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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"}],"title":"Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape","month":"04","article_type":"original","article_number":"eaea6343","day":"16","scopus_import":"1","author":[{"id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","full_name":"Springstein, Benjamin L","orcid":"0000-0002-3461-5391","first_name":"Benjamin L","last_name":"Springstein"},{"full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","orcid":"0000-0003-2311-2112","last_name":"Javoor","first_name":"Manjunath"},{"full_name":"Megrian, Daniela","last_name":"Megrian","first_name":"Daniela"},{"id":"ffab949d-133f-11ed-8f02-94de21ace503","full_name":"Hajdu, Roman","first_name":"Roman","last_name":"Hajdu"},{"first_name":"Dustin M.","last_name":"Hanke","full_name":"Hanke, Dustin M."},{"last_name":"Zens","first_name":"Bettina","orcid":"0000-0002-9561-1239","full_name":"Zens, Bettina","id":"45FD126C-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Weiss","first_name":"Gregor L.","full_name":"Weiss, Gregor L."},{"last_name":"Schur","first_name":"Florian Km","orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian Km"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}],"project":[{"_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","call_identifier":"H2020","name":"IST-BRIDGE: International postdoctoral program"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb"}],"year":"2026","doi":"10.1126/science.aea6343","date_published":"2026-04-16T00:00:00Z","volume":392,"ec_funded":1,"oa_version":"None","publication_status":"published","publisher":"AAAS","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.).","intvolume":"       392","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Science","_id":"21762","date_updated":"2026-04-28T13:29:05Z","article_processing_charge":"No","issue":"6795","language":[{"iso":"eng"}],"OA_type":"closed access","citation":{"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.","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).","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>.","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>","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.","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>."},"publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"pmid":1,"department":[{"_id":"MaLo"},{"_id":"FlSc"},{"_id":"GradSch"},{"_id":"EM-Fac"}],"external_id":{"pmid":["41990175"]}},{"oa":1,"file":[{"file_size":2003892,"checksum":"5b85c299bdd46cbde000e3449da835e0","file_id":"19916","relation":"main_file","date_updated":"2025-06-27T07:35:29Z","access_level":"open_access","creator":"bsprings","content_type":"video/x-msvideo","date_created":"2025-06-27T07:35:29Z","file_name":"Supplementary Movie 1) in vivo time lapse microscopy of mNG-CorM.avi","success":1},{"date_created":"2025-06-27T07:35:28Z","content_type":"video/x-msvideo","file_name":"Supplementary Movie 2) mNG-CorM single 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9.pdf","content_type":"application/pdf","date_created":"2025-07-02T08:10:21Z","success":1},{"creator":"bsprings","access_level":"open_access","date_updated":"2025-07-02T08:10:21Z","relation":"main_file","file_id":"19955","checksum":"31ecac7daf4b50e2ea443f398fdc2110","file_size":6168864,"success":1,"file_name":"Supplementary Figure 10.pdf","content_type":"application/pdf","date_created":"2025-07-02T08:10:21Z"}],"acknowledgement":"We thank all members of the Martin Loose lab at ISTA for helpful discussions and Marko Kojic for critical reading of the manuscript. This research was supported by the Scientific Service Units (SSU) of ISTA through resources provided by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp) and the Electron Microscopy Facility (EMF), as well as the Lab Support Facility (LSF). This project has received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie Grant Agreement No.101034413 awarded to BLS as well as an ERC grant (ActinID, 101076260) from the European Union awarded to FKMS. Views and opinions expressed are however those of the author(s) only and do not necessarily reflect those of the European Union or the European Research Council. Neither the European Union nor the granting authority can be held responsible for them.\r\n\r\nWe are grateful for Antonia Herrero (Sevilla University) for sharing her extensive BACTH plasmid library and other plasmids as well as cyanobacterial strains. Likewise, we would like to thank Tal Dagan and Fabian Nies (both Kiel University) for sharing cyanobacterial strains and plasmids and for valuable discussions.\r\n\r\nWe would further like to express our gratitude to Nicolas Sapay and Alexis Michon for providing the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix screen of cyanobacterial CorR proteins. Finally, we also want to thank Jesse Hansen for advice in cryo-EM data processing","type":"research_data","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","file_date_updated":"2025-07-02T08:10:21Z","date_created":"2025-06-27T07:34:52Z","oa_version":"None","ec_funded":1,"date_published":"2025-06-27T00:00:00Z","status":"public","corr_author":"1","publisher":"Institute of Science and Technology Austria","contributor":[{"id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","contributor_type":"project_leader","first_name":"Benjamin L","last_name":"Springstein","orcid":"0000-0002-3461-5391"},{"contributor_type":"researcher","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","first_name":"Manjunath","last_name":"Javoor"},{"last_name":"Megrian","first_name":"Daniela","contributor_type":"researcher"},{"id":"ffab949d-133f-11ed-8f02-94de21ace503","contributor_type":"researcher","first_name":"Roman","last_name":"Hajdu"},{"first_name":"Dustin M","last_name":"Hanke","contributor_type":"researcher"},{"contributor_type":"researcher","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","first_name":"Florian KM","last_name":"Schur"},{"orcid":"0000-0001-7309-9724","last_name":"Loose","first_name":"Martin","contributor_type":"supervisor","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"has_accepted_license":"1","year":"2025","doi":"10.15479/AT:ISTA:19915","project":[{"name":"IST-BRIDGE: International postdoctoral program","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","call_identifier":"H2020"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb","grant_number":"101076260"}],"author":[{"full_name":"Springstein, Benjamin L","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","first_name":"Benjamin L","last_name":"Springstein","orcid":"0000-0002-3461-5391"}],"department":[{"_id":"MaLo"}],"day":"27","citation":{"apa":"Springstein, B. 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Kümmel, Science Advances 11 (2025) eadx2893.","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.","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>.","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>"},"publication_identifier":{"eissn":["2375-2548"]},"external_id":{"pmid":["40864718"],"isi":["001559806100033"]},"has_accepted_license":"1","OA_place":"publisher","OA_type":"gold","language":[{"iso":"eng"}],"publisher":"AAAS","publication_status":"published","date_published":"2025-08-29T00:00:00Z","volume":11,"oa_version":"Published Version","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"        11","file_date_updated":"2025-09-15T07:23:12Z","license":"https://creativecommons.org/licenses/by/4.0/","publication":"Science Advances","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"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).","PlanS_conform":"1","ddc":["570"],"title":"Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned","month":"08","page":"eadx2893","scopus_import":"1","DOAJ_listed":"1","day":"29","year":"2025","doi":"10.1126/sciadv.adx2893","project":[{"name":"Synthetic and structural biology of Rab GTPase networks","grant_number":"101045340","_id":"bd6ae2ca-d553-11ed-ba76-a4aa239da5ee"}],"author":[{"full_name":"Wilmes, Stephan","last_name":"Wilmes","first_name":"Stephan"},{"full_name":"Tönjes, Jesse","first_name":"Jesse","last_name":"Tönjes"},{"full_name":"Drechsler, Maik","last_name":"Drechsler","first_name":"Maik"},{"first_name":"Anita","last_name":"Ruf","full_name":"Ruf, Anita"},{"last_name":"Schäfer","first_name":"Jan Hannes","full_name":"Schäfer, Jan Hannes"},{"full_name":"Lürick, Anna","first_name":"Anna","last_name":"Lürick"},{"full_name":"Januliene, Dovile","last_name":"Januliene","first_name":"Dovile"},{"last_name":"Apelt","first_name":"Steven","full_name":"Apelt, Steven"},{"full_name":"Di Iorio, Daniele","first_name":"Daniele","last_name":"Di Iorio"},{"full_name":"Wegner, Seraphine V.","first_name":"Seraphine V.","last_name":"Wegner"},{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"},{"full_name":"Moeller, Arne","first_name":"Arne","last_name":"Moeller"},{"first_name":"Achim","last_name":"Paululat","full_name":"Paululat, Achim"},{"first_name":"Daniel","last_name":"Kümmel","full_name":"Kümmel, Daniel"}],"article_type":"original","status":"public","quality_controlled":"1","date_created":"2025-09-14T22:01:32Z","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"}],"type":"journal_article","oa":1,"file":[{"file_name":"2025_ScienceAdvance_Wilmes.pdf","content_type":"application/pdf","date_created":"2025-09-15T07:23:12Z","success":1,"relation":"main_file","access_level":"open_access","creator":"dernst","date_updated":"2025-09-15T07:23:12Z","checksum":"a3de801f3c6c1deadd7099d965db799a","file_size":3434827,"file_id":"20355"}]},{"has_accepted_license":"1","OA_place":"publisher","language":[{"iso":"eng"}],"department":[{"_id":"GradSch"},{"_id":"JiFr"},{"_id":"MaLo"}],"publication_identifier":{"issn":["2663-337X"]},"citation":{"apa":"Giannini, C. (2025). <i>Nuclear and cell surface auxin signaling in A. thaliana developmental transitions</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-20364\">https://doi.org/10.15479/AT-ISTA-20364</a>","ama":"Giannini C. Nuclear and cell surface auxin signaling in A. thaliana developmental transitions. 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20364\">10.15479/AT-ISTA-20364</a>","mla":"Giannini, Caterina. <i>Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions</i>. Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20364\">10.15479/AT-ISTA-20364</a>.","short":"C. Giannini, Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions, Institute of Science and Technology Austria, 2025.","ista":"Giannini C. 2025. Nuclear and cell surface auxin signaling in A. thaliana developmental transitions. Institute of Science and Technology Austria.","chicago":"Giannini, Caterina. “Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions.” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-20364\">https://doi.org/10.15479/AT-ISTA-20364</a>.","ieee":"C. Giannini, “Nuclear and cell surface auxin signaling in A. thaliana developmental transitions,” Institute of Science and Technology Austria, 2025."},"_id":"20364","article_processing_charge":"No","date_updated":"2026-04-07T11:52:16Z","alternative_title":["ISTA Thesis"],"acknowledgement":"Plant Facility,\r\nProtein Service Facility","supervisor":[{"orcid":"0000-0002-8302-7596","last_name":"Friml","first_name":"Jiří","full_name":"Friml, Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87"}],"user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","file_date_updated":"2025-09-30T14:31:29Z","date_published":"2025-09-19T00:00:00Z","oa_version":"Published Version","publisher":"Institute of Science and Technology Austria","publication_status":"published","page":"151","day":"19","year":"2025","doi":"10.15479/AT-ISTA-20364","author":[{"last_name":"Giannini","first_name":"Caterina","id":"e3fdddd5-f6e0-11ea-865d-ca99ee6367f4","full_name":"Giannini, Caterina"}],"title":"Nuclear and cell surface auxin signaling in A. thaliana developmental transitions","month":"09","degree_awarded":"PhD","related_material":{"record":[{"id":"12291","status":"public","relation":"part_of_dissertation"},{"relation":"part_of_dissertation","status":"public","id":"19399"}]},"ddc":["580"],"type":"dissertation","file":[{"file_id":"20390","file_size":14278965,"checksum":"536ba1701453b0b2346be14c046b2911","date_updated":"2025-09-30T14:31:29Z","access_level":"closed","creator":"cgiannin","relation":"main_file","embargo":"2026-09-30","content_type":"application/pdf","embargo_to":"open_access","date_created":"2025-09-24T14:46:34Z","file_name":"2025_Giannini_Caterina_Thesis...pdf"},{"file_name":"2025_Giannini_Caterina_Thesis...docx","date_created":"2025-09-24T14:46:35Z","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","access_level":"closed","creator":"cgiannin","date_updated":"2025-09-24T14:46:35Z","relation":"source_file","file_id":"20391","checksum":"192f55262f2da2ea0a59d9c23a1b8573","file_size":24499022}],"acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"Bio"}],"keyword":["Auxin Signaling","Plant Development"],"date_created":"2025-09-19T12:23:38Z","status":"public","corr_author":"1"},{"file_date_updated":"2025-12-10T13:09:58Z","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","alternative_title":["ISTA Thesis"],"supervisor":[{"full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724"}],"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication_status":"published","publisher":"Institute of Science and Technology Austria","oa_version":"Published Version","date_published":"2025-12-09T00:00:00Z","publication_identifier":{"isbn":["978-3-99078-073-2"],"issn":["2663-337X"]},"citation":{"chicago":"Kojic, Marko. “Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria.” Institute of Science and Technology Austria, 2025. <a href=\"https://doi.org/10.15479/AT-ISTA-20741\">https://doi.org/10.15479/AT-ISTA-20741</a>.","ieee":"M. Kojic, “Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria,” Institute of Science and Technology Austria, 2025.","apa":"Kojic, M. (2025). <i>Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT-ISTA-20741\">https://doi.org/10.15479/AT-ISTA-20741</a>","ama":"Kojic M. Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria. 2025. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20741\">10.15479/AT-ISTA-20741</a>","mla":"Kojic, Marko. <i>Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria</i>. Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-20741\">10.15479/AT-ISTA-20741</a>.","short":"M. Kojic, Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria, Institute of Science and Technology Austria, 2025.","ista":"Kojic M. 2025. Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria. Institute of Science and Technology Austria."},"department":[{"_id":"GradSch"},{"_id":"MaLo"}],"language":[{"iso":"eng"}],"OA_place":"publisher","has_accepted_license":"1","date_updated":"2026-04-07T12:27:58Z","article_processing_charge":"No","_id":"20741","abstract":[{"text":"Life on Earth emerged when biomacromolecules were membrane-enclosed in a confined space where many essential chemical reactions were more likely to happen and thereby accelerate evolution. These kinds of membranes separated internal reactions from the outside chaos while staying flexible so that those primordial cells can move, adopt their shape and, most importantly, propagate. Such membrane plasticity still remains a defining feature of all modern cell types. This remarkable ability to change their shape is most prominently observed during their propagation (i.e., cell division). Throughout division, a cell undergoes drastic change in its shape, usually at the middle of the cell, pulling the two opposite membrane sides inward, closer to each other, and, finally, culminating in pinching off to separate the cell into two daughter cells. To achieve this, a cell needs to employ a protein machinery, usually termed divisome, that can coordinate all necessary intracellular processes with membrane remodelling and synthesis of other extracellular structures that decorate a cell. The focus of this dissertation is a membrane-remodelling FtsZ system that is present across all domains of life. FtsZ forms filaments that further self-organize into ring-like structures at the cell septum and together with other division proteins perform cell envelope synthesis and constriction. However, there are still knowledge gaps in our mechanistic understanding of division in both archaea and bacteria. My work presented in this dissertation centres around a simple yet not well understood question: How is the divisome positioned correctly at the mid-cell? To achieve the proper positioning, the divisome needs to (i) be recruited to the mid-cell and (ii) localized orthogonally to the long cell axis. I tackle these processes in two different systems by applying an in vitro biochemical bottom-up reconstitution approach. I use purified components of Haloferax volcanii and Escherichia coli divisome to explore how divisome is recruited to the mid-cell in archaea and how the Z-ring positions orthogonally to the long cell axis in bacteria, respectively. \r\n\r\nFirstly, I collaborate with archaeal cell and structural biologists to explore the assembly of early division proteins in two FtsZ-containing archaeon H. volcanii, a standard model system for understudied archaeal organisms. I particularly address the hierarchy of interactions that allow a tripartite complex formation (SepF-CdpB1-CdpB2) and how the hierarchy of interactions ultimately leads to the recruitment of FtsZ filaments to the septum. This part of work has been published in (Nußbaum et al., 2024). In collaboration with evolutionary biologists, I shed light on ancient features that archaeal divisome has retained to this day and also speculate on a property that it might have lost during the course of evolution. \r\n\r\nNext, I switch my attention to E. coli divisome. Particularly, I address the FtsZ’s intrinsic biophysical property that drives the Z-ring diameter, and thereby the perpendicular orientation of the Z-ring to the long cell axis based on suggested membrane curvature sensing mechanism (Vanhille-Campos et al., 2024). This property allows formation of different Z-ring diameters that match the variety of cell diameters present in prokaryotes. The results showcase that the distribution of charged amino acids in the intrinsically disordered linker at the C-terminus (CTL) of FtsZ is the major determining factor of Z-ring diameter with inter-CTL interactions as an underlying mechanism. \r\n\r\nFinally, I thoroughly explain the methodology I used to address the abovementioned projects, and I finish with a discussion on how early archaeal divisome assembly and curvature sensing mechanism in bacteria, at first sight unrelated topics, are interconnected and important groundwork for both fundamental and translational research. ","lang":"eng"}],"date_created":"2025-12-09T13:08:11Z","acknowledged_ssus":[{"_id":"Bio"}],"oa":1,"file":[{"checksum":"a3643d07e93134b2490a566b02a4517d","file_size":142876975,"file_id":"20774","relation":"source_file","creator":"mkojic","access_level":"closed","date_updated":"2025-12-10T13:09:58Z","file_name":"2025_marko_kojic_thesis.docx","date_created":"2025-12-10T13:09:58Z","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document"},{"relation":"main_file","date_updated":"2025-12-10T13:09:38Z","access_level":"open_access","creator":"mkojic","file_size":8597045,"checksum":"0a096f0af6ccc3a8329d5bb8797ad533","file_id":"20775","content_type":"application/pdf","date_created":"2025-12-10T13:09:38Z","file_name":"2025_marko_kojic_thesis.pdf","success":1}],"type":"dissertation","corr_author":"1","status":"public","author":[{"full_name":"Kojic, Marko","id":"73e7ecd4-dc85-11ea-9058-88a16394b160","last_name":"Kojic","first_name":"Marko","orcid":"0000-0001-7244-8128"}],"doi":"10.15479/AT-ISTA-20741","year":"2025","day":"09","ddc":["572"],"related_material":{"record":[{"id":"15118","relation":"part_of_dissertation","status":"public"}]},"degree_awarded":"PhD","month":"12","title":"Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria"},{"has_accepted_license":"1","OA_type":"gold","language":[{"iso":"eng"}],"OA_place":"publisher","department":[{"_id":"MaLo"},{"_id":"JiFr"}],"pmid":1,"publication_identifier":{"eissn":["1460-2075"],"issn":["0261-4189"]},"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>.","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>","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.","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.","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>.","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>"},"external_id":{"isi":["001306286100002"],"pmid":["39232130"]},"_id":"18073","article_processing_charge":"Yes","date_updated":"2025-09-08T09:22:11Z","issue":"20","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"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.","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","file_date_updated":"2025-01-13T08:43:20Z","intvolume":"        43","publication":"EMBO Journal","date_published":"2024-10-15T00:00:00Z","volume":43,"oa_version":"Published Version","publisher":"Embo Press","publication_status":"published","article_type":"original","page":"4668-4698","scopus_import":"1","day":"15","year":"2024","doi":"10.1038/s44318-024-00207-0","author":[{"last_name":"Kettel","first_name":"Paulina","full_name":"Kettel, Paulina"},{"full_name":"Marosits, Laura","first_name":"Laura","last_name":"Marosits"},{"last_name":"Spinetti","first_name":"Elena","full_name":"Spinetti, Elena"},{"first_name":"Michael","last_name":"Rechberger","full_name":"Rechberger, Michael"},{"id":"e3fdddd5-f6e0-11ea-865d-ca99ee6367f4","full_name":"Giannini, Caterina","first_name":"Caterina","last_name":"Giannini"},{"first_name":"Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 ","full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Isabell","last_name":"Niedermoser","full_name":"Niedermoser, Isabell"},{"full_name":"Fischer, Irmgard","first_name":"Irmgard","last_name":"Fischer"},{"last_name":"Versteeg","first_name":"Gijs A.","full_name":"Versteeg, Gijs A."},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Covino","first_name":"Roberto","full_name":"Covino, Roberto"},{"first_name":"G. Elif","last_name":"Karagöz","full_name":"Karagöz, G. Elif"}],"title":"Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering","month":"10","ddc":["570"],"type":"journal_article","oa":1,"file":[{"success":1,"file_name":"2024_Embo_Kettel.pdf","date_created":"2025-01-13T08:43:20Z","content_type":"application/pdf","creator":"dernst","access_level":"open_access","date_updated":"2025-01-13T08:43:20Z","relation":"main_file","file_id":"18827","checksum":"04f4df1a561083f2846676442fc4eb3c","file_size":10080854}],"date_created":"2024-09-15T22:01:42Z","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."}],"status":"public","quality_controlled":"1"},{"status":"public","quality_controlled":"1","date_created":"2025-01-29T08:39:27Z","abstract":[{"lang":"eng","text":"The synthesis of proteins as encoded in the genome depends critically on translational fidelity. Nevertheless, errors inevitably occur, and those that result in reading frame shifts are particularly consequential because the resulting polypeptides are typically nonfunctional. Despite the generally maladaptive impact of such errors, the proper decoding of certain mRNAs, including many viral mRNAs, depends on a process known as programmed ribosomal frameshifting. The fact that these programmed events, commonly involving a shift to the –1 frame, occur at specific evolutionarily optimized “slippery” sites has facilitated mechanistic investigation. By contrast, less is known about the scope and nature of error (i.e., nonprogrammed) frameshifting. Here, we examine error frameshifting by monitoring spontaneous frameshift events that suppress the effects of single base pair deletions affecting two unrelated test proteins. To map the precise sites of frameshifting, we developed a targeted mass spectrometry–based method called “translational tiling proteomics” for interrogating the full set of possible –1 slippage events that could produce the observed frameshift suppression. Surprisingly, such events occur at many sites along the transcripts, involving up to one half of the available codons. Only a subset of these resembled canonical “slippery” sites, implicating alternative mechanisms potentially involving noncognate mispairing events. Additionally, the aggregate frequency of these events (ranging from 1 to 10% in our test cases) was higher than we might have anticipated. Our findings point to an unexpected degree of mechanistic diversity among ribosomal frameshifting events and suggest that frameshifted products may contribute more significantly to the proteome than generally assumed."}],"type":"journal_article","oa":1,"file":[{"relation":"main_file","creator":"dernst","access_level":"open_access","date_updated":"2025-01-29T08:43:16Z","checksum":"5bd62c7cb4287e3706a1d45d6ef61fd1","file_size":720902,"file_id":"18939","file_name":"2024_PNAS_Springstein.pdf","content_type":"application/pdf","date_created":"2025-01-29T08:43:16Z","success":1}],"ddc":["570"],"title":"Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics","month":"02","day":"06","scopus_import":"1","author":[{"id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","full_name":"Springstein, Benjamin L","last_name":"Springstein","first_name":"Benjamin L","orcid":"0000-0002-3461-5391"},{"first_name":"Joao A.","last_name":"Paulo","full_name":"Paulo, Joao A."},{"first_name":"Hankum","last_name":"Park","full_name":"Park, Hankum"},{"last_name":"Henry","first_name":"Kemardo","full_name":"Henry, Kemardo"},{"first_name":"Eleanor","last_name":"Fleming","full_name":"Fleming, Eleanor"},{"full_name":"Feder, Zoë","first_name":"Zoë","last_name":"Feder"},{"full_name":"Harper, J. Wade","last_name":"Harper","first_name":"J. Wade"},{"last_name":"Hochschild","first_name":"Ann","full_name":"Hochschild, Ann"}],"year":"2024","doi":"10.1073/pnas.2317453121","article_type":"original","article_number":"e2317453121","publication_status":"published","publisher":"National Academy of Sciences","volume":121,"date_published":"2024-02-06T00:00:00Z","oa_version":"Published Version","file_date_updated":"2025-01-29T08:43:16Z","intvolume":"       121","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Proceedings of the National Academy of Sciences of the United States of America","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"acknowledgement":"We thank S. L. Dove for valuable discussion and comments on the manuscript and R. Hellmiss for artwork. This work was supported by NIH grants GM136247 to A.H., AG011085 to J.W.H., and GM132129 to J.A.P.","issue":"6","_id":"18938","date_updated":"2025-05-14T11:02:52Z","article_processing_charge":"No","citation":{"apa":"Springstein, B. L., Paulo, J. A., Park, H., Henry, K., Fleming, E., Feder, Z., … Hochschild, A. (2024). Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics. <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.2317453121\">https://doi.org/10.1073/pnas.2317453121</a>","ista":"Springstein BL, Paulo JA, Park H, Henry K, Fleming E, Feder Z, Harper JW, Hochschild A. 2024. Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics. Proceedings of the National Academy of Sciences of the United States of America. 121(6), e2317453121.","short":"B.L. Springstein, J.A. Paulo, H. Park, K. Henry, E. Fleming, Z. Feder, J.W. Harper, A. Hochschild, Proceedings of the National Academy of Sciences of the United States of America 121 (2024).","mla":"Springstein, Benjamin L., et al. “Systematic Analysis of Nonprogrammed Frameshift Suppression in E.Coli via Translational Tiling Proteomics.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 6, e2317453121, National Academy of Sciences, 2024, doi:<a href=\"https://doi.org/10.1073/pnas.2317453121\">10.1073/pnas.2317453121</a>.","ama":"Springstein BL, Paulo JA, Park H, et al. Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2024;121(6). doi:<a href=\"https://doi.org/10.1073/pnas.2317453121\">10.1073/pnas.2317453121</a>","ieee":"B. L. Springstein <i>et al.</i>, “Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 6. National Academy of Sciences, 2024.","chicago":"Springstein, Benjamin L, Joao A. Paulo, Hankum Park, Kemardo Henry, Eleanor Fleming, Zoë Feder, J. Wade Harper, and Ann Hochschild. “Systematic Analysis of Nonprogrammed Frameshift Suppression in E.Coli via Translational Tiling Proteomics.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2024. <a href=\"https://doi.org/10.1073/pnas.2317453121\">https://doi.org/10.1073/pnas.2317453121</a>."},"publication_identifier":{"issn":["0027-8424"],"eissn":["1091-6490"]},"pmid":1,"department":[{"_id":"MaLo"}],"external_id":{"pmid":["38289956"]},"OA_type":"hybrid","language":[{"iso":"eng"}],"OA_place":"publisher","has_accepted_license":"1"},{"abstract":[{"lang":"eng","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."}],"date_created":"2024-01-14T23:00:56Z","file":[{"content_type":"application/pdf","date_created":"2024-01-16T10:53:31Z","file_name":"2024_CurrentBiology_Arslan.pdf","success":1,"relation":"main_file","date_updated":"2024-01-16T10:53:31Z","creator":"dernst","access_level":"open_access","file_size":5183861,"checksum":"51220b76d72a614208f84bdbfbaf9b72","file_id":"14813"}],"oa":1,"acknowledged_ssus":[{"_id":"Bio"},{"_id":"PreCl"}],"type":"journal_article","corr_author":"1","quality_controlled":"1","status":"public","author":[{"orcid":"0000-0001-5809-9566","last_name":"Arslan","first_name":"Feyza N","full_name":"Arslan, Feyza N","id":"49DA7910-F248-11E8-B48F-1D18A9856A87"},{"id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","full_name":"Hannezo, Edouard B","orcid":"0000-0001-6005-1561","last_name":"Hannezo","first_name":"Edouard B"},{"id":"4515C308-F248-11E8-B48F-1D18A9856A87","full_name":"Merrin, Jack","last_name":"Merrin","first_name":"Jack","orcid":"0000-0001-5145-4609"},{"full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724"},{"full_name":"Heisenberg, Carl-Philipp J","id":"39427864-F248-11E8-B48F-1D18A9856A87","first_name":"Carl-Philipp J","last_name":"Heisenberg","orcid":"0000-0002-0912-4566"}],"project":[{"name":"Interaction and feedback between cell mechanics and fate specification in vertebrate gastrulation","call_identifier":"H2020","grant_number":"742573","_id":"260F1432-B435-11E9-9278-68D0E5697425"}],"doi":"10.1016/j.cub.2023.11.067","year":"2024","day":"08","page":"171-182.e8","scopus_import":"1","article_type":"original","ddc":["570"],"month":"01","title":"Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts","publication":"Current Biology","intvolume":"        34","file_date_updated":"2024-01-16T10:53:31Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","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.","isi":1,"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication_status":"published","publisher":"Elsevier","ec_funded":1,"oa_version":"Published Version","date_published":"2024-01-08T00:00:00Z","volume":34,"external_id":{"pmid":["38134934"],"isi":["001154500400001"]},"publication_identifier":{"issn":["0960-9822"],"eissn":["1879-0445"]},"citation":{"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>.","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.","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>.","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>","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.","short":"F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current Biology 34 (2024) 171–182.e8.","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>"},"department":[{"_id":"CaHe"},{"_id":"EdHa"},{"_id":"MaLo"},{"_id":"NanoFab"}],"pmid":1,"language":[{"iso":"eng"}],"has_accepted_license":"1","issue":"1","date_updated":"2025-09-04T11:39:10Z","article_processing_charge":"Yes (via OA deal)","_id":"14795"},{"article_type":"review","article_number":"151380","scopus_import":"1","day":"01","year":"2024","doi":"10.1016/j.ejcb.2023.151380","project":[{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"}],"author":[{"full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","first_name":"Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 "},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"title":"A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches","month":"03","ddc":["570"],"type":"journal_article","oa":1,"file":[{"success":1,"file_name":"2024_EJCB_Radler.pdf","content_type":"application/pdf","date_created":"2024-07-16T12:07:20Z","file_id":"17265","checksum":"5d170abbc87585205c010657e4552360","file_size":9995304,"access_level":"open_access","creator":"dernst","date_updated":"2024-07-16T12:07:20Z","relation":"main_file"}],"keyword":["Cell Biology","General Medicine","Histology","Pathology and Forensic Medicine"],"date_created":"2024-01-18T08:16:43Z","abstract":[{"lang":"eng","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."}],"status":"public","quality_controlled":"1","corr_author":"1","has_accepted_license":"1","language":[{"iso":"eng"}],"department":[{"_id":"MaLo"}],"pmid":1,"publication_identifier":{"issn":["0171-9335"]},"citation":{"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>.","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>","short":"P. Radler, M. Loose, European Journal of Cell Biology 103 (2024).","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.","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>.","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>"},"external_id":{"pmid":["38218128"],"isi":["001166216800001"]},"_id":"14834","article_processing_charge":"Yes","date_updated":"2025-09-04T11:45:31Z","issue":"1","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"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.","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","file_date_updated":"2024-07-16T12:07:20Z","intvolume":"       103","publication":"European Journal of Cell Biology","volume":103,"date_published":"2024-03-01T00:00:00Z","oa_version":"Published Version","publisher":"Elsevier","publication_status":"published"},{"issue":"8","date_updated":"2025-09-04T13:49:45Z","article_processing_charge":"Yes (via OA deal)","_id":"15330","external_id":{"pmid":["38506228"],"isi":["001266917100005"]},"citation":{"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>.","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.","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>","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>.","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>","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).","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."},"publication_identifier":{"eissn":["1477-9137"],"issn":["0021-9533"]},"pmid":1,"department":[{"_id":"MaLo"},{"_id":"JiFr"},{"_id":"CaBe"}],"OA_place":"publisher","OA_type":"hybrid","language":[{"iso":"eng"}],"has_accepted_license":"1","publication_status":"published","publisher":"The Company of Biologists","ec_funded":1,"oa_version":"Published Version","date_published":"2024-04-01T00:00:00Z","volume":137,"publication":"Journal of Cell Science","intvolume":"       137","file_date_updated":"2025-01-09T08:41:16Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","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).","isi":1,"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"ddc":["570"],"related_material":{"record":[{"id":"14591","status":"public","relation":"earlier_version"}]},"month":"04","title":"Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana","author":[{"orcid":"0000-0002-2198-0509","first_name":"Nataliia","last_name":"Gnyliukh","id":"390C1120-F248-11E8-B48F-1D18A9856A87","full_name":"Gnyliukh, Nataliia"},{"orcid":"0000-0002-2739-8843","last_name":"Johnson","first_name":"Alexander J","full_name":"Johnson, Alexander J","id":"46A62C3A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"MK","last_name":"Nagel","full_name":"Nagel, MK"},{"id":"2DB5D88C-D7B3-11E9-B8FD-7907E6697425","full_name":"Monzer, Aline","last_name":"Monzer","first_name":"Aline"},{"last_name":"Babic","first_name":"David","id":"db566d23-f6e0-11ea-865d-e6f270e968e7","full_name":"Babic, David"},{"id":"36062FEC-F248-11E8-B48F-1D18A9856A87","full_name":"Hlavata, Annamaria","last_name":"Hlavata","first_name":"Annamaria"},{"full_name":"Alotaibi, SS","last_name":"Alotaibi","first_name":"SS"},{"full_name":"Isono, E","first_name":"E","last_name":"Isono"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"id":"4159519E-F248-11E8-B48F-1D18A9856A87","full_name":"Friml, Jiří","last_name":"Friml","first_name":"Jiří","orcid":"0000-0002-8302-7596"}],"project":[{"name":"International IST Doctoral Program","_id":"2564DBCA-B435-11E9-9278-68D0E5697425","grant_number":"665385","call_identifier":"H2020"},{"name":"Peptide receptors for auxin canalization in Arabidopsis","_id":"bd76d395-d553-11ed-ba76-f678c14f9033","grant_number":"I06123"}],"year":"2024","doi":"10.1242/jcs.261720","day":"01","scopus_import":"1","article_number":"jcs.261720","article_type":"original","corr_author":"1","quality_controlled":"1","status":"public","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."}],"date_created":"2024-04-19T09:54:59Z","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"Bio"}],"file":[{"content_type":"application/pdf","date_created":"2025-01-09T08:41:16Z","file_name":"2024_JourCellScience_Gnyliukh.pdf","success":1,"relation":"main_file","date_updated":"2025-01-09T08:41:16Z","access_level":"open_access","creator":"dernst","file_size":25845948,"checksum":"6dc023f0cc7052ad3cf0a42589d2e30f","file_id":"18792"}],"oa":1,"type":"journal_article"},{"corr_author":"1","quality_controlled":"1","status":"public","abstract":[{"text":"Clathrin-mediated endocytosis (CME) is an essential process of cargo uptake operating in all eukaryotes. In animals and yeast, BAR-SH3 domain proteins, endophilins and amphiphysins, function at the conclusion of CME to recruit factors for vesicle scission and uncoating. Arabidopsis thaliana contains the BAR-SH3 domain proteins SH3P1–SH3P3, but their role is poorly understood. Here, we identify SH3Ps as functional homologs of endophilin/amphiphysin. SH3P1–SH3P3 bind to discrete foci at the plasma membrane (PM), and SH3P2 recruits late to a subset of clathrin-coated pits. The SH3P2 PM recruitment pattern is nearly identical to its interactor, a putative uncoating factor, AUXILIN-LIKE1. Notably, SH3P1–SH3P3 are required for most of AUXILIN-LIKE1 recruitment to the PM. This indicates a plant-specific modification of CME, where BAR-SH3 proteins recruit auxilin-like uncoating factors rather than the uncoating phosphatases, synaptojanins. SH3P1–SH3P3 act redundantly in overall CME with the plant-specific endocytic adaptor TPLATE complex but not due to an SH3 domain in its TASH3 subunit.","lang":"eng"}],"date_created":"2024-05-12T22:01:01Z","file":[{"relation":"main_file","creator":"dernst","access_level":"open_access","date_updated":"2024-05-13T12:11:22Z","checksum":"a06bb85be4fc765c51554d27ee2da802","file_size":5698598,"file_id":"15387","file_name":"2024_CellReports_Adamowski.pdf","content_type":"application/pdf","date_created":"2024-05-13T12:11:22Z","success":1}],"oa":1,"type":"journal_article","ddc":["580"],"month":"05","title":"SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis","author":[{"full_name":"Adamowski, Maciek","id":"45F536D2-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6463-5257","last_name":"Adamowski","first_name":"Maciek"},{"id":"6ac4636d-15b2-11ec-abd3-fb8df79972ae","full_name":"Randuch, Marek","first_name":"Marek","last_name":"Randuch"},{"id":"83c17ce3-15b2-11ec-abd3-f486545870bd","full_name":"Matijevic, Ivana","last_name":"Matijevic","first_name":"Ivana"},{"id":"44BF24D0-F248-11E8-B48F-1D18A9856A87","full_name":"Narasimhan, Madhumitha","orcid":"0000-0002-8600-0671","last_name":"Narasimhan","first_name":"Madhumitha"},{"full_name":"Friml, Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8302-7596","last_name":"Friml","first_name":"Jiří"}],"project":[{"name":"Molecular mechanisms of endocytic cargo recognition in plants","call_identifier":"FWF","grant_number":"I03630","_id":"26538374-B435-11E9-9278-68D0E5697425"}],"doi":"10.1016/j.celrep.2024.114195","year":"2024","day":"28","scopus_import":"1","article_number":"114195","article_type":"original","publication_status":"published","publisher":"Cell Press","oa_version":"Published Version","date_published":"2024-05-28T00:00:00Z","volume":43,"publication":"Cell Reports","intvolume":"        43","file_date_updated":"2024-05-13T12:11:22Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","acknowledgement":"The authors wish to acknowledge Dr. Daniel van Damme for mRuby3/pDONRP2rP3 and Prof. Qi-Jun Chen for sharing plasmids used for CRISPR-Cas9 mutagenesis. This work was supported by the Austrian Science Fund (FWF): I 3630-B25.","isi":1,"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"issue":"5","date_updated":"2025-09-08T07:23:07Z","article_processing_charge":"Yes","_id":"15374","external_id":{"pmid":["38717900"],"isi":["001240362800001"]},"publication_identifier":{"eissn":["2211-1247"]},"citation":{"ista":"Adamowski M, Randuch M, Matijevic I, Narasimhan M, Friml J. 2024. SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. Cell Reports. 43(5), 114195.","short":"M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, J. Friml, Cell Reports 43 (2024).","mla":"Adamowski, Maciek, et al. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors for Clathrin-Mediated Endocytosis.” <i>Cell Reports</i>, vol. 43, no. 5, 114195, Cell Press, 2024, doi:<a href=\"https://doi.org/10.1016/j.celrep.2024.114195\">10.1016/j.celrep.2024.114195</a>.","ama":"Adamowski M, Randuch M, Matijevic I, Narasimhan M, Friml J. SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. <i>Cell Reports</i>. 2024;43(5). doi:<a href=\"https://doi.org/10.1016/j.celrep.2024.114195\">10.1016/j.celrep.2024.114195</a>","apa":"Adamowski, M., Randuch, M., Matijevic, I., Narasimhan, M., &#38; Friml, J. (2024). SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2024.114195\">https://doi.org/10.1016/j.celrep.2024.114195</a>","ieee":"M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, and J. Friml, “SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis,” <i>Cell Reports</i>, vol. 43, no. 5. Cell Press, 2024.","chicago":"Adamowski, Maciek, Marek Randuch, Ivana Matijevic, Madhumitha Narasimhan, and Jiří Friml. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors for Clathrin-Mediated Endocytosis.” <i>Cell Reports</i>. Cell Press, 2024. <a href=\"https://doi.org/10.1016/j.celrep.2024.114195\">https://doi.org/10.1016/j.celrep.2024.114195</a>."},"pmid":1,"department":[{"_id":"JiFr"},{"_id":"MaLo"}],"language":[{"iso":"eng"}],"has_accepted_license":"1"},{"ddc":["570"],"month":"10","title":"Self-organization of mortal filaments and its role in bacterial division ring formation","doi":"10.1038/s41567-024-02597-8","year":"2024","project":[{"grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","name":"In vitro reconstitution of bacterial cell division"},{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines"}],"author":[{"id":"3adeca52-9313-11ed-b1ac-c170b2505714","full_name":"Vanhille-Campos, Christian Eduardo","first_name":"Christian Eduardo","last_name":"Vanhille-Campos"},{"first_name":"Kevin D.","last_name":"Whitley","full_name":"Whitley, Kevin D."},{"first_name":"Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 ","full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Holden, Séamus","last_name":"Holden","first_name":"Séamus"},{"full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela","orcid":"0000-0002-7854-2139"}],"scopus_import":"1","page":"1670-1678","day":"01","article_type":"original","corr_author":"1","quality_controlled":"1","status":"public","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"}],"date_created":"2024-08-25T22:01:08Z","oa":1,"file":[{"success":1,"content_type":"application/pdf","date_created":"2025-04-14T06:06:35Z","file_name":"2024_NaturePhysics_VanhilleCampos.pdf","date_updated":"2025-04-14T06:06:35Z","access_level":"open_access","creator":"dernst","relation":"main_file","file_id":"19556","file_size":8058249,"checksum":"c4842152e2b90d67f48ea8c9ed7c473b"}],"type":"journal_article","article_processing_charge":"Yes (in subscription journal)","date_updated":"2025-09-08T09:02:20Z","_id":"17460","external_id":{"isi":["001289394500005"],"pmid":["39416851"]},"pmid":1,"department":[{"_id":"AnSa"},{"_id":"MaLo"}],"publication_identifier":{"eissn":["1745-2481"],"issn":["1745-2473"]},"citation":{"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>.","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.","short":"C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić, Nature Physics 20 (2024) 1670–1678.","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>.","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>","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>"},"has_accepted_license":"1","language":[{"iso":"eng"}],"OA_type":"hybrid","OA_place":"publisher","publisher":"Springer Nature","publication_status":"published","APC_amount":"12348 EUR","oa_version":"Published Version","ec_funded":1,"date_published":"2024-10-01T00:00:00Z","volume":20,"publication":"Nature Physics","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"        20","file_date_updated":"2025-04-14T06:06:35Z","isi":1,"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.).","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"}},{"publication_status":"published","publisher":"Springer Nature","date_published":"2024-03-04T00:00:00Z","volume":9,"oa_version":"None","intvolume":"         9","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication":"Nature Microbiology","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.","isi":1,"issue":"3","_id":"15118","date_updated":"2026-04-07T12:27:57Z","article_processing_charge":"No","citation":{"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.","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.","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>.","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>","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>."},"publication_identifier":{"eissn":["2058-5276"]},"pmid":1,"department":[{"_id":"MaLo"}],"external_id":{"pmid":["38443575"],"isi":["001183270800021"]},"language":[{"iso":"eng"}],"status":"public","quality_controlled":"1","date_created":"2024-03-17T23:00:58Z","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."}],"type":"journal_article","acknowledged_ssus":[{"_id":"LifeSc"}],"related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"20741"}]},"title":"Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division","month":"03","day":"04","page":"698-711","scopus_import":"1","project":[{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"}],"author":[{"full_name":"Nußbaum, Phillip","last_name":"Nußbaum","first_name":"Phillip"},{"first_name":"Danguole","last_name":"Kureisaite-Ciziene","full_name":"Kureisaite-Ciziene, Danguole"},{"last_name":"Bellini","first_name":"Dom","full_name":"Bellini, Dom"},{"full_name":"Van Der Does, Chris","first_name":"Chris","last_name":"Van Der Does"},{"full_name":"Kojic, Marko","id":"73e7ecd4-dc85-11ea-9058-88a16394b160","last_name":"Kojic","first_name":"Marko","orcid":"0000-0001-7244-8128"},{"last_name":"Taib","first_name":"Najwa","full_name":"Taib, Najwa"},{"full_name":"Yeates, Anna","first_name":"Anna","last_name":"Yeates"},{"first_name":"Maxime","last_name":"Tourte","full_name":"Tourte, Maxime"},{"last_name":"Gribaldo","first_name":"Simonetta","full_name":"Gribaldo, Simonetta"},{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"},{"full_name":"Löwe, Jan","last_name":"Löwe","first_name":"Jan"},{"full_name":"Albers, Sonja Verena","first_name":"Sonja Verena","last_name":"Albers"}],"year":"2024","doi":"10.1038/s41564-024-01600-5","article_type":"original"},{"date_created":"2023-01-12T12:09:58Z","abstract":[{"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.","lang":"eng"}],"type":"journal_article","keyword":["Cell Biology","Genetics","Molecular Biology","Biochemistry","Structural Biology","Biophysics"],"file":[{"checksum":"7492244d3f9c5faa1347ef03f6e5bc84","file_size":3148143,"file_id":"14063","relation":"main_file","access_level":"open_access","creator":"dernst","date_updated":"2023-08-16T08:31:04Z","file_name":"2023_FEBSLetters_Loose.pdf","date_created":"2023-08-16T08:31:04Z","content_type":"application/pdf","success":1}],"oa":1,"corr_author":"1","status":"public","quality_controlled":"1","day":"01","scopus_import":"1","page":"762-777","author":[{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"},{"full_name":"Auer, Albert","id":"3018E8C2-F248-11E8-B48F-1D18A9856A87","first_name":"Albert","last_name":"Auer","orcid":"0000-0002-3580-2906"},{"first_name":"Gabriel","last_name":"Brognara","id":"D96FFDA0-A884-11E9-9968-DC26E6697425","full_name":"Brognara, Gabriel"},{"id":"55380f95-15b2-11ec-abd3-aff8e230696b","full_name":"Budiman, Hanifatul R","last_name":"Budiman","first_name":"Hanifatul R"},{"full_name":"Kowalski, Lukasz M","id":"e3a512e2-4bbe-11eb-a68a-e3857a7844c2","first_name":"Lukasz M","last_name":"Kowalski"},{"full_name":"Matijevic, Ivana","id":"83c17ce3-15b2-11ec-abd3-f486545870bd","first_name":"Ivana","last_name":"Matijevic"}],"year":"2023","doi":"10.1002/1873-3468.14540","article_type":"review","ddc":["570"],"title":"In vitro reconstitution of small GTPase regulation","month":"03","intvolume":"       597","file_date_updated":"2023-08-16T08:31:04Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"FEBS Letters","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"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.","isi":1,"publication_status":"published","publisher":"Wiley","volume":597,"date_published":"2023-03-01T00:00:00Z","oa_version":"Published Version","publication_identifier":{"issn":["0014-5793"],"eissn":["1873-3468"]},"citation":{"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>.","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.","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>.","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.","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>"},"department":[{"_id":"MaLo"}],"pmid":1,"external_id":{"pmid":["36448231"],"isi":["000891573000001"]},"language":[{"iso":"eng"}],"has_accepted_license":"1","issue":"6","_id":"12163","date_updated":"2024-10-09T21:03:42Z","article_processing_charge":"Yes (via OA deal)"},{"scopus_import":"1","page":"1315-1332","day":"07","year":"2023","doi":"10.1016/j.devcel.2023.06.001","author":[{"last_name":"Leonard","first_name":"Thomas A.","full_name":"Leonard, Thomas A."},{"orcid":"0000-0001-7309-9724","last_name":"Loose","first_name":"Martin","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Martens","first_name":"Sascha","full_name":"Martens, Sascha"}],"project":[{"name":"In vitro reconstitution of bacterial cell division","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607"},{"name":"Synthetic and structural biology of Rab GTPase networks","_id":"bd6ae2ca-d553-11ed-ba76-a4aa239da5ee","grant_number":"101045340"}],"article_type":"original","ddc":["570"],"title":"The membrane surface as a platform that organizes cellular and biochemical processes","month":"08","date_created":"2023-08-13T22:01:12Z","abstract":[{"lang":"eng","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."}],"type":"journal_article","oa":1,"file":[{"content_type":"application/pdf","date_created":"2023-08-14T07:57:55Z","file_name":"2023_DevelopmentalCell_Leonard.pdf","success":1,"relation":"main_file","date_updated":"2023-08-14T07:57:55Z","creator":"dernst","access_level":"open_access","file_size":3184217,"checksum":"d8c5dc97cd40c26da2ec98ae723ab368","file_id":"14049"}],"corr_author":"1","status":"public","quality_controlled":"1","pmid":1,"department":[{"_id":"MaLo"}],"citation":{"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>","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.","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>","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>.","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.","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>."},"publication_identifier":{"issn":["1534-5807"],"eissn":["1878-1551"]},"external_id":{"pmid":["37419118"],"isi":["001059110400001"]},"has_accepted_license":"1","language":[{"iso":"eng"}],"issue":"15","_id":"14039","article_processing_charge":"Yes (via OA deal)","date_updated":"2024-10-22T11:40:18Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file_date_updated":"2023-08-14T07:57:55Z","intvolume":"        58","publication":"Developmental Cell","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"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.","publisher":"Elsevier","publication_status":"published","date_published":"2023-08-07T00:00:00Z","volume":58,"oa_version":"Published Version"},{"quality_controlled":"1","status":"public","file":[{"checksum":"d09ebb68fee61f4e2e09ec286c9cf1d3","file_size":1518350,"file_id":"14810","relation":"main_file","access_level":"open_access","creator":"dernst","date_updated":"2024-01-16T09:42:10Z","file_name":"2023_EnvirMicroBiolReports_Nies.pdf","content_type":"application/pdf","date_created":"2024-01-16T09:42:10Z","success":1}],"oa":1,"keyword":["Agricultural and Biological Sciences (miscellaneous)","Ecology","Evolution","Behavior and Systematics"],"type":"journal_article","abstract":[{"text":"Small cryptic plasmids have no clear effect on the host fitness and their functional repertoire remains obscure. The naturally competent cyanobacterium Synechocystis sp. PCC 6803 harbours several small cryptic plasmids; whether their evolution with this species is supported by horizontal transfer remains understudied. Here, we show that the small cryptic plasmid DNA is transferred in the population exclusively by natural transformation, where the transfer frequency of plasmid‐encoded genes is similar to that of chromosome‐encoded genes. Establishing a system to follow gene transfer, we compared the transfer frequency of genes encoded in cryptic plasmids pCA2.4 (2378 bp) and pCB2.4 (2345 bp) within and between populations of two <jats:italic>Synechocystis</jats:italic> sp. PCC 6803 labtypes (termed Kiel and Sevilla). Our results reveal that plasmid gene transfer frequency depends on the recipient labtype. Furthermore, gene transfer via whole plasmid uptake in the Sevilla labtype ranged among the lowest detected transfer rates in our experiments. Our study indicates that horizontal DNA transfer via natural transformation is frequent in the evolution of small cryptic plasmids that reside in naturally competent organisms. Furthermore, we suggest that the contribution of natural transformation to cryptic plasmid persistence in Synechocystis is limited.","lang":"eng"}],"date_created":"2024-01-10T10:41:07Z","month":"12","title":"Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803","ddc":["570"],"article_type":"original","year":"2023","doi":"10.1111/1758-2229.13203","author":[{"full_name":"Nies, Fabian","first_name":"Fabian","last_name":"Nies"},{"full_name":"Wein, Tanita","last_name":"Wein","first_name":"Tanita"},{"full_name":"Hanke, Dustin M.","first_name":"Dustin M.","last_name":"Hanke"},{"orcid":"0000-0002-3461-5391","last_name":"Springstein","first_name":"Benjamin L","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","full_name":"Springstein, Benjamin L"},{"full_name":"Alcorta, Jaime","last_name":"Alcorta","first_name":"Jaime"},{"full_name":"Taubenheim, Claudia","last_name":"Taubenheim","first_name":"Claudia"},{"first_name":"Tal","last_name":"Dagan","full_name":"Dagan, Tal"}],"page":"656-668","day":"01","oa_version":"Published Version","date_published":"2023-12-01T00:00:00Z","volume":15,"publisher":"Wiley","publication_status":"published","isi":1,"acknowledgement":"We thank the lab of Francisco Javier Florencio Bel-lido, Sevilla, Spain for supplying theSynechocystislabtype Sevilla used in this work and the lab of MartinHagemann, Rostock, Germany for supplying the pIGAplasmidusedinthiswork.WethankNilsHülterforfruitful discussions. We thank Fenna Stücker forgraphical illustrations and Katrin Schumann, FennaStücker,  and  Lidusha  Manivannan  for  technicalsupport.\r\nChilean National Agency for Research andDevelopment (ANID), Grant/Award Number:21191763; DeutscheForschungsgemeinschaft, Grant/AwardNumbers: 456882089, RTG2501; EuropeanResearch Council (ERC), Grant/AwardNumber: 101043835","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication":"Environmental Microbiology Reports","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file_date_updated":"2024-01-16T09:42:10Z","intvolume":"        15","article_processing_charge":"Yes (in subscription journal)","date_updated":"2024-01-16T09:46:12Z","_id":"14785","issue":"6","has_accepted_license":"1","language":[{"iso":"eng"}],"external_id":{"isi":["001080203100001"],"pmid":["37794696"]},"department":[{"_id":"MaLo"}],"pmid":1,"citation":{"apa":"Nies, F., Wein, T., Hanke, D. M., Springstein, B. L., Alcorta, J., Taubenheim, C., &#38; Dagan, T. (2023). Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803. <i>Environmental Microbiology Reports</i>. Wiley. <a href=\"https://doi.org/10.1111/1758-2229.13203\">https://doi.org/10.1111/1758-2229.13203</a>","short":"F. Nies, T. Wein, D.M. Hanke, B.L. Springstein, J. Alcorta, C. Taubenheim, T. Dagan, Environmental Microbiology Reports 15 (2023) 656–668.","ista":"Nies F, Wein T, Hanke DM, Springstein BL, Alcorta J, Taubenheim C, Dagan T. 2023. Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803. Environmental Microbiology Reports. 15(6), 656–668.","ama":"Nies F, Wein T, Hanke DM, et al. Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803. <i>Environmental Microbiology Reports</i>. 2023;15(6):656-668. doi:<a href=\"https://doi.org/10.1111/1758-2229.13203\">10.1111/1758-2229.13203</a>","mla":"Nies, Fabian, et al. “Role of Natural Transformation in the Evolution of Small Cryptic Plasmids in Synechocystis Sp. PCC 6803.” <i>Environmental Microbiology Reports</i>, vol. 15, no. 6, Wiley, 2023, pp. 656–68, doi:<a href=\"https://doi.org/10.1111/1758-2229.13203\">10.1111/1758-2229.13203</a>.","ieee":"F. Nies <i>et al.</i>, “Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803,” <i>Environmental Microbiology Reports</i>, vol. 15, no. 6. Wiley, pp. 656–668, 2023.","chicago":"Nies, Fabian, Tanita Wein, Dustin M. Hanke, Benjamin L Springstein, Jaime Alcorta, Claudia Taubenheim, and Tal Dagan. “Role of Natural Transformation in the Evolution of Small Cryptic Plasmids in Synechocystis Sp. PCC 6803.” <i>Environmental Microbiology Reports</i>. Wiley, 2023. <a href=\"https://doi.org/10.1111/1758-2229.13203\">https://doi.org/10.1111/1758-2229.13203</a>."},"publication_identifier":{"eissn":["1758-2229"]}},{"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"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). ","file_date_updated":"2023-08-08T11:17:28Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2023-07-26T00:00:00Z","ec_funded":1,"oa_version":"Published Version","publisher":"Institute of Science and Technology Austria","has_accepted_license":"1","citation":{"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>.","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>","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).","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>.","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.” 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."},"department":[{"_id":"MaLo"},{"_id":"EdHa"},{"_id":"JoDa"}],"_id":"13116","date_updated":"2026-03-17T12:02:11Z","article_processing_charge":"No","type":"research_data","oa":1,"file":[{"success":1,"file_name":"ReadMe File.docx","date_created":"2023-08-08T11:17:28Z","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","access_level":"open_access","creator":"pradler","date_updated":"2023-08-08T11:17:28Z","relation":"main_file","file_id":"13983","checksum":"4b4ec5d4df7672b3af5ba23b126b171b","file_size":13111},{"date_updated":"2023-07-25T06:55:43Z","creator":"pradler","access_level":"open_access","relation":"main_file","file_id":"13298","file_size":1499504777,"checksum":"6f1673d6ae4f547cd49cfe7f87d9ab7e","success":1,"date_created":"2023-07-25T06:55:43Z","content_type":"application/octet-stream","file_name":"TIRF_FtsZ WT 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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. ","lang":"eng"}],"status":"public","corr_author":"1","day":"26","project":[{"name":"Self-Organization of the Bacterial Cell","_id":"2595697A-B435-11E9-9278-68D0E5697425","grant_number":"679239","call_identifier":"H2020"},{"_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607","name":"In vitro reconstitution of bacterial cell division"},{"name":"Motile active matter models of migrating cells and chiral filaments","_id":"34d75525-11ca-11ed-8bc3-89b6307fee9d","grant_number":"26360"}],"author":[{"last_name":"Dunajova","first_name":"Zuzana","full_name":"Dunajova, Zuzana","id":"4B39F286-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Prats Mateu","first_name":"Batirtze","full_name":"Prats Mateu, Batirtze","id":"299FE892-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Radler","first_name":"Philipp","orcid":"0000-0001-9198-2182 ","full_name":"Radler, Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Lim, Keesiang","first_name":"Keesiang","last_name":"Lim"},{"first_name":"Dörte","last_name":"Brandis","full_name":"Brandis, Dörte"},{"full_name":"Velicky, Philipp","id":"39BDC62C-F248-11E8-B48F-1D18A9856A87","first_name":"Philipp","last_name":"Velicky","orcid":"0000-0002-2340-7431"},{"full_name":"Danzl, Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","last_name":"Danzl","first_name":"Johann G","orcid":"0000-0001-8559-3973"},{"full_name":"Wong, Richard W.","last_name":"Wong","first_name":"Richard W."},{"first_name":"Jens","last_name":"Elgeti","full_name":"Elgeti, Jens"},{"orcid":"0000-0001-6005-1561","last_name":"Hannezo","first_name":"Edouard B","id":"3A9DB764-F248-11E8-B48F-1D18A9856A87","full_name":"Hannezo, Edouard B"},{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"doi":"10.15479/AT:ISTA:13116","year":"2023","title":"Chiral and nematic phases of flexible active filaments","month":"07","related_material":{"record":[{"status":"public","relation":"used_in_publication","id":"13314"},{"relation":"used_in_publication","status":"public","id":"21423"}]},"ddc":["539"]},{"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"        19","file_date_updated":"2024-01-30T14:28:30Z","publication":"Nature Physics","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"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).","publisher":"Springer Nature","publication_status":"published","date_published":"2023-12-01T00:00:00Z","volume":19,"oa_version":"Published Version","ec_funded":1,"pmid":1,"department":[{"_id":"JoDa"},{"_id":"EdHa"},{"_id":"MaLo"},{"_id":"GradSch"}],"citation":{"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>.","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.","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>","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>.","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>"},"publication_identifier":{"eissn":["1745-2481"],"issn":["1745-2473"]},"external_id":{"isi":["001178645300041"],"pmid":["38075437"]},"has_accepted_license":"1","language":[{"iso":"eng"}],"_id":"13314","article_processing_charge":"Yes (in subscription journal)","date_updated":"2026-03-18T14:11:35Z","date_created":"2023-07-27T14:44:45Z","abstract":[{"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.","lang":"eng"}],"type":"journal_article","oa":1,"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"file":[{"file_id":"14916","checksum":"bc7673ca07d37309013a86166577b2f7","file_size":22471673,"creator":"dernst","access_level":"open_access","date_updated":"2024-01-30T14:28:30Z","relation":"main_file","success":1,"file_name":"2023_NaturePhysics_Dunajova.pdf","content_type":"application/pdf","date_created":"2024-01-30T14:28:30Z"}],"corr_author":"1","status":"public","quality_controlled":"1","page":"1916-1926","scopus_import":"1","day":"01","year":"2023","doi":"10.1038/s41567-023-02218-w","author":[{"first_name":"Zuzana","last_name":"Dunajova","id":"4B39F286-F248-11E8-B48F-1D18A9856A87","full_name":"Dunajova, Zuzana"},{"last_name":"Prats Mateu","first_name":"Batirtze","id":"299FE892-F248-11E8-B48F-1D18A9856A87","full_name":"Prats Mateu, Batirtze"},{"last_name":"Radler","first_name":"Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","full_name":"Radler, Philipp"},{"full_name":"Lim, Keesiang","first_name":"Keesiang","last_name":"Lim"},{"first_name":"Dörte","last_name":"Brandis","id":"21d64d35-f128-11eb-9611-b8bcca7a12fd","full_name":"Brandis, Dörte"},{"orcid":"0000-0002-2340-7431","last_name":"Velicky","first_name":"Philipp","id":"39BDC62C-F248-11E8-B48F-1D18A9856A87","full_name":"Velicky, Philipp"},{"id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","full_name":"Danzl, Johann G","orcid":"0000-0001-8559-3973","last_name":"Danzl","first_name":"Johann G"},{"full_name":"Wong, Richard W.","first_name":"Richard W.","last_name":"Wong"},{"first_name":"Jens","last_name":"Elgeti","full_name":"Elgeti, Jens"},{"first_name":"Edouard B","last_name":"Hannezo","orcid":"0000-0001-6005-1561","full_name":"Hannezo, Edouard B","id":"3A9DB764-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}],"project":[{"_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","grant_number":"679239","name":"Self-Organization of the Bacterial Cell"},{"name":"In vitro reconstitution of bacterial cell division","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607"},{"grant_number":"26360","_id":"34d75525-11ca-11ed-8bc3-89b6307fee9d","name":"Motile active matter models of migrating cells and chiral filaments"}],"article_type":"original","related_material":{"record":[{"status":"public","relation":"research_data","id":"13116"},{"relation":"dissertation_contains","status":"public","id":"21423"},{"status":"public","relation":"research_data","id":"21439"}]},"ddc":["530"],"title":"Chiral and nematic phases of flexible active filaments","month":"12"},{"page":"156","day":"25","year":"2023","doi":"10.15479/at:ista:14280","author":[{"first_name":"Philipp","last_name":"Radler","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","full_name":"Radler, Philipp"}],"project":[{"grant_number":"679239","call_identifier":"H2020","_id":"2595697A-B435-11E9-9278-68D0E5697425","name":"Self-Organization of the Bacterial Cell"},{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"},{"grant_number":"ALTF 2015-1163","_id":"2596EAB6-B435-11E9-9278-68D0E5697425","name":"Synthesis of bacterial cell wall"},{"name":"Reconstitution of bacterial cell wall synthesis","_id":"259B655A-B435-11E9-9278-68D0E5697425","grant_number":"LT000824/2016"}],"related_material":{"record":[{"id":"10934","relation":"research_data","status":"public"},{"id":"11373","status":"public","relation":"part_of_dissertation"},{"id":"7387","relation":"part_of_dissertation","status":"public"}]},"degree_awarded":"PhD","ddc":["572"],"title":"Spatiotemporal signaling during assembly of the bacterial divisome","month":"09","date_created":"2023-09-06T10:58:25Z","abstract":[{"text":"Cell division in Escherichia coli is performed by the divisome, a multi-protein complex composed of more than 30 proteins. The divisome spans from the cytoplasm through the inner membrane to the cell wall and the outer membrane. Divisome assembly is initiated by a cytoskeletal structure, the so-called Z-ring, which localizes at the center of the E. coli cell and determines the position of the future cell septum. The Z-ring is composed of the highly conserved bacterial tubulin homologue FtsZ, which forms treadmilling filaments. These filaments are recruited to the inner membrane by FtsA, a highly conserved bacterial actin homologue. FtsA interacts with other proteins in the periplasm and thus connects the cytoplasmic and periplasmic components of the divisome. \r\nA previous model postulated that FtsA regulates maturation of the divisome by switching from an oligomeric, inactive state to a monomeric and active state. This model was based mostly on in vivo studies, as a biochemical characterization of FtsA has been hampered by difficulties in purifying the protein. Here, we studied FtsA using an in vitro reconstitution approach and aimed to answer two questions: (i) How are dynamics from cytoplasmic, treadmilling FtsZ filaments coupled to proteins acting in the periplasmic space and (ii) How does FtsA regulate the maturation of the divisome?\r\nWe found that the cytoplasmic peptides of the transmembrane proteins FtsN and FtsQ interact directly with FtsA and can follow the spatiotemporal signal of FtsA/Z filaments. When we investigated the underlying mechanism by imaging single molecules of FtsNcyto, we found the peptide to interact transiently with FtsA. An in depth analysis of the single molecule trajectories helped to postulate a model where PG synthases follow the dynamics of FtsZ by a diffusion and capture mechanism. \r\nFollowing up on these findings we were interested in how the self-interaction of FtsA changes when it encounters FtsNcyto and if we can confirm the proposed oligomer-monomer switch. For this, we compared the behavior of the previously identified, hyperactive mutant FtsA R286W with wildtype FtsA. The mutant outperforms WT in mirroring and transmitting the spatiotemporal signal of treadmilling FtsZ filaments. Surprisingly however, we found that this was not due to a difference in the self-interaction strength of the two variants, but a difference in their membrane residence time. Furthermore, in contrast to our expectations, upon binding of FtsNcyto the measured self-interaction of FtsA actually increased. \r\nWe propose that FtsNcyto induces a rearrangement of the oligomeric architecture of FtsA. In further consequence this change leads to more persistent FtsZ filaments which results in a defined signalling zone, allowing formation of the mature divisome. The observed difference between FtsA WT and R286W is due to the vastly different membrane turnover of the proteins. R286W cycles 5-10x faster compared to WT which allows to sample FtsZ filaments at faster frequencies. These findings can explain the observed differences in toxicity for overexpression of FtsA WT and R286W and help to understand how FtsA regulates divisome maturation.","lang":"eng"}],"type":"dissertation","oa":1,"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"file":[{"checksum":"87eef11fbc5c7df0826f12a3a629b444","file_size":114932847,"file_id":"14390","relation":"source_file","access_level":"closed","creator":"pradler","date_updated":"2024-10-05T22:30:03Z","file_name":"PhD Thesis_Philipp Radler_20231004.docx","date_created":"2023-10-04T10:11:53Z","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","embargo_to":"open_access"},{"file_size":37838778,"checksum":"3253e099b7126469d941fd9419d68b4f","file_id":"14391","relation":"main_file","date_updated":"2024-10-05T22:30:03Z","creator":"pradler","access_level":"open_access","date_created":"2023-10-04T10:11:21Z","content_type":"application/pdf","file_name":"PhD Thesis_Philipp Radler_20231004.pdf","embargo":"2024-10-04"}],"keyword":["Cell Division","Reconstitution","FtsZ","FtsA","Divisome","E.coli"],"corr_author":"1","status":"public","department":[{"_id":"GradSch"},{"_id":"MaLo"}],"citation":{"chicago":"Radler, Philipp. “Spatiotemporal Signaling during Assembly of the Bacterial Divisome.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/at:ista:14280\">https://doi.org/10.15479/at:ista:14280</a>.","ieee":"P. Radler, “Spatiotemporal signaling during assembly of the bacterial divisome,” Institute of Science and Technology Austria, 2023.","mla":"Radler, Philipp. <i>Spatiotemporal Signaling during Assembly of the Bacterial Divisome</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/at:ista:14280\">10.15479/at:ista:14280</a>.","ama":"Radler P. Spatiotemporal signaling during assembly of the bacterial divisome. 2023. doi:<a href=\"https://doi.org/10.15479/at:ista:14280\">10.15479/at:ista:14280</a>","short":"P. Radler, Spatiotemporal Signaling during Assembly of the Bacterial Divisome, Institute of Science and Technology Austria, 2023.","ista":"Radler P. 2023. Spatiotemporal signaling during assembly of the bacterial divisome. Institute of Science and Technology Austria.","apa":"Radler, P. (2023). <i>Spatiotemporal signaling during assembly of the bacterial divisome</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/at:ista:14280\">https://doi.org/10.15479/at:ista:14280</a>"},"publication_identifier":{"isbn":["978-3-99078-033-6"],"issn":["2663-337X"]},"has_accepted_license":"1","language":[{"iso":"eng"}],"OA_place":"publisher","_id":"14280","article_processing_charge":"No","date_updated":"2026-04-07T14:06:05Z","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","file_date_updated":"2024-10-05T22:30:03Z","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"supervisor":[{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724"}],"alternative_title":["ISTA Thesis"],"publisher":"Institute of Science and Technology Austria","publication_status":"published","date_published":"2023-09-25T00:00:00Z","oa_version":"Published Version","ec_funded":1},{"file_date_updated":"2024-11-23T23:30:38Z","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","alternative_title":["ISTA Thesis"],"supervisor":[{"first_name":"Jiří","last_name":"Friml","orcid":"0000-0002-8302-7596","id":"4159519E-F248-11E8-B48F-1D18A9856A87","full_name":"Friml, Jiří"},{"full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin","last_name":"Loose"}],"tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"publication_status":"published","publisher":"Institute of Science and Technology Austria","ec_funded":1,"oa_version":"Published Version","date_published":"2023-11-10T00:00:00Z","publication_identifier":{"isbn":["978-3-99078-037-4"],"issn":["2663-337X"]},"citation":{"chicago":"Gnyliukh, Nataliia. “Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/at:ista:14510\">https://doi.org/10.15479/at:ista:14510</a>.","ieee":"N. Gnyliukh, “Mechanism of clathrin-coated vesicle  formation during endocytosis in plants,” Institute of Science and Technology Austria, 2023.","apa":"Gnyliukh, N. (2023). <i>Mechanism of clathrin-coated vesicle  formation during endocytosis in plants</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/at:ista:14510\">https://doi.org/10.15479/at:ista:14510</a>","ama":"Gnyliukh N. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. 2023. doi:<a href=\"https://doi.org/10.15479/at:ista:14510\">10.15479/at:ista:14510</a>","mla":"Gnyliukh, Nataliia. <i>Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/at:ista:14510\">10.15479/at:ista:14510</a>.","ista":"Gnyliukh N. 2023. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. Institute of Science and Technology Austria.","short":"N. Gnyliukh, Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants, Institute of Science and Technology Austria, 2023."},"department":[{"_id":"GradSch"},{"_id":"JiFr"},{"_id":"MaLo"}],"OA_place":"publisher","language":[{"iso":"eng"}],"has_accepted_license":"1","date_updated":"2026-04-29T22:30:32Z","article_processing_charge":"No","_id":"14510","abstract":[{"lang":"eng","text":"Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth and\r\ndevelopment by controlling plasma membrane protein composition and cargo uptake. CME\r\nrelies on the precise recruitment control of protein regulators for vesicle maturation and\r\nrelease. During the early stages of endocytosis, an area of flat membrane is remodelled by\r\nproteins to create a spherical vesicle against intracellular forces. After the Clathrin-coated\r\nvesicle (CCV) is fully formed, scission machinery releases it from the plasma membrane,\r\nand cargo proceeds for recycling or degradation through early endosomes / Trans Golgi\r\nnetwork. Protein machineries that mediate membrane bending and vesicle release in plants\r\nare unknown. However, studies show, that plant endocytosis is actin independent, thus\r\nindicating that plants utilize a unique mechanism to mediate membrane bending against highturgor pressure compared to other model systems. First, by using biochemical and advanced\r\nlive microscopy approaches we investigate the TPLATE complex, a plant-specific\r\nendocytosis protein complex. We found that TPLATE is peripherally associated with\r\nclathrin-coated vesicles and localises at the rim of endocytosis events. Next, our study of\r\nplant Dynamin-related protein 1C (DRP1C), which was hypothesised previously to play a\r\nrole in vesicle release, shows the recruitment of the protein already at the early stages of\r\nendocytosis. Moreover, DRP1C assembles into organised ring-like structures and is able to\r\ninduce membrane deformation and tubulation, suggesting its role also in membrane bending\r\nduring early CME. Based on the data from mammalian and yeast systems, plant DynaminRelated Proteins 2 and SH3P2 protein are strong candidates to be part of the plant vesicle\r\nscission machinery; however, their precise role in plant CME has not been yet elucidated.\r\nHere, we characterised DRP2s and SH3P2 roles in CME by combining high-resolution\r\nimaging of endocytic events in vivo and protein characterisation. Although DRP2s and\r\nSH3P2 arrive together during late CME and physically interact, genetic analysis using\r\n∆sh3p1,2,3 mutant and complementation with non-DRP2-interacting SH3P2 variants suggest\r\nthat SH3P2 does not directly recruit DRP2s to the site of endocytosis. Summarising our\r\nresearch, these observations provide new important insights into the mechanism of plant\r\nCME and show that, despite plants posses many homologues of mammalian and yeast CME\r\ncomponents, they do not necessarily act in the same manner. "}],"date_created":"2023-11-10T09:10:06Z","keyword":["Clathrin-Mediated Endocytosis","vesicle scission","Dynamin-Related Protein 2","SH3P2","TPLATE complex","Total internal reflection fluorescence microscopy","Arabidopsis thaliana"],"oa":1,"file":[{"content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","embargo_to":"open_access","date_created":"2023-11-20T09:18:51Z","file_name":"Thesis_Gnyliukh_final_08_11_23.docx","file_size":20824903,"checksum":"3d5e680bfc61f98e308c434f45cc9bd6","file_id":"14567","relation":"source_file","date_updated":"2024-11-23T23:30:38Z","access_level":"closed","creator":"ngnyliuk"},{"embargo":"2024-11-23","file_name":"Thesis_Gnyliukh_final_20_11_23.pdf","date_created":"2023-11-20T09:23:11Z","content_type":"application/pdf","file_id":"14568","checksum":"bfc96d47fc4e7e857dd71656097214a4","file_size":24871844,"access_level":"open_access","creator":"ngnyliuk","date_updated":"2024-11-23T23:30:38Z","relation":"main_file"}],"acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"Bio"},{"_id":"LifeSc"}],"type":"dissertation","corr_author":"1","status":"public","project":[{"name":"International IST Doctoral Program","call_identifier":"H2020","grant_number":"665385","_id":"2564DBCA-B435-11E9-9278-68D0E5697425"}],"author":[{"orcid":"0000-0002-2198-0509","first_name":"Nataliia","last_name":"Gnyliukh","full_name":"Gnyliukh, Nataliia","id":"390C1120-F248-11E8-B48F-1D18A9856A87"}],"doi":"10.15479/at:ista:14510","year":"2023","day":"10","page":"180","ddc":["570"],"degree_awarded":"PhD","related_material":{"record":[{"status":"public","relation":"part_of_dissertation","id":"14591"},{"id":"9887","status":"public","relation":"part_of_dissertation"},{"id":"8139","relation":"part_of_dissertation","status":"public"}]},"month":"11","title":"Mechanism of clathrin-coated vesicle  formation during endocytosis in plants"}]