["1460-2075"]},"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"oa_version":"Published Version","month":"10","external_id":{"isi":["001306286100002"],"pmid":["39232130"]},"article_type":"original","isi":1,"date_updated":"2025-09-08T09:22:11Z","ddc":["570"],"file":[{"creator":"dernst","checksum":"04f4df1a561083f2846676442fc4eb3c","content_type":"application/pdf","file_size":10080854,"access_level":"open_access","date_created":"2025-01-13T08:43:20Z","success":1,"relation":"main_file","file_name":"2024_Embo_Kettel.pdf","file_id":"18827","date_updated":"2025-01-13T08:43:20Z"}],"date_created":"2024-09-15T22:01:42Z","oa":1,"citation":{"ieee":"P. Kettel <i>et al.</i>, “Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering,” <i>EMBO Journal</i>, vol. 43, no. 20. Embo Press, pp. 4668–4698, 2024.","chicago":"Kettel, Paulina, Laura Marosits, Elena Spinetti, Michael Rechberger, Caterina Giannini, Philipp Radler, Isabell Niedermoser, et al. “Disordered Regions in the IRE1α ER Lumenal Domain Mediate Its Stress-Induced Clustering.” <i>EMBO Journal</i>. Embo Press, 2024. <a href=\"https://doi.org/10.1038/s44318-024-00207-0\">https://doi.org/10.1038/s44318-024-00207-0</a>.","ama":"Kettel P, Marosits L, Spinetti E, et al. Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering. <i>EMBO Journal</i>. 2024;43(20):4668-4698. doi:<a href=\"https://doi.org/10.1038/s44318-024-00207-0\">10.1038/s44318-024-00207-0</a>","short":"P. Kettel, L. Marosits, E. Spinetti, M. Rechberger, C. Giannini, P. Radler, I. Niedermoser, I. Fischer, G.A. Versteeg, M. Loose, R. Covino, G.E. Karagöz, EMBO Journal 43 (2024) 4668–4698.","ista":"Kettel P, Marosits L, Spinetti E, Rechberger M, Giannini C, Radler P, Niedermoser I, Fischer I, Versteeg GA, Loose M, Covino R, Karagöz GE. 2024. Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering. EMBO Journal. 43(20), 4668–4698.","apa":"Kettel, P., Marosits, L., Spinetti, E., Rechberger, M., Giannini, C., Radler, P., … Karagöz, G. E. (2024). Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering. <i>EMBO Journal</i>. Embo Press. <a href=\"https://doi.org/10.1038/s44318-024-00207-0\">https://doi.org/10.1038/s44318-024-00207-0</a>","mla":"Kettel, Paulina, et al. “Disordered Regions in the IRE1α ER Lumenal Domain Mediate Its Stress-Induced Clustering.” <i>EMBO Journal</i>, vol. 43, no. 20, Embo Press, 2024, pp. 4668–98, doi:<a href=\"https://doi.org/10.1038/s44318-024-00207-0\">10.1038/s44318-024-00207-0</a>."}},{"researchdata_availability":"yes","dataavailabilitystatement":"The simulation data presented in this work are available from the University College London public data repository at https://doi.org/10.5522/04/24754527 (ref. 74). Live-cell imaging of FtsZ rings data presented in this work are from ref. 23. High-speed atomic force microscopy data presented in this work are from ref. 9. Total internal reflection fluorescence microscopy data presented in this work are from refs. 37,75,76","_id":"17460","publisher":"Springer Nature","file_date_updated":"2025-04-14T06:06:35Z","doi":"10.1038/s41567-024-02597-8","OA_place":"publisher","das_tickbox":"1","fulldoi":"https://doi.org/10.1038/s41567-024-02597-8","has_accepted_license":"1","supplementarymaterial":"yes","quality_controlled":"1","day":"01","abstract":[{"text":"Filaments in the cell commonly treadmill. Driven by energy consumption, they grow on one end while shrinking on the other, causing filaments to appear motile even though individual proteins remain static. This process is characteristic of cytoskeletal filaments and leads to collective filament self-organization. Here we show that treadmilling drives filament nematic ordering by dissolving misaligned filaments. Taking the bacterial FtsZ protein involved in cell division as an example, we show that this mechanism aligns FtsZ filaments in vitro and drives the organization of the division ring in living Bacillus subtilis cells. We find that ordering via local dissolution also allows the system to quickly respond to chemical and geometrical biases in the cell, enabling us to quantitatively explain the ring formation dynamics in vivo. Beyond FtsZ and other cytoskeletal filaments, our study identifies a mechanism for self-organization via constant birth and death of energy-consuming filaments.","lang":"eng"}],"acknowledgement":"We thank I. Palaia (ISTA) for useful discussions and K. Lim and R. W. Wong (WPI-Nano Life Science Institute, Kanazawa University) for providing access to HS-AFM. We would like to thank B. Prats Mateu (MSD Austria, Vienna) for providing the HS-AFM data. This work was supported by the Royal Society (grant no. UF160266; C.V.-C. and A.Š.), the European Union’s Horizon 2020 Research and Innovation Programme (grant no. 802960; A.Š.), the Austrian Science Fund (FWF) Stand-Alone P34607 (M.L.) and a Wellcome Trust and Royal Society Sir Henry Dale Fellowship (grant no. 206670/Z/17/Z; S.H. and K.D.W.).","article_processing_charge":"Yes (in subscription journal)","OA_type":"hybrid","intvolume":"        20","title":"Self-organization of mortal filaments and its role in bacterial division ring formation","author":[{"first_name":"Christian Eduardo","full_name":"Vanhille-Campos, Christian Eduardo","id":"3adeca52-9313-11ed-b1ac-c170b2505714","last_name":"Vanhille-Campos"},{"full_name":"Whitley, Kevin D.","last_name":"Whitley","first_name":"Kevin D."},{"first_name":"Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","last_name":"Radler","full_name":"Radler, Philipp"},{"first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose"},{"full_name":"Holden, Séamus","last_name":"Holden","first_name":"Séamus"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela"}],"publication_status":"published","date_published":"2024-10-01T00:00:00Z","volume":20,"popular_science":"1","pmid":1,"status":"public","page":"1670-1678","publication":"Nature Physics","department":[{"_id":"AnSa"},{"_id":"MaLo"}],"ec_funded":1,"language":[{"iso":"eng"}],"related_material":{"record":[{"id":"22988","relation":"research_data","status":"public"}]},"oa_version":"Published Version","scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"external_id":{"pmid":["39416851"],"isi":["001289394500005"]},"month":"10","year":"2024","project":[{"grant_number":"P34607","name":"In vitro reconstitution of bacterial cell division","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"},{"call_identifier":"H2020","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e"}],"APC_amount":"12348 EUR","publication_identifier":{"issn":["1745-2473"],"eissn":["1745-2481"]},"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","type":"journal_article","corr_author":"1","date_created":"2024-08-25T22:01:08Z","file":[{"file_name":"2024_NaturePhysics_VanhilleCampos.pdf","date_updated":"2025-04-14T06:06:35Z","file_id":"19556","relation":"main_file","content_type":"application/pdf","file_size":8058249,"access_level":"open_access","date_created":"2025-04-14T06:06:35Z","success":1,"creator":"dernst","checksum":"c4842152e2b90d67f48ea8c9ed7c473b"}],"citation":{"short":"C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić, Nature Physics 20 (2024) 1670–1678.","ama":"Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. Self-organization of mortal filaments and its role in bacterial division ring formation. <i>Nature Physics</i>. 2024;20:1670-1678. doi:<a href=\"https://doi.org/10.1038/s41567-024-02597-8\">10.1038/s41567-024-02597-8</a>","mla":"Vanhille-Campos, Christian Eduardo, et al. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” <i>Nature Physics</i>, vol. 20, Springer Nature, 2024, pp. 1670–78, doi:<a href=\"https://doi.org/10.1038/s41567-024-02597-8\">10.1038/s41567-024-02597-8</a>.","apa":"Vanhille-Campos, C. E., Whitley, K. D., Radler, P., Loose, M., Holden, S., &#38; Šarić, A. (2024). Self-organization of mortal filaments and its role in bacterial division ring formation. <i>Nature Physics</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41567-024-02597-8\">https://doi.org/10.1038/s41567-024-02597-8</a>","ista":"Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. 2024. Self-organization of mortal filaments and its role in bacterial division ring formation. Nature Physics. 20, 1670–1678.","ieee":"C. E. Vanhille-Campos, K. D. Whitley, P. Radler, M. Loose, S. Holden, and A. Šarić, “Self-organization of mortal filaments and its role in bacterial division ring formation,” <i>Nature Physics</i>, vol. 20. Springer Nature, pp. 1670–1678, 2024.","chicago":"Vanhille-Campos, Christian Eduardo, Kevin D. Whitley, Philipp Radler, Martin Loose, Séamus Holden, and Anđela Šarić. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” <i>Nature Physics</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41567-024-02597-8\">https://doi.org/10.1038/s41567-024-02597-8</a>."},"oa":1,"date_updated":"2026-09-24T10:58:39Z","article_type":"original","isi":1,"ddc":["570"]},{"pmid":1,"volume":597,"date_published":"2023-03-01T00:00:00Z","author":[{"first_name":"Martin","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","orcid":"0000-0001-7309-9724"},{"first_name":"Albert","last_name":"Auer","orcid":"0000-0002-3580-2906","id":"3018E8C2-F248-11E8-B48F-1D18A9856A87","full_name":"Auer, Albert"},{"id":"D96FFDA0-A884-11E9-9968-DC26E6697425","last_name":"Brognara","full_name":"Brognara, Gabriel","first_name":"Gabriel"},{"first_name":"Hanifatul R","id":"55380f95-15b2-11ec-abd3-aff8e230696b","full_name":"Budiman, Hanifatul R","last_name":"Budiman"},{"full_name":"Kowalski, Lukasz M","last_name":"Kowalski","id":"e3a512e2-4bbe-11eb-a68a-e3857a7844c2","first_name":"Lukasz M"},{"first_name":"Ivana","id":"83c17ce3-15b2-11ec-abd3-f486545870bd","last_name":"Matijevic","full_name":"Matijevic, Ivana"}],"publication_status":"published","title":"In vitro reconstitution of small GTPase regulation","intvolume":"       597","acknowledgement":"The authors acknowledge support from IST Austria and helpful comments from the anonymous reviewers that helped to improve this manuscript. We apologize to the authors of primary literature and outstanding research not cited here due to space restraints.","article_processing_charge":"Yes (via OA deal)","language":[{"iso":"eng"}],"department":[{"_id":"MaLo"}],"publication":"FEBS Letters","status":"public","page":"762-777","file_date_updated":"2023-08-16T08:31:04Z","doi":"10.1002/1873-3468.14540","publisher":"Wiley","_id":"12163","keyword":["Cell Biology","Genetics","Molecular Biology","Biochemistry","Structural Biology","Biophysics"],"abstract":[{"lang":"eng","text":"Small GTPases play essential roles in the organization of eukaryotic cells. In recent years, it has become clear that their intracellular functions result from intricate biochemical networks of the GTPase and their regulators that dynamically bind to a membrane surface. Due to the inherent complexities of their interactions, however, revealing the underlying mechanisms of action is often difficult to achieve from in vivo studies. This review summarizes in vitro reconstitution approaches developed to obtain a better mechanistic understanding of how small GTPase activities are regulated in space and time."}],"day":"01","quality_controlled":"1","issue":"6","fulldoi":"https://doi.org/10.1002/1873-3468.14540","has_accepted_license":"1","oa":1,"citation":{"ieee":"M. Loose, A. Auer, G. Brognara, H. R. Budiman, L. M. Kowalski, and I. Matijevic, “In vitro reconstitution of small GTPase regulation,” <i>FEBS Letters</i>, vol. 597, no. 6. Wiley, pp. 762–777, 2023.","chicago":"Loose, Martin, Albert Auer, Gabriel Brognara, Hanifatul R Budiman, Lukasz M Kowalski, and Ivana Matijevic. “In Vitro Reconstitution of Small GTPase Regulation.” <i>FEBS Letters</i>. Wiley, 2023. <a href=\"https://doi.org/10.1002/1873-3468.14540\">https://doi.org/10.1002/1873-3468.14540</a>.","ama":"Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. In vitro reconstitution of small GTPase regulation. <i>FEBS Letters</i>. 2023;597(6):762-777. doi:<a href=\"https://doi.org/10.1002/1873-3468.14540\">10.1002/1873-3468.14540</a>","short":"M. Loose, A. Auer, G. Brognara, H.R. Budiman, L.M. Kowalski, I. Matijevic, FEBS Letters 597 (2023) 762–777.","ista":"Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. 2023. In vitro reconstitution of small GTPase regulation. FEBS Letters. 597(6), 762–777.","mla":"Loose, Martin, et al. “In Vitro Reconstitution of Small GTPase Regulation.” <i>FEBS Letters</i>, vol. 597, no. 6, Wiley, 2023, pp. 762–77, doi:<a href=\"https://doi.org/10.1002/1873-3468.14540\">10.1002/1873-3468.14540</a>.","apa":"Loose, M., Auer, A., Brognara, G., Budiman, H. R., Kowalski, L. M., &#38; Matijevic, I. (2023). In vitro reconstitution of small GTPase regulation. <i>FEBS Letters</i>. Wiley. <a href=\"https://doi.org/10.1002/1873-3468.14540\">https://doi.org/10.1002/1873-3468.14540</a>"},"file":[{"date_updated":"2023-08-16T08:31:04Z","file_id":"14063","file_name":"2023_FEBSLetters_Loose.pdf","relation":"main_file","date_created":"2023-08-16T08:31:04Z","success":1,"content_type":"application/pdf","file_size":3148143,"access_level":"open_access","checksum":"7492244d3f9c5faa1347ef03f6e5bc84","creator":"dernst"}],"date_created":"2023-01-12T12:09:58Z","ddc":["570"],"article_type":"review","isi":1,"date_updated":"2024-10-09T21:03:42Z","month":"03","external_id":{"pmid":["36448231"],"isi":["000891573000001"]},"tmp":{"image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)"},"scopus_import":"1","oa_version":"Published Version","type":"journal_article","corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["0014-5793"],"eissn":["1873-3468"]},"year":"2023"},{"oa":1,"citation":{"chicago":"Leonard, Thomas A., Martin Loose, and Sascha Martens. “The Membrane Surface as a Platform That Organizes Cellular and Biochemical Processes.” <i>Developmental Cell</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.devcel.2023.06.001\">https://doi.org/10.1016/j.devcel.2023.06.001</a>.","ieee":"T. A. Leonard, M. Loose, and S. Martens, “The membrane surface as a platform that organizes cellular and biochemical processes,” <i>Developmental Cell</i>, vol. 58, no. 15. Elsevier, pp. 1315–1332, 2023.","ista":"Leonard TA, Loose M, Martens S. 2023. The membrane surface as a platform that organizes cellular and biochemical processes. Developmental Cell. 58(15), 1315–1332.","apa":"Leonard, T. A., Loose, M., &#38; Martens, S. (2023). The membrane surface as a platform that organizes cellular and biochemical processes. <i>Developmental Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.devcel.2023.06.001\">https://doi.org/10.1016/j.devcel.2023.06.001</a>","mla":"Leonard, Thomas A., et al. “The Membrane Surface as a Platform That Organizes Cellular and Biochemical Processes.” <i>Developmental Cell</i>, vol. 58, no. 15, Elsevier, 2023, pp. 1315–32, doi:<a href=\"https://doi.org/10.1016/j.devcel.2023.06.001\">10.1016/j.devcel.2023.06.001</a>.","short":"T.A. Leonard, M. Loose, S. Martens, Developmental Cell 58 (2023) 1315–1332.","ama":"Leonard TA, Loose M, Martens S. The membrane surface as a platform that organizes cellular and biochemical processes. <i>Developmental Cell</i>. 2023;58(15):1315-1332. doi:<a href=\"https://doi.org/10.1016/j.devcel.2023.06.001\">10.1016/j.devcel.2023.06.001</a>"},"date_created":"2023-08-13T22:01:12Z","file":[{"access_level":"open_access","content_type":"application/pdf","file_size":3184217,"success":1,"date_created":"2023-08-14T07:57:55Z","creator":"dernst","checksum":"d8c5dc97cd40c26da2ec98ae723ab368","file_name":"2023_DevelopmentalCell_Leonard.pdf","file_id":"14049","date_updated":"2023-08-14T07:57:55Z","relation":"main_file"}],"ddc":["570"],"article_type":"original","isi":1,"date_updated":"2024-10-22T11:40:18Z","month":"08","external_id":{"isi":["001059110400001"],"pmid":["37419118"]},"scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"oa_version":"Published Version","type":"journal_article","corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["1534-5807"],"eissn":["1878-1551"]},"year":"2023","project":[{"_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607","name":"In vitro reconstitution of bacterial cell division"},{"_id":"bd6ae2ca-d553-11ed-ba76-a4aa239da5ee","name":"Synthetic and structural biology of Rab GTPase networks","grant_number":"101045340"}],"volume":58,"pmid":1,"date_published":"2023-08-07T00:00:00Z","publication_status":"published","author":[{"last_name":"Leonard","full_name":"Leonard, Thomas A.","first_name":"Thomas A."},{"orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose","first_name":"Martin"},{"first_name":"Sascha","full_name":"Martens, Sascha","last_name":"Martens"}],"intvolume":"        58","title":"The membrane surface as a platform that organizes cellular and biochemical processes","article_processing_charge":"Yes (via OA deal)","acknowledgement":"We acknowledge funding from the Austrian Science Fund (FWF F79, P32814-B, and P35061-B to S.M.; P34607-B to M.L.; and P30584-B and P33066-B to T.A.L.) and the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement no. 101045340 to M.L.). We are grateful for comments on the manuscript by Justyna Sawa-Makarska, Verena Baumann, Marko Kojic, Philipp Radler, Ronja Reinhardt, and Sumire Antonioli.","language":[{"iso":"eng"}],"department":[{"_id":"MaLo"}],"publication":"Developmental Cell","status":"public","page":"1315-1332","file_date_updated":"2023-08-14T07:57:55Z","doi":"10.1016/j.devcel.2023.06.001","publisher":"Elsevier","_id":"14039","abstract":[{"text":"Membranes are essential for life. They act as semi-permeable boundaries that define cells and organelles. In addition, their surfaces actively participate in biochemical reaction networks, where they confine proteins, align reaction partners, and directly control enzymatic activities. Membrane-localized reactions shape cellular membranes, define the identity of organelles, compartmentalize biochemical processes, and can even be the source of signaling gradients that originate at the plasma membrane and reach into the cytoplasm and nucleus. The membrane surface is, therefore, an essential platform upon which myriad cellular processes are scaffolded. In this review, we summarize our current understanding of the biophysics and biochemistry of membrane-localized reactions with particular focus on insights derived from reconstituted and cellular systems. We discuss how the interplay of cellular factors results in their self-organization, condensation, assembly, and activity, and the emergent properties derived from them.","lang":"eng"}],"day":"07","quality_controlled":"1","issue":"15","fulldoi":"https://doi.org/10.1016/j.devcel.2023.06.001","has_accepted_license":"1"},{"project":[{"call_identifier":"H2020","name":"Self-Organization of the Bacterial Cell","grant_number":"679239","_id":"2595697A-B435-11E9-9278-68D0E5697425"},{"_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607"},{"_id":"34d75525-11ca-11ed-8bc3-89b6307fee9d","grant_number":"26360","name":"Motile active matter models of migrating cells and chiral filaments"}],"year":"2023","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"research_data","corr_author":"1","oa_version":"Published Version","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License 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Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of Flexible Active Filaments.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/AT:ISTA:13116\">https://doi.org/10.15479/AT:ISTA:13116</a>.","ieee":"Z. Dunajova <i>et al.</i>, “Chiral and nematic phases of flexible active filaments.” Institute of Science and Technology Austria, 2023.","apa":"Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P., … Loose, M. (2023). Chiral and nematic phases of flexible active filaments. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:13116\">https://doi.org/10.15479/AT:ISTA:13116</a>","mla":"Dunajova, Zuzana, et al. <i>Chiral and Nematic Phases of Flexible Active Filaments</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:13116\">10.15479/AT:ISTA:13116</a>.","ista":"Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG, Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible active filaments, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:13116\">10.15479/AT:ISTA:13116</a>.","short":"Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G. Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, (2023).","ama":"Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible active filaments. 2023. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:13116\">10.15479/AT:ISTA:13116</a>"},"oa":1,"fulldoi":"https://doi.org/10.15479/AT:ISTA:13116","has_accepted_license":"1","day":"26","abstract":[{"lang":"eng","text":"The emergence of large-scale order in self-organized systems relies on local interactions between individual components. During bacterial cell division, FtsZ -- a prokaryotic homologue of the eukaryotic protein tubulin -- polymerizes into treadmilling filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments can form dynamic chiral assemblies. However, how the active and passive properties of individual filaments relate to these large-scale self-organized structures remains poorly understood. Here, we connect single filament properties with the mesoscopic scale by combining minimal active matter simulations and biochemical reconstitution experiments. We show that density and flexibility of active chiral filaments define their global order. At intermediate densities, curved, flexible filaments organize into chiral rings and polar bands. An effectively nematic organization dominates for high densities and for straight, mutant filaments with increased rigidity. Our predicted phase diagram captures these features quantitatively, demonstrating how the flexibility, density and chirality of active filaments affect their collective behaviour. Our findings shed light on the fundamental properties of active chiral matter and explain how treadmilling FtsZ filaments organize during bacterial cell division. "}],"_id":"13116","publisher":"Institute of Science and Technology Austria","doi":"10.15479/AT:ISTA:13116","file_date_updated":"2023-08-08T11:17:28Z","status":"public","department":[{"_id":"MaLo"},{"_id":"EdHa"},{"_id":"JoDa"}],"ec_funded":1,"related_material":{"record":[{"relation":"used_in_publication","id":"13314","status":"public"},{"id":"21423","relation":"used_in_publication","status":"public"}]},"article_processing_charge":"No","acknowledgement":"This work was supported by the European Research Council through grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L., B. P.M.  was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM collaborative research program. Z.D. has received funding from Doctoral Programme of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria), Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments on the manuscript. We are also thankful for the support by the Scientific Service Units (SSU) of IST Austria through resources provided by the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF). ","title":"Chiral and nematic phases of flexible active filaments","author":[{"first_name":"Zuzana","full_name":"Dunajova, Zuzana","id":"4B39F286-F248-11E8-B48F-1D18A9856A87","last_name":"Dunajova"},{"first_name":"Batirtze","full_name":"Prats Mateu, Batirtze","last_name":"Prats Mateu","id":"299FE892-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Radler, Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","last_name":"Radler","first_name":"Philipp"},{"last_name":"Lim","full_name":"Lim, Keesiang","first_name":"Keesiang"},{"first_name":"Dörte","last_name":"Brandis","full_name":"Brandis, Dörte"},{"last_name":"Velicky","orcid":"0000-0002-2340-7431","full_name":"Velicky, Philipp","id":"39BDC62C-F248-11E8-B48F-1D18A9856A87","first_name":"Philipp"},{"first_name":"Johann G","last_name":"Danzl","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","full_name":"Danzl, Johann G","orcid":"0000-0001-8559-3973"},{"first_name":"Richard W.","full_name":"Wong, Richard W.","last_name":"Wong"},{"first_name":"Jens","last_name":"Elgeti","full_name":"Elgeti, Jens"},{"id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6005-1561","last_name":"Hannezo","full_name":"Hannezo, Edouard B","first_name":"Edouard B"},{"first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"date_published":"2023-07-26T00:00:00Z"},{"_id":"13314","file_date_updated":"2024-01-30T14:28:30Z","doi":"10.1038/s41567-023-02218-w","publisher":"Springer Nature","has_accepted_license":"1","fulldoi":"https://doi.org/10.1038/s41567-023-02218-w","quality_controlled":"1","abstract":[{"lang":"eng","text":"The emergence of large-scale order in self-organized systems relies on local interactions between individual components. During bacterial cell division, FtsZ—a prokaryotic homologue of the eukaryotic protein tubulin—polymerizes into treadmilling filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments can form dynamic chiral assemblies. However, how the active and passive properties of individual filaments relate to these large-scale self-organized structures remains poorly understood. Here we connect single-filament properties with the mesoscopic scale by combining minimal active matter simulations and biochemical reconstitution experiments. We show that the density and flexibility of active chiral filaments define their global order. At intermediate densities, curved, flexible filaments organize into chiral rings and polar bands. An effectively nematic organization dominates for high densities and for straight, mutant filaments with increased rigidity. Our predicted phase diagram quantitatively captures these features, demonstrating how the flexibility, density and chirality of the active filaments affect their collective behaviour. Our findings shed light on the fundamental properties of active chiral matter and explain how treadmilling FtsZ filaments organize during bacterial cell division."}],"day":"01","title":"Chiral and nematic phases of flexible active filaments","intvolume":"        19","acknowledgement":"This work was supported by the European Research Council through grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM collaborative research program. Z.D. has received funding from Doctoral Programme of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria), Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments on the manuscript. We are also thankful for the support by the Scientific Service Units (SSU) of IST Austria through resources provided by the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF).","article_processing_charge":"Yes (in subscription journal)","author":[{"full_name":"Dunajova, Zuzana","id":"4B39F286-F248-11E8-B48F-1D18A9856A87","last_name":"Dunajova","first_name":"Zuzana"},{"first_name":"Batirtze","full_name":"Prats Mateu, Batirtze","id":"299FE892-F248-11E8-B48F-1D18A9856A87","last_name":"Prats Mateu"},{"first_name":"Philipp","full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","last_name":"Radler","orcid":"0000-0001-9198-2182 "},{"first_name":"Keesiang","last_name":"Lim","full_name":"Lim, Keesiang"},{"last_name":"Brandis","id":"21d64d35-f128-11eb-9611-b8bcca7a12fd","full_name":"Brandis, Dörte","first_name":"Dörte"},{"first_name":"Philipp","orcid":"0000-0002-2340-7431","full_name":"Velicky, Philipp","id":"39BDC62C-F248-11E8-B48F-1D18A9856A87","last_name":"Velicky"},{"first_name":"Johann G","orcid":"0000-0001-8559-3973","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","last_name":"Danzl","full_name":"Danzl, Johann G"},{"last_name":"Wong","full_name":"Wong, Richard W.","first_name":"Richard W."},{"last_name":"Elgeti","full_name":"Elgeti, Jens","first_name":"Jens"},{"first_name":"Edouard B","last_name":"Hannezo","id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","full_name":"Hannezo, Edouard B","orcid":"0000-0001-6005-1561"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}],"publication_status":"published","acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"volume":19,"date_published":"2023-12-01T00:00:00Z","pmid":1,"publication":"Nature Physics","status":"public","page":"1916-1926","ec_funded":1,"department":[{"_id":"JoDa"},{"_id":"EdHa"},{"_id":"MaLo"},{"_id":"GradSch"}],"related_material":{"record":[{"status":"public","id":"13116","relation":"research_data"},{"status":"public","relation":"research_data","id":"21439"},{"status":"public","id":"21423","relation":"dissertation_contains"}]},"language":[{"iso":"eng"}],"tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"scopus_import":"1","oa_version":"Published Version","external_id":{"isi":["001178645300041"],"pmid":["38075437"]},"month":"12","project":[{"call_identifier":"H2020","name":"Self-Organization of the Bacterial Cell","grant_number":"679239","_id":"2595697A-B435-11E9-9278-68D0E5697425"},{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"},{"name":"Motile active matter models of migrating cells and chiral filaments","grant_number":"26360","_id":"34d75525-11ca-11ed-8bc3-89b6307fee9d"}],"year":"2023","publication_identifier":{"issn":["1745-2473"],"eissn":["1745-2481"]},"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","type":"journal_article","corr_author":"1","file":[{"file_name":"2023_NaturePhysics_Dunajova.pdf","file_id":"14916","date_updated":"2024-01-30T14:28:30Z","relation":"main_file","access_level":"open_access","content_type":"application/pdf","file_size":22471673,"success":1,"date_created":"2024-01-30T14:28:30Z","creator":"dernst","checksum":"bc7673ca07d37309013a86166577b2f7"}],"date_created":"2023-07-27T14:44:45Z","oa":1,"citation":{"short":"Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G. Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, Nature Physics 19 (2023) 1916–1926.","ama":"Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible active filaments. <i>Nature Physics</i>. 2023;19:1916-1926. doi:<a href=\"https://doi.org/10.1038/s41567-023-02218-w\">10.1038/s41567-023-02218-w</a>","apa":"Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P., … Loose, M. (2023). Chiral and nematic phases of flexible active filaments. <i>Nature Physics</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41567-023-02218-w\">https://doi.org/10.1038/s41567-023-02218-w</a>","mla":"Dunajova, Zuzana, et al. “Chiral and Nematic Phases of Flexible Active Filaments.” <i>Nature Physics</i>, vol. 19, Springer Nature, 2023, pp. 1916–26, doi:<a href=\"https://doi.org/10.1038/s41567-023-02218-w\">10.1038/s41567-023-02218-w</a>.","ista":"Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG, Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible active filaments. Nature Physics. 19, 1916–1926.","ieee":"Z. Dunajova <i>et al.</i>, “Chiral and nematic phases of flexible active filaments,” <i>Nature Physics</i>, vol. 19. Springer Nature, pp. 1916–1926, 2023.","chicago":"Dunajova, Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of Flexible Active Filaments.” <i>Nature Physics</i>. Springer Nature, 2023. <a href=\"https://doi.org/10.1038/s41567-023-02218-w\">https://doi.org/10.1038/s41567-023-02218-w</a>."},"date_updated":"2026-09-28T22:30:10Z","isi":1,"article_type":"original","ddc":["530"]},{"oa_version":"Preprint","_id":"14591","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/2023.10.09.561523"}],"OA_place":"repository","month":"10","doi":"10.1101/2023.10.09.561523","fulldoi":"https://doi.org/10.1101/2023.10.09.561523","year":"2023","project":[{"call_identifier":"H2020","grant_number":"665385","name":"International IST Doctoral Program","_id":"2564DBCA-B435-11E9-9278-68D0E5697425"}],"day":"10","abstract":[{"text":"Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth and development by controlling plasma membrane protein composition and cargo uptake. CME relies on the precise recruitment of regulators for vesicle maturation and release. Homologues of components of mammalian vesicle scission are strong candidates to be part of the scissin machinery in plants, but the precise roles of these proteins in this process is not fully understood. Here, we characterised the roles of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein 2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin, in the CME by combining high-resolution imaging of endocytic events in vivo and characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive similarly late during CME and physically interact, genetic analysis of the Dsh3p1,2,3 triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis. These observations imply that despite the presence of many well-conserved endocytic components, plants have acquired a distinct mechanism for CME. One Sentence Summary In contrast to predictions based on mammalian systems, plant Dynamin-related proteins 2 are recruited to the site of Clathrin-mediated endocytosis independently of BAR-SH3 proteins.","lang":"eng"}],"type":"preprint","corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"draft","author":[{"orcid":"0000-0002-2198-0509","id":"390C1120-F248-11E8-B48F-1D18A9856A87","last_name":"Gnyliukh","full_name":"Gnyliukh, Nataliia","first_name":"Nataliia"},{"first_name":"Alexander J","id":"46A62C3A-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-2739-8843","full_name":"Johnson, Alexander J","last_name":"Johnson"},{"full_name":"Nagel, Marie-Kristin","last_name":"Nagel","first_name":"Marie-Kristin"},{"first_name":"Aline","last_name":"Monzer","id":"2DB5D88C-D7B3-11E9-B8FD-7907E6697425","full_name":"Monzer, Aline"},{"id":"36062FEC-F248-11E8-B48F-1D18A9856A87","last_name":"Hlavata","full_name":"Hlavata, Annamaria","first_name":"Annamaria"},{"first_name":"Erika","full_name":"Isono, Erika","last_name":"Isono"},{"first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","full_name":"Loose, Martin"},{"first_name":"Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8302-7596","last_name":"Friml","full_name":"Friml, Jiří"}],"article_processing_charge":"No","title":"Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in plants","date_created":"2023-11-22T10:17:49Z","citation":{"apa":"Gnyliukh, N., Johnson, A. J., Nagel, M.-K., Monzer, A., Hlavata, A., Isono, E., … Friml, J. (n.d.). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in plants. <i>bioRxiv</i>. <a href=\"https://doi.org/10.1101/2023.10.09.561523\">https://doi.org/10.1101/2023.10.09.561523</a>","mla":"Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” <i>BioRxiv</i>, doi:<a href=\"https://doi.org/10.1101/2023.10.09.561523\">10.1101/2023.10.09.561523</a>.","ista":"Gnyliukh N, Johnson AJ, Nagel M-K, Monzer A, Hlavata A, Isono E, Loose M, Friml J. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in plants. bioRxiv, <a href=\"https://doi.org/10.1101/2023.10.09.561523\">10.1101/2023.10.09.561523</a>.","ama":"Gnyliukh N, Johnson AJ, Nagel M-K, et al. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in plants. <i>bioRxiv</i>. doi:<a href=\"https://doi.org/10.1101/2023.10.09.561523\">10.1101/2023.10.09.561523</a>","short":"N. Gnyliukh, A.J. Johnson, M.-K. Nagel, A. Monzer, A. Hlavata, E. Isono, M. Loose, J. Friml, BioRxiv (n.d.).","chicago":"Gnyliukh, Nataliia, Alexander J Johnson, Marie-Kristin Nagel, Aline Monzer, Annamaria Hlavata, Erika Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” <i>BioRxiv</i>, n.d. <a href=\"https://doi.org/10.1101/2023.10.09.561523\">https://doi.org/10.1101/2023.10.09.561523</a>.","ieee":"N. Gnyliukh <i>et al.</i>, “Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in plants,” <i>bioRxiv</i>. ."},"oa":1,"date_published":"2023-10-10T00:00:00Z","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"Bio"}],"department":[{"_id":"JiFr"},{"_id":"MaLo"},{"_id":"CaBe"}],"ec_funded":1,"date_updated":"2026-09-28T22:30:51Z","status":"public","publication":"bioRxiv","language":[{"iso":"eng"}],"related_material":{"record":[{"relation":"later_version","id":"15330","status":"public"},{"status":"public","relation":"dissertation_contains","id":"14510"}]}},{"quality_controlled":"1","day":"19","abstract":[{"lang":"eng","text":"Martin Loose studied chemistry at the University of Heidelberg, Germany. He then joined Petra Schwille's group at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden, where he obtained his PhD degree in 2010 for work on self-organization and pattern formation in the bacterial Min protein system. He then moved to Tim Mitchison's lab at Harvard Medical School, Boston, USA for his postdoc, funded by Human Frontier Science Program (HSFP) and European Molecular Biology Organization (EMBO) long-term fellowships; there, he discovered that the bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Martin established his independent research group at the Institute of Science and Technology (IST) Austria in 2015, supported by an European Research Council (ERC) starting grant and HFSP Young Investigator Grant. His lab studies the self-organization of bacterial cell division and small GTPase networks."}],"fulldoi":"https://doi.org/10.1242/jcs.259715","issue":"2","publisher":"The Company of Biologists","doi":"10.1242/jcs.259715","_id":"17057","language":[{"iso":"eng"}],"status":"public","publication":"Journal of Cell Science","article_number":"jcs259715","department":[{"_id":"MaLo"}],"date_published":"2022-01-19T00:00:00Z","volume":135,"article_processing_charge":"No","intvolume":"       135","title":"Cell scientist to watch – Martin Loose","author":[{"first_name":"Martin","full_name":"Loose, Martin","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724"}],"publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"type":"other_academic_publication","year":"2022","external_id":{"isi":["000762665200015"]},"month":"01","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1242/jcs.259715"}],"oa_version":"Published Version","ddc":["570"],"date_updated":"2026-06-18T17:51:26Z","isi":1,"citation":{"chicago":"Loose, Martin. <i>Cell Scientist to Watch – Martin Loose</i>. <i>Journal of Cell Science</i>. Vol. 135. The Company of Biologists, 2022. <a href=\"https://doi.org/10.1242/jcs.259715\">https://doi.org/10.1242/jcs.259715</a>.","ieee":"M. Loose, <i>Cell scientist to watch – Martin Loose</i>, vol. 135, no. 2. The Company of Biologists, 2022.","ista":"Loose M. 2022. Cell scientist to watch – Martin Loose, The Company of Biologists,p.","apa":"Loose, M. (2022). <i>Cell scientist to watch – Martin Loose</i>. <i>Journal of Cell Science</i> (Vol. 135). The Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.259715\">https://doi.org/10.1242/jcs.259715</a>","mla":"Loose, Martin. “Cell Scientist to Watch – Martin Loose.” <i>Journal of Cell Science</i>, vol. 135, no. 2, jcs259715, The Company of Biologists, 2022, doi:<a href=\"https://doi.org/10.1242/jcs.259715\">10.1242/jcs.259715</a>.","short":"M. Loose, Cell Scientist to Watch – Martin Loose, The Company of Biologists, 2022.","ama":"Loose M. <i>Cell Scientist to Watch – Martin Loose</i>. Vol 135. The Company of Biologists; 2022. doi:<a href=\"https://doi.org/10.1242/jcs.259715\">10.1242/jcs.259715</a>"},"oa":1,"date_created":"2024-05-28T13:28:30Z"},{"oa":1,"citation":{"chicago":"Radler, Philipp, Natalia S. Baranova, Paulo R Dos Santos Caldas, Christoph M Sommer, Maria D Lopez Pelegrin, David Michalik, and Martin Loose. “In Vitro Reconstitution of Escherichia Coli Divisome Activation.” <i>Nature Communications</i>. Springer Nature, 2022. <a href=\"https://doi.org/10.1038/s41467-022-30301-y\">https://doi.org/10.1038/s41467-022-30301-y</a>.","ieee":"P. Radler <i>et al.</i>, “In vitro reconstitution of Escherichia coli divisome activation,” <i>Nature Communications</i>, vol. 13. Springer Nature, 2022.","ista":"Radler P, Baranova NS, Dos Santos Caldas PR, Sommer CM, Lopez Pelegrin MD, Michalik D, Loose M. 2022. In vitro reconstitution of Escherichia coli divisome activation. Nature Communications. 13, 2635.","apa":"Radler, P., Baranova, N. S., Dos Santos Caldas, P. R., Sommer, C. M., Lopez Pelegrin, M. D., Michalik, D., &#38; Loose, M. (2022). In vitro reconstitution of Escherichia coli divisome activation. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-022-30301-y\">https://doi.org/10.1038/s41467-022-30301-y</a>","mla":"Radler, Philipp, et al. “In Vitro Reconstitution of Escherichia Coli Divisome Activation.” <i>Nature Communications</i>, vol. 13, 2635, Springer Nature, 2022, doi:<a href=\"https://doi.org/10.1038/s41467-022-30301-y\">10.1038/s41467-022-30301-y</a>.","ama":"Radler P, Baranova NS, Dos Santos Caldas PR, et al. In vitro reconstitution of Escherichia coli divisome activation. <i>Nature Communications</i>. 2022;13. doi:<a href=\"https://doi.org/10.1038/s41467-022-30301-y\">10.1038/s41467-022-30301-y</a>","short":"P. Radler, N.S. Baranova, P.R. Dos Santos Caldas, C.M. Sommer, M.D. Lopez Pelegrin, D. Michalik, M. Loose, Nature Communications 13 (2022)."},"file":[{"checksum":"5af863ee1b95a0710f6ee864d68dc7a6","creator":"dernst","date_created":"2022-05-13T09:10:51Z","success":1,"file_size":6945191,"content_type":"application/pdf","access_level":"open_access","relation":"main_file","file_id":"11374","date_updated":"2022-05-13T09:10:51Z","file_name":"2022_NatureCommunications_Radler.pdf"}],"date_created":"2022-05-13T09:06:28Z","ddc":["570"],"date_updated":"2026-09-28T22:30:07Z","isi":1,"article_type":"original","external_id":{"isi":["000795171100037"]},"month":"05","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"scopus_import":"1","oa_version":"Published Version","publication_identifier":{"issn":["2041-1723"]},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","corr_author":"1","type":"journal_article","year":"2022","project":[{"_id":"2595697A-B435-11E9-9278-68D0E5697425","name":"Self-Organization of the Bacterial Cell","grant_number":"679239","call_identifier":"H2020"},{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"date_published":"2022-05-12T00:00:00Z","volume":13,"intvolume":"        13","title":"In vitro reconstitution of Escherichia coli divisome activation","acknowledgement":"We acknowledge members of the Loose laboratory at IST Austria for helpful discussions—in particular L. Lindorfer for his assistance with cloning and purifications. We thank J. Löwe and T. Nierhaus (MRC-LMB Cambridge, UK) for sharing unpublished work and helpful discussions, as well as D. Vavylonis and D. Rutkowski (Lehigh University, Bethlehem, PA, USA) and S. Martin (University of Lausanne, Switzerland) for sharing their code for FRAP analysis. We are also thankful for the support by the Scientific Service Units (SSU) of IST Austria through resources provided by the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF). This work was supported by the European Research Council through grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L. and HFSP LT 000824/2016-L4 to N.B. For the purpose of open access, we have applied a CC BY public copyright licence to any Author Accepted Manuscript version arising from this submission.","article_processing_charge":"No","author":[{"last_name":"Radler","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","full_name":"Radler, Philipp","first_name":"Philipp"},{"first_name":"Natalia S.","full_name":"Baranova, Natalia S.","orcid":"0000-0002-3086-9124","id":"38661662-F248-11E8-B48F-1D18A9856A87","last_name":"Baranova"},{"last_name":"Dos Santos Caldas","id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87","full_name":"Dos Santos Caldas, Paulo R","orcid":"0000-0001-6730-4461","first_name":"Paulo R"},{"first_name":"Christoph M","full_name":"Sommer, Christoph M","last_name":"Sommer","id":"4DF26D8C-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1216-9105"},{"first_name":"Maria D","id":"319AA9CE-F248-11E8-B48F-1D18A9856A87","last_name":"Lopez Pelegrin","full_name":"Lopez Pelegrin, Maria D"},{"full_name":"Michalik, David","last_name":"Michalik","id":"B9577E20-AA38-11E9-AC9A-0930E6697425","first_name":"David"},{"last_name":"Loose","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin"}],"publication_status":"published","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41467-022-34485-1"}],"record":[{"id":"10934","relation":"research_data","status":"public"},{"status":"public","relation":"dissertation_contains","id":"14280"}]},"language":[{"iso":"eng"}],"article_number":"2635","publication":"Nature Communications","status":"public","ec_funded":1,"department":[{"_id":"MaLo"}],"file_date_updated":"2022-05-13T09:10:51Z","doi":"10.1038/s41467-022-30301-y","publisher":"Springer Nature","keyword":["General Physics and Astronomy","General Biochemistry","Genetics and Molecular Biology","General Chemistry"],"_id":"11373","quality_controlled":"1","abstract":[{"lang":"eng","text":"The actin-homologue FtsA is essential for E. coli cell division, as it links FtsZ filaments in the Z-ring to transmembrane proteins. FtsA is thought to initiate cell constriction by switching from an inactive polymeric to an active monomeric conformation, which recruits downstream proteins and stabilizes the Z-ring. However, direct biochemical evidence for this mechanism is missing. Here, we use reconstitution experiments and quantitative fluorescence microscopy to study divisome activation in vitro. By comparing wild-type FtsA with FtsA R286W, we find that this hyperactive mutant outperforms FtsA WT in replicating FtsZ treadmilling dynamics, FtsZ filament stabilization and recruitment of FtsN. We could attribute these differences to a faster exchange and denser packing of FtsA R286W below FtsZ filaments. Using FRET microscopy, we also find that FtsN binding promotes FtsA self-interaction. We propose that in the active divisome FtsA and FtsN exist as a dynamic copolymer that follows treadmilling filaments of FtsZ."}],"day":"12","fulldoi":"https://doi.org/10.1038/s41467-022-30301-y","has_accepted_license":"1"},{"scopus_import":"1","oa_version":"Published Version","main_file_link":[{"url":"https://doi.org/10.1073/pnas.2010054118","open_access":"1"}],"month":"01","external_id":{"pmid":["33443153"],"isi":["000607270100018"]},"project":[{"grant_number":"RGY0083/2016","name":"Reconstitution of cell polarity and axis determination in a cell-free system","_id":"2599F062-B435-11E9-9278-68D0E5697425"}],"year":"2021","corr_author":"1","type":"journal_article","publication_identifier":{"issn":["0027-8424"],"eissn":["1091-6490"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2021-01-03T23:01:23Z","oa":1,"citation":{"ieee":"C. F. Düllberg, A. Auer, N. Canigova, K. Loibl, and M. Loose, “In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 118, no. 1. National Academy of Sciences, 2021.","chicago":"Düllberg, Christian F, Albert Auer, Nikola Canigova, Katrin Loibl, and Martin Loose. “In Vitro Reconstitution Reveals Phosphoinositides as Cargo-Release Factors and Activators of the ARF6 GAP ADAP1.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2021. <a href=\"https://doi.org/10.1073/pnas.2010054118\">https://doi.org/10.1073/pnas.2010054118</a>.","short":"C.F. Düllberg, A. Auer, N. Canigova, K. Loibl, M. Loose, Proceedings of the National Academy of Sciences of the United States of America 118 (2021).","ama":"Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2021;118(1). doi:<a href=\"https://doi.org/10.1073/pnas.2010054118\">10.1073/pnas.2010054118</a>","mla":"Düllberg, Christian F., et al. “In Vitro Reconstitution Reveals Phosphoinositides as Cargo-Release Factors and Activators of the ARF6 GAP ADAP1.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 118, no. 1, e2010054118, National Academy of Sciences, 2021, doi:<a href=\"https://doi.org/10.1073/pnas.2010054118\">10.1073/pnas.2010054118</a>.","apa":"Düllberg, C. F., Auer, A., Canigova, N., Loibl, K., &#38; Loose, M. (2021). In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.2010054118\">https://doi.org/10.1073/pnas.2010054118</a>","ista":"Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. 2021. In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1. Proceedings of the National Academy of Sciences of the United States of America. 118(1), e2010054118."},"isi":1,"article_type":"original","date_updated":"2026-06-18T19:37:53Z","ddc":["570"],"_id":"8988","doi":"10.1073/pnas.2010054118","publisher":"National Academy of Sciences","fulldoi":"https://doi.org/10.1073/pnas.2010054118","issue":"1","abstract":[{"lang":"eng","text":"The differentiation of cells depends on a precise control of their internal organization, which is the result of a complex dynamic interplay between the cytoskeleton, molecular motors, signaling molecules, and membranes. For example, in the developing neuron, the protein ADAP1 (ADP-ribosylation factor GTPase-activating protein [ArfGAP] with dual pleckstrin homology [PH] domains 1) has been suggested to control dendrite branching by regulating the small GTPase ARF6. Together with the motor protein KIF13B, ADAP1 is also thought to mediate delivery of the second messenger phosphatidylinositol (3,4,5)-trisphosphate (PIP3) to the axon tip, thus contributing to PIP3 polarity. However, what defines the function of ADAP1 and how its different roles are coordinated are still not clear. Here, we studied ADAP1’s functions using in vitro reconstitutions. We found that KIF13B transports ADAP1 along microtubules, but that PIP3 as well as PI(3,4)P2 act as stop signals for this transport instead of being transported. We also demonstrate that these phosphoinositides activate ADAP1’s enzymatic activity to catalyze GTP hydrolysis by ARF6. Together, our results support a model for the cellular function of ADAP1, where KIF13B transports ADAP1 until it encounters high PIP3/PI(3,4)P2 concentrations in the plasma membrane. Here, ADAP1 disassociates from the motor to inactivate ARF6, promoting dendrite branching."}],"day":"05","quality_controlled":"1","publication_status":"published","author":[{"orcid":"0000-0001-6335-9748","last_name":"Düllberg","id":"459064DC-F248-11E8-B48F-1D18A9856A87","full_name":"Düllberg, Christian F","first_name":"Christian F"},{"last_name":"Auer","id":"3018E8C2-F248-11E8-B48F-1D18A9856A87","full_name":"Auer, Albert","orcid":"0000-0002-3580-2906","first_name":"Albert"},{"first_name":"Nikola","last_name":"Canigova","orcid":"0000-0002-8518-5926","full_name":"Canigova, Nikola","id":"3795523E-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Loibl, Katrin","orcid":"0000-0002-2429-7668","id":"3760F32C-F248-11E8-B48F-1D18A9856A87","last_name":"Loibl","first_name":"Katrin"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"intvolume":"       118","title":"In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1","article_processing_charge":"No","acknowledgement":"We thank Urban Bezeljak, Natalia Baranova, Mar Lopez-Pelegrin, Catarina Alcarva, and Victoria Faas for sharing reagents and helpful discussions. We thank Veronika Szentirmai for help with protein purifications. We thank Carrie Bernecky, Sascha Martens, and the M.L. lab for comments on the manuscript. We thank the bioimaging facility, the life science facility, and Armel Nicolas from the mass spec facility at the Institute of Science and Technology (IST) Austria for technical support. C.D. acknowledges funding from the IST fellowship program; this work was supported by Human Frontier Science Program Young Investigator Grant\r\nRGY0083/2016. ","volume":118,"date_published":"2021-01-05T00:00:00Z","pmid":1,"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"},{"_id":"EM-Fac"}],"department":[{"_id":"MaLo"},{"_id":"MiSi"}],"article_number":"e2010054118","publication":"Proceedings of the National Academy of Sciences of the United States of America","status":"public","language":[{"iso":"eng"}]},{"publisher":"eLife Sciences Publications","doi":"10.7554/eLife.61525","file_date_updated":"2021-03-22T07:36:08Z","_id":"9243","quality_controlled":"1","day":"24","abstract":[{"lang":"eng","text":"Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials."}],"has_accepted_license":"1","fulldoi":"https://doi.org/10.7554/eLife.61525","date_published":"2021-02-24T00:00:00Z","volume":10,"acknowledgement":"We thank Alexander Egan (Newcastle University) for purified proteins LpoB(sol) and LpoPPa(sol), Federico Corona (Newcastle University) for purified MepM, and Oliver Birkholz and Jacob Piehler (Department of Biology and Center of Cellular Nanoanalytics, University of Osnabru¨ ck) for their help with PBP1B reconstitution into polymer-SLBs and initial guidance on single particle tracking. We also acknowledge Christian P Richter and Changjiang You (Department of Biology and Center of Cellular Nanoanalytics, University of Osnabru¨ ck) for providing SLIMfast software and tris-DODA-NTA reagent, respectively. This work was funded by the BBSRC grant BB/R017409/1 (to WV), the European Research Council through grant ERC-2015-StG-679239 (to ML), and long-term fellowships HFSP LT 000824/2016-L4 and EMBO ALTF 1163–2015 (to NB). ","article_processing_charge":"No","intvolume":"        10","title":"Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins","author":[{"first_name":"Víctor M.","last_name":"Hernández-Rocamora","full_name":"Hernández-Rocamora, Víctor M."},{"first_name":"Natalia S.","orcid":"0000-0002-3086-9124","id":"38661662-F248-11E8-B48F-1D18A9856A87","full_name":"Baranova, Natalia S.","last_name":"Baranova"},{"first_name":"Katharina","full_name":"Peters, Katharina","last_name":"Peters"},{"last_name":"Breukink","full_name":"Breukink, Eefjan","first_name":"Eefjan"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","last_name":"Loose","first_name":"Martin"},{"first_name":"Waldemar","full_name":"Vollmer, Waldemar","last_name":"Vollmer"}],"publication_status":"published","language":[{"iso":"eng"}],"status":"public","publication":"eLife","article_number":"1-32","department":[{"_id":"MaLo"}],"ec_funded":1,"external_id":{"isi":["000627596400001"]},"month":"02","oa_version":"Published Version","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"scopus_import":"1","publication_identifier":{"eissn":["2050-084X"]},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","type":"journal_article","project":[{"grant_number":"679239","name":"Self-Organization of the Bacterial Cell","call_identifier":"H2020","_id":"2595697A-B435-11E9-9278-68D0E5697425"},{"grant_number":"ALTF 2015-1163","name":"Synthesis of bacterial cell wall","_id":"2596EAB6-B435-11E9-9278-68D0E5697425"},{"_id":"259B655A-B435-11E9-9278-68D0E5697425","name":"Reconstitution of bacterial cell wall synthesis","grant_number":"LT000824/2016"}],"year":"2021","citation":{"ieee":"V. M. Hernández-Rocamora, N. S. Baranova, K. Peters, E. Breukink, M. Loose, and W. Vollmer, “Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins,” <i>eLife</i>, vol. 10. eLife Sciences Publications, 2021.","chicago":"Hernández-Rocamora, Víctor M., Natalia S. Baranova, Katharina Peters, Eefjan Breukink, Martin Loose, and Waldemar Vollmer. “Real Time Monitoring of Peptidoglycan Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” <i>ELife</i>. eLife Sciences Publications, 2021. <a href=\"https://doi.org/10.7554/eLife.61525\">https://doi.org/10.7554/eLife.61525</a>.","ama":"Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer W. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins. <i>eLife</i>. 2021;10. doi:<a href=\"https://doi.org/10.7554/eLife.61525\">10.7554/eLife.61525</a>","short":"V.M. Hernández-Rocamora, N.S. Baranova, K. Peters, E. Breukink, M. Loose, W. Vollmer, ELife 10 (2021).","mla":"Hernández-Rocamora, Víctor M., et al. “Real Time Monitoring of Peptidoglycan Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” <i>ELife</i>, vol. 10, 1–32, eLife Sciences Publications, 2021, doi:<a href=\"https://doi.org/10.7554/eLife.61525\">10.7554/eLife.61525</a>.","apa":"Hernández-Rocamora, V. M., Baranova, N. S., Peters, K., Breukink, E., Loose, M., &#38; Vollmer, W. (2021). Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/eLife.61525\">https://doi.org/10.7554/eLife.61525</a>","ista":"Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer W. 2021. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin binding proteins. eLife. 10, 1–32."},"oa":1,"file":[{"access_level":"open_access","file_size":2314698,"content_type":"application/pdf","success":1,"date_created":"2021-03-22T07:36:08Z","creator":"dernst","checksum":"79897a09bfecd9914d39c4aea2841855","file_name":"2021_eLife_HernandezRocamora.pdf","date_updated":"2021-03-22T07:36:08Z","file_id":"9268","relation":"main_file"}],"date_created":"2021-03-14T23:01:33Z","ddc":["570"],"date_updated":"2024-10-22T10:04:21Z","isi":1,"article_type":"original"},{"_id":"9414","license":"https://creativecommons.org/licenses/by-nc-sa/3.0/","publisher":"American Society for Cell Biology","doi":"10.1091/MBC.E20-11-0723","fulldoi":"https://doi.org/10.1091/MBC.E20-11-0723","issue":"9","day":"19","abstract":[{"text":"Microtubule plus-end depolymerization rate is a potentially important target of physiological regulation, but it has been challenging to measure, so its role in spatial organization is poorly understood. Here we apply a method for tracking plus ends based on time difference imaging to measure depolymerization rates in large interphase asters growing in Xenopus egg extract. We observed strong spatial regulation of depolymerization rates, which were higher in the aster interior compared with the periphery, and much less regulation of polymerization or catastrophe rates. We interpret these data in terms of a limiting component model, where aster growth results in lower levels of soluble tubulin and microtubule-associated proteins (MAPs) in the interior cytosol compared with that at the periphery. The steady-state polymer fraction of tubulin was ∼30%, so tubulin is not strongly depleted in the aster interior. We propose that the limiting component for microtubule assembly is a MAP that inhibits depolymerization, and that egg asters are tuned to low microtubule density.","lang":"eng"}],"quality_controlled":"1","author":[{"first_name":"Keisuke","full_name":"Ishihara, Keisuke","last_name":"Ishihara"},{"first_name":"Franziska","last_name":"Decker","full_name":"Decker, Franziska"},{"orcid":"0000-0001-6730-4461","full_name":"Dos Santos Caldas, Paulo R","last_name":"Dos Santos Caldas","id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87","first_name":"Paulo R"},{"full_name":"Pelletier, James F.","last_name":"Pelletier","first_name":"James F."},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","first_name":"Martin"},{"full_name":"Brugués, Jan","last_name":"Brugués","first_name":"Jan"},{"first_name":"Timothy J.","last_name":"Mitchison","full_name":"Mitchison, Timothy J."}],"publication_status":"published","article_processing_charge":"No","acknowledgement":"The authors thank the members of Mitchison, Brugués, and Jay Gatlin groups (University of Wyoming) for discussions. We thank Heino Andreas (MPI-CBG) for frog maintenance. We thank Nikon for microscopy support at Marine Biological Laboratory (MBL). K.I. was supported by fellowships from the Honjo International Scholarship Foundation and Center of Systems Biology Dresden. F.D. was supported by the DIGGS-BB fellowship provided by the German Research Foundation (DFG). P.C. is supported by a Boehringer Ingelheim Fonds PhD fellowship. J.F.P. was supported by a fellowship from the Fannie and John Hertz Foundation. M.L.’s research is supported by European Research Council (ERC) Grant no. ERC-2015-StG-679239. J.B.’s research is supported by the Human Frontiers Science Program (CDA00074/2014). T.J.M.’s research is supported by National Institutes of Health Grant no. R35GM131753.","intvolume":"        32","title":"Spatial variation of microtubule depolymerization in large asters","volume":32,"date_published":"2021-04-19T00:00:00Z","pmid":1,"department":[{"_id":"MaLo"}],"ec_funded":1,"status":"public","page":"869-879","publication":"Molecular Biology of the Cell","language":[{"iso":"eng"}],"oa_version":"Published Version","tmp":{"short":"CC BY-NC-SA (3.0)","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA 3.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/3.0/legalcode"},"scopus_import":"1","main_file_link":[{"open_access":"1","url":"https://www.molbiolcell.org/doi/10.1091/mbc.E20-11-0723"}],"month":"04","external_id":{"isi":["000641574700005"],"pmid":["33439671"]},"year":"2021","project":[{"_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","grant_number":"679239","name":"Self-Organization of the Bacterial Cell"},{"_id":"260D98C8-B435-11E9-9278-68D0E5697425","name":"Reconstitution of Bacterial Cell Division Using Purified Components"}],"type":"journal_article","publication_identifier":{"eissn":["1939-4586"],"issn":["1059-1524"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2021-05-23T22:01:45Z","citation":{"mla":"Ishihara, Keisuke, et al. “Spatial Variation of Microtubule Depolymerization in Large Asters.” <i>Molecular Biology of the Cell</i>, vol. 32, no. 9, American Society for Cell Biology, 2021, pp. 869–79, doi:<a href=\"https://doi.org/10.1091/MBC.E20-11-0723\">10.1091/MBC.E20-11-0723</a>.","apa":"Ishihara, K., Decker, F., Dos Santos Caldas, P. R., Pelletier, J. F., Loose, M., Brugués, J., &#38; Mitchison, T. J. (2021). Spatial variation of microtubule depolymerization in large asters. <i>Molecular Biology of the Cell</i>. American Society for Cell Biology. <a href=\"https://doi.org/10.1091/MBC.E20-11-0723\">https://doi.org/10.1091/MBC.E20-11-0723</a>","ista":"Ishihara K, Decker F, Dos Santos Caldas PR, Pelletier JF, Loose M, Brugués J, Mitchison TJ. 2021. Spatial variation of microtubule depolymerization in large asters. Molecular Biology of the Cell. 32(9), 869–879.","short":"K. Ishihara, F. Decker, P.R. Dos Santos Caldas, J.F. Pelletier, M. Loose, J. Brugués, T.J. Mitchison, Molecular Biology of the Cell 32 (2021) 869–879.","ama":"Ishihara K, Decker F, Dos Santos Caldas PR, et al. Spatial variation of microtubule depolymerization in large asters. <i>Molecular Biology of the Cell</i>. 2021;32(9):869-879. doi:<a href=\"https://doi.org/10.1091/MBC.E20-11-0723\">10.1091/MBC.E20-11-0723</a>","chicago":"Ishihara, Keisuke, Franziska Decker, Paulo R Dos Santos Caldas, James F. Pelletier, Martin Loose, Jan Brugués, and Timothy J. Mitchison. “Spatial Variation of Microtubule Depolymerization in Large Asters.” <i>Molecular Biology of the Cell</i>. American Society for Cell Biology, 2021. <a href=\"https://doi.org/10.1091/MBC.E20-11-0723\">https://doi.org/10.1091/MBC.E20-11-0723</a>.","ieee":"K. Ishihara <i>et al.</i>, “Spatial variation of microtubule depolymerization in large asters,” <i>Molecular Biology of the Cell</i>, vol. 32, no. 9. American Society for Cell Biology, pp. 869–879, 2021."},"oa":1,"article_type":"original","isi":1,"date_updated":"2026-06-18T19:52:16Z","ddc":["570"]},{"language":[{"iso":"eng"}],"article_number":"8350","publication":"International Journal of Molecular Sciences","status":"public","ec_funded":1,"department":[{"_id":"MaLo"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"date_published":"2021-08-01T00:00:00Z","volume":22,"pmid":1,"title":"Cardiolipin-containing lipid membranes attract the bacterial cell division protein diviva","intvolume":"        22","acknowledgement":"We thank Daniela Krajˇcíkova, Katarína Muchová, Zuzana Chromíkova and other members of Barák’s laboratory for useful discussions, suggestions and help. Special thanks also to Emília Chovancová for technical support. We are grateful to Juraj Labaj for drawing the model and for help with graphics. Many thanks to all members of Loose’s laboratory: Maria del Mar\r\nLópez, Paulo Caldas, Philipp Radler, and other members of the Loose’s laboratory for sharing their knowledge of SLB preparation and TIRF experiment chambers, for sharing coverslips and for help with the TIRF microscope and data analysis. We also thank the members of the Dept. of Biochemistry of Biomembranes at the Institute of Animal Biochemistry and Genetics, CBs SAS for their help with preparing the lipid mixtures. We thank J. Bauer for critically reading the manuscript.","article_processing_charge":"Yes","author":[{"first_name":"Naďa","full_name":"Labajová, Naďa","last_name":"Labajová"},{"first_name":"Natalia S.","last_name":"Baranova","full_name":"Baranova, Natalia S.","id":"38661662-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-3086-9124"},{"full_name":"Jurásek, Miroslav","last_name":"Jurásek","first_name":"Miroslav"},{"full_name":"Vácha, Robert","last_name":"Vácha","first_name":"Robert"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Barák, Imrich","last_name":"Barák","first_name":"Imrich"}],"publication_status":"published","quality_controlled":"1","abstract":[{"text":"DivIVA is a protein initially identified as a spatial regulator of cell division in the model organism Bacillus subtilis, but its homologues are present in many other Gram-positive bacteria, including Clostridia species. Besides its role as topological regulator of the Min system during bacterial cell division, DivIVA is involved in chromosome segregation during sporulation, genetic competence, and cell wall synthesis. DivIVA localizes to regions of high membrane curvature, such as the cell poles and cell division site, where it recruits distinct binding partners. Previously, it was suggested that negative curvature sensing is the main mechanism by which DivIVA binds to these specific regions. Here, we show that Clostridioides difficile DivIVA binds preferably to membranes containing negatively charged phospholipids, especially cardiolipin. Strikingly, we observed that upon binding, DivIVA modifies the lipid distribution and induces changes to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA might play a more complex and so far unknown active role during the formation of the cell division septal membrane. ","lang":"eng"}],"day":"01","fulldoi":"https://doi.org/10.3390/ijms22158350","issue":"15","has_accepted_license":"1","file_date_updated":"2021-08-16T09:35:56Z","doi":"10.3390/ijms22158350","publisher":"MDPI","_id":"9907","ddc":["570"],"date_updated":"2025-07-10T12:02:05Z","article_type":"original","isi":1,"oa":1,"citation":{"ama":"Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. Cardiolipin-containing lipid membranes attract the bacterial cell division protein diviva. <i>International Journal of Molecular Sciences</i>. 2021;22(15). doi:<a href=\"https://doi.org/10.3390/ijms22158350\">10.3390/ijms22158350</a>","short":"N. Labajová, N.S. Baranova, M. Jurásek, R. Vácha, M. Loose, I. Barák, International Journal of Molecular Sciences 22 (2021).","ista":"Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. 2021. Cardiolipin-containing lipid membranes attract the bacterial cell division protein diviva. International Journal of Molecular Sciences. 22(15), 8350.","mla":"Labajová, Naďa, et al. “Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein Diviva.” <i>International Journal of Molecular Sciences</i>, vol. 22, no. 15, 8350, MDPI, 2021, doi:<a href=\"https://doi.org/10.3390/ijms22158350\">10.3390/ijms22158350</a>.","apa":"Labajová, N., Baranova, N. S., Jurásek, M., Vácha, R., Loose, M., &#38; Barák, I. (2021). Cardiolipin-containing lipid membranes attract the bacterial cell division protein diviva. <i>International Journal of Molecular Sciences</i>. MDPI. <a href=\"https://doi.org/10.3390/ijms22158350\">https://doi.org/10.3390/ijms22158350</a>","ieee":"N. Labajová, N. S. Baranova, M. Jurásek, R. Vácha, M. Loose, and I. Barák, “Cardiolipin-containing lipid membranes attract the bacterial cell division protein diviva,” <i>International Journal of Molecular Sciences</i>, vol. 22, no. 15. MDPI, 2021.","chicago":"Labajová, Naďa, Natalia S. Baranova, Miroslav Jurásek, Robert Vácha, Martin Loose, and Imrich Barák. “Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein Diviva.” <i>International Journal of Molecular Sciences</i>. MDPI, 2021. <a href=\"https://doi.org/10.3390/ijms22158350\">https://doi.org/10.3390/ijms22158350</a>."},"date_created":"2021-08-15T22:01:27Z","file":[{"date_updated":"2021-08-16T09:35:56Z","file_id":"9923","file_name":"2021_InternationalJournalOfMolecularSciences_Labajová .pdf","relation":"main_file","date_created":"2021-08-16T09:35:56Z","success":1,"file_size":6132410,"content_type":"application/pdf","access_level":"open_access","checksum":"a4bc06e9a2c803ceff5a91f10b174054","creator":"asandaue"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_identifier":{"issn":["1661-6596"],"eissn":["1422-0067"]},"type":"journal_article","year":"2021","project":[{"name":"Self-Organization of the Bacterial Cell","grant_number":"679239","call_identifier":"H2020","_id":"2595697A-B435-11E9-9278-68D0E5697425"}],"external_id":{"isi":["000681815400001"],"pmid":["34361115"]},"month":"08","scopus_import":"1","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"oa_version":"Published Version"}]