--- OA_type: closed access _id: '21762' abstract: - lang: eng text: Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal system named CorMR with a function in cell shape control rather than DNA segregation. Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed that CorM formed dynamically unstable, antiparallel double-stranded filaments that were recruited to the membrane by CorR through an amphipathic helix conserved in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which excluded them from the poles and division plane. Comparative genomics indicated that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity, highlighting the evolutionary plasticity of cytoskeletal systems in bacteria. acknowledged_ssus: - _id: Bio - _id: ScienComp - _id: EM-Fac - _id: LifeSc acknowledgement: "We thank all members of the Loose lab at ISTA for helpful discussions; M. Kojic for critical reading of the manuscript; A. Herrero (Sevilla University) for sharing her extensive BACTH plasmid library and other plasmids, as well as cyanobacterial strains; T. Dagan and F. Nies (both Kiel University) for sharing cyanobacterial strains and plasmids and for valuable discussions; N. Sapay and A. Michon for providing the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix screen of cyanobacterial CorR proteins; V.-V. Hodirnau for support in cryo-ET data collection; and J. Hansen for advice about cryo-EM data processing.\r\nThis work was supported by the Scientific Service Units (SSU) of ISTA through resources provided by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp), the Electron Microscopy Facility (EMF), and the Lab Support Facility (LSF). This work was funded by the European Union’s Horizon 2020 research and innovation program (Marie Skłodowska-Curie grant 101034413 to B.L.S.); the European Research Council (ERC) of the European Union (grant ActinID 101076260 to F.K.M.S.); the Swiss National Science Foundation (starting grant TMSGI3_226208 to G.L.W.); and the Jean-Jacques et Letitia Lopez-Loreta Foundation (G.L.W.)." article_number: eaea6343 article_processing_charge: No article_type: original author: - first_name: Benjamin L full_name: Springstein, Benjamin L id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083 last_name: Springstein orcid: 0000-0002-3461-5391 - first_name: Manjunath full_name: Javoor, Manjunath id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2 last_name: Javoor orcid: 0000-0003-2311-2112 - first_name: Daniela full_name: Megrian, Daniela last_name: Megrian - first_name: Roman full_name: Hajdu, Roman id: ffab949d-133f-11ed-8f02-94de21ace503 last_name: Hajdu - first_name: Dustin M. full_name: Hanke, Dustin M. last_name: Hanke - first_name: Bettina full_name: Zens, Bettina id: 45FD126C-F248-11E8-B48F-1D18A9856A87 last_name: Zens orcid: 0000-0002-9561-1239 - first_name: Gregor L. full_name: Weiss, Gregor L. last_name: Weiss - first_name: Florian Km full_name: Schur, Florian Km id: 48AD8942-F248-11E8-B48F-1D18A9856A87 last_name: Schur orcid: 0000-0003-4790-8078 - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 citation: ama: Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. Science. 2026;392(6795). doi:10.1126/science.aea6343 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. Science. AAAS. https://doi.org/10.1126/science.aea6343 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.” Science. AAAS, 2026. https://doi.org/10.1126/science.aea6343. ieee: B. L. Springstein et al., “Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape,” Science, vol. 392, no. 6795. AAAS, 2026. 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. mla: Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” Science, vol. 392, no. 6795, eaea6343, AAAS, 2026, doi:10.1126/science.aea6343. 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). corr_author: '1' date_created: 2026-04-26T22:01:46Z date_published: 2026-04-16T00:00:00Z date_updated: 2026-04-28T13:29:05Z day: '16' department: - _id: MaLo - _id: FlSc - _id: GradSch - _id: EM-Fac doi: 10.1126/science.aea6343 ec_funded: 1 external_id: pmid: - '41990175' intvolume: ' 392' issue: '6795' language: - iso: eng month: '04' oa_version: None pmid: 1 project: - _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: bd980d18-d553-11ed-ba76-ceaa645c97eb grant_number: '101076260' name: A molecular atlas of Actin filament IDentities in the cell motility machinery publication: Science publication_identifier: eissn: - 1095-9203 issn: - 0036-8075 publication_status: published publisher: AAAS quality_controlled: '1' scopus_import: '1' status: public title: Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 392 year: '2026' ... --- _id: '19915' 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" article_processing_charge: No author: - first_name: Benjamin L full_name: Springstein, Benjamin L id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083 last_name: Springstein orcid: 0000-0002-3461-5391 citation: ama: Springstein BL. Files for “Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape.” 2025. doi:10.15479/AT:ISTA:19915 apa: Springstein, B. L. (2025). Files for “Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape.” Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:19915 chicago: Springstein, Benjamin L. “Files for ‘Evolutionary Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cyanobacterial Cell Shape.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT:ISTA:19915. ieee: B. L. Springstein, “Files for ‘Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape.’” Institute of Science and Technology Austria, 2025. ista: Springstein BL. 2025. Files for ‘Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape’, Institute of Science and Technology Austria, 10.15479/AT:ISTA:19915. mla: Springstein, Benjamin L. Files for “Evolutionary Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cyanobacterial Cell Shape.” Institute of Science and Technology Austria, 2025, doi:10.15479/AT:ISTA:19915. short: B.L. Springstein, (2025). contributor: - contributor_type: project_leader first_name: Benjamin L id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083 last_name: Springstein orcid: 0000-0002-3461-5391 - contributor_type: researcher first_name: Manjunath id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2 last_name: Javoor - contributor_type: researcher first_name: Daniela last_name: Megrian - contributor_type: researcher first_name: Roman id: ffab949d-133f-11ed-8f02-94de21ace503 last_name: Hajdu - contributor_type: researcher first_name: Dustin M last_name: Hanke - contributor_type: researcher first_name: Florian KM id: 48AD8942-F248-11E8-B48F-1D18A9856A87 last_name: Schur orcid: 0000-0003-4790-8078 - contributor_type: supervisor first_name: Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 corr_author: '1' date_created: 2025-06-27T07:34:52Z date_published: 2025-06-27T00:00:00Z date_updated: 2025-07-02T08:25:37Z day: '27' department: - _id: MaLo doi: 10.15479/AT:ISTA:19915 ec_funded: 1 file: - 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access_level: open_access checksum: 57e0cbcfdd347f75808c7ae049136f22 content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19920' file_name: Supplementary Movie 5) in vitro FRAP of (1-40)CorM.avi file_size: 3862712 relation: main_file success: 1 - access_level: open_access checksum: 58d36666c1f3155d5a641e6b47f3843f content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19921' file_name: Supplementary Movie 6) in vitro CorM filament tracking.avi file_size: 3183046 relation: main_file success: 1 - access_level: open_access checksum: 509a0d7db16cf1db581b719d355718db content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19922' file_name: Supplementary Movie 7) in vitro CorM dual color imaging.avi file_size: 468600 relation: main_file success: 1 - access_level: open_access checksum: e6e5f8755819503eeb7081049d3d6aa5 content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19923' file_name: Supplementary Movie 8) in vivo MinC oscillation.avi file_size: 3038980 relation: main_file success: 1 - access_level: open_access checksum: c6c0e4cd9766ecafce52d99a0ac8c339 content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19924' file_name: Supplementary Movie 9) in vitro CorM + MinC.avi file_size: 21730482 relation: main_file success: 1 - access_level: open_access checksum: abe15b253a7c9a1dc484a614dd2ab30a content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:29Z date_updated: 2025-06-27T07:35:29Z file_id: '19925' file_name: Supplementary Movie 10) in vitro CorM + MinC(S50A+L55D).avi file_size: 28315550 relation: main_file success: 1 - access_level: open_access checksum: d5cc3426aa3e066ee175e6c3a66cf84d content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:30Z date_updated: 2025-06-27T07:35:30Z file_id: '19926' file_name: Supplementary Movie 11) in vitro CorM + MinC(delta46-67).avi file_size: 25693552 relation: main_file success: 1 - access_level: open_access checksum: 70daf423216753ec5c73afe18f347821 content_type: video/x-msvideo creator: bsprings date_created: 2025-06-27T07:35:30Z date_updated: 2025-06-27T07:35:30Z file_id: '19927' file_name: Supplementary Movie 12) in vitro CorM + buffer ctrl.avi file_size: 25349196 relation: main_file success: 1 - 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_id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c call_identifier: H2020 grant_number: '101034413' name: 'IST-BRIDGE: International postdoctoral program' - _id: bd980d18-d553-11ed-ba76-ceaa645c97eb grant_number: '101076260' name: A molecular atlas of Actin filament IDentities in the cell motility machinery publisher: Institute of Science and Technology Austria status: public title: Files for "Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape" tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: research_data user_id: 68b8ca59-c5b3-11ee-8790-cd641c68093d year: '2025' ... --- DOAJ_listed: '1' OA_place: publisher OA_type: gold PlanS_conform: '1' _id: '20351' abstract: - lang: eng 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. 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).' article_processing_charge: Yes article_type: original author: - first_name: Stephan full_name: Wilmes, Stephan last_name: Wilmes - first_name: Jesse full_name: Tönjes, Jesse last_name: Tönjes - first_name: Maik full_name: Drechsler, Maik last_name: Drechsler - first_name: Anita full_name: Ruf, Anita last_name: Ruf - first_name: Jan Hannes full_name: Schäfer, Jan Hannes last_name: Schäfer - first_name: Anna full_name: Lürick, Anna last_name: Lürick - first_name: Dovile full_name: Januliene, Dovile last_name: Januliene - first_name: Steven full_name: Apelt, Steven last_name: Apelt - first_name: Daniele full_name: Di Iorio, Daniele last_name: Di Iorio - first_name: Seraphine V. full_name: Wegner, Seraphine V. last_name: Wegner - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Arne full_name: Moeller, Arne last_name: Moeller - first_name: Achim full_name: Paululat, Achim last_name: Paululat - first_name: Daniel full_name: Kümmel, Daniel last_name: Kümmel citation: ama: Wilmes S, Tönjes J, Drechsler M, et al. Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science Advances. 2025;11(35):eadx2893. doi:10.1126/sciadv.adx2893 apa: Wilmes, S., Tönjes, J., Drechsler, M., Ruf, A., Schäfer, J. H., Lürick, A., … Kümmel, D. (2025). Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science Advances. AAAS. https://doi.org/10.1126/sciadv.adx2893 chicago: Wilmes, Stephan, Jesse Tönjes, Maik Drechsler, Anita Ruf, Jan Hannes Schäfer, Anna Lürick, Dovile Januliene, et al. “Mechanistic Adaptation of the Metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.” Science Advances. AAAS, 2025. https://doi.org/10.1126/sciadv.adx2893. ieee: S. Wilmes et al., “Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned,” Science Advances, vol. 11, no. 35. AAAS, p. eadx2893, 2025. 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.” Science Advances, vol. 11, no. 35, AAAS, 2025, p. eadx2893, doi:10.1126/sciadv.adx2893. short: S. Wilmes, J. Tönjes, M. Drechsler, A. Ruf, J.H. Schäfer, A. Lürick, D. Januliene, S. Apelt, D. Di Iorio, S.V. Wegner, M. Loose, A. Moeller, A. Paululat, D. Kümmel, Science Advances 11 (2025) eadx2893. date_created: 2025-09-14T22:01:32Z date_published: 2025-08-29T00:00:00Z date_updated: 2025-09-30T14:40:27Z day: '29' ddc: - '570' department: - _id: MaLo doi: 10.1126/sciadv.adx2893 external_id: isi: - '001559806100033' pmid: - '40864718' file: - access_level: open_access checksum: a3de801f3c6c1deadd7099d965db799a content_type: application/pdf creator: dernst date_created: 2025-09-15T07:23:12Z date_updated: 2025-09-15T07:23:12Z file_id: '20355' file_name: 2025_ScienceAdvance_Wilmes.pdf file_size: 3434827 relation: main_file success: 1 file_date_updated: 2025-09-15T07:23:12Z has_accepted_license: '1' intvolume: ' 11' isi: 1 issue: '35' language: - iso: eng month: '08' oa: 1 oa_version: Published Version page: eadx2893 pmid: 1 project: - _id: bd6ae2ca-d553-11ed-ba76-a4aa239da5ee grant_number: '101045340' name: Synthetic and structural biology of Rab GTPase networks publication: Science Advances publication_identifier: eissn: - 2375-2548 publication_status: published publisher: AAAS quality_controlled: '1' scopus_import: '1' status: public title: Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 11 year: '2025' ... --- OA_place: publisher _id: '20364' acknowledged_ssus: - _id: LifeSc - _id: Bio acknowledgement: "Plant Facility,\r\nProtein Service Facility" alternative_title: - ISTA Thesis article_processing_charge: No author: - first_name: Caterina full_name: Giannini, Caterina id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4 last_name: Giannini citation: ama: Giannini C. Nuclear and cell surface auxin signaling in A. thaliana developmental transitions. 2025. doi:10.15479/AT-ISTA-20364 apa: Giannini, C. (2025). Nuclear and cell surface auxin signaling in A. thaliana developmental transitions. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20364 chicago: Giannini, Caterina. “Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions.” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20364. ieee: 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. mla: Giannini, Caterina. Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions. Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-20364. short: C. Giannini, Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental Transitions, Institute of Science and Technology Austria, 2025. corr_author: '1' date_created: 2025-09-19T12:23:38Z date_published: 2025-09-19T00:00:00Z date_updated: 2026-04-07T11:52:16Z day: '19' ddc: - '580' degree_awarded: PhD department: - _id: GradSch - _id: JiFr - _id: MaLo doi: 10.15479/AT-ISTA-20364 file: - access_level: closed checksum: 536ba1701453b0b2346be14c046b2911 content_type: application/pdf creator: cgiannin date_created: 2025-09-24T14:46:34Z date_updated: 2025-09-30T14:31:29Z embargo: 2026-09-30 embargo_to: open_access file_id: '20390' file_name: 2025_Giannini_Caterina_Thesis...pdf file_size: 14278965 relation: main_file - access_level: closed checksum: 192f55262f2da2ea0a59d9c23a1b8573 content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document creator: cgiannin date_created: 2025-09-24T14:46:35Z date_updated: 2025-09-24T14:46:35Z file_id: '20391' file_name: 2025_Giannini_Caterina_Thesis...docx file_size: 24499022 relation: source_file file_date_updated: 2025-09-30T14:31:29Z has_accepted_license: '1' keyword: - Auxin Signaling - Plant Development language: - iso: eng month: '09' oa_version: Published Version page: '151' publication_identifier: issn: - 2663-337X publication_status: published publisher: Institute of Science and Technology Austria related_material: record: - id: '12291' relation: part_of_dissertation status: public - id: '19399' relation: part_of_dissertation status: public status: public supervisor: - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 title: Nuclear and cell surface auxin signaling in A. thaliana developmental transitions type: dissertation user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd year: '2025' ... --- OA_place: publisher _id: '20741' abstract: - lang: eng 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. " acknowledged_ssus: - _id: Bio alternative_title: - ISTA Thesis article_processing_charge: No author: - first_name: Marko full_name: Kojic, Marko id: 73e7ecd4-dc85-11ea-9058-88a16394b160 last_name: Kojic orcid: 0000-0001-7244-8128 citation: ama: Kojic M. Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria. 2025. doi:10.15479/AT-ISTA-20741 apa: Kojic, M. (2025). Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20741 chicago: Kojic, Marko. “Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria.” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20741. ieee: 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. mla: Kojic, Marko. Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria. Institute of Science and Technology Austria, 2025, doi:10.15479/AT-ISTA-20741. short: M. Kojic, Towards Understanding the Assembly Mechanisms of the Z-Ring in Archaea and Bacteria, Institute of Science and Technology Austria, 2025. corr_author: '1' date_created: 2025-12-09T13:08:11Z date_published: 2025-12-09T00:00:00Z date_updated: 2026-04-07T12:27:58Z day: '09' ddc: - '572' degree_awarded: PhD department: - _id: GradSch - _id: MaLo doi: 10.15479/AT-ISTA-20741 file: - access_level: closed checksum: a3643d07e93134b2490a566b02a4517d content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document creator: mkojic date_created: 2025-12-10T13:09:58Z date_updated: 2025-12-10T13:09:58Z file_id: '20774' file_name: 2025_marko_kojic_thesis.docx file_size: 142876975 relation: source_file - access_level: open_access checksum: 0a096f0af6ccc3a8329d5bb8797ad533 content_type: application/pdf creator: mkojic date_created: 2025-12-10T13:09:38Z date_updated: 2025-12-10T13:09:38Z file_id: '20775' file_name: 2025_marko_kojic_thesis.pdf file_size: 8597045 relation: main_file success: 1 file_date_updated: 2025-12-10T13:09:58Z has_accepted_license: '1' language: - iso: eng month: '12' oa: 1 oa_version: Published Version publication_identifier: isbn: - 978-3-99078-073-2 issn: - 2663-337X publication_status: published publisher: Institute of Science and Technology Austria related_material: record: - id: '15118' relation: part_of_dissertation status: public status: public supervisor: - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 title: Towards understanding the assembly mechanisms of the Z-ring in Archaea and Bacteria tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: dissertation user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd year: '2025' ... --- OA_place: publisher OA_type: gold _id: '18073' 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. acknowledgement: We thank late Thomas Peterbauer at the Max Perutz Labs Biooptics Light Microscopy Facility for his help and support. We are grateful to Kitti Csalyi and Thomas Sauer at Max Perutz Labs Biooptics FACS facility for their help. We thank Grzegorz Scibisz and Sertan Atilla for their support with the expression and purification of mCherry-IRE1α LD-10His. We are grateful to Aleksandra S Anisimova with her help in the generation of stable cell lines and the statistical analyses of the data. We thank Venja Vieweger for her help with the characterization of the WLLI and D123P IRE1 mutants in cells. We are thankful to Monika Kubickova for the help with the AUC experiments. We acknowledge CF BIC of CIISB, Instruct-CZ Centre, supported by MEYS CR (LM2023042)) and European Regional Development Fund-Project, UP CIISB“ (No. CZ.02.1.01/0.0/0.0/18_046/0015974). We thank the members of the Karagöz lab for the critical reading and editing of the manuscript. We are thankful to our colleagues Diego Acosta-Alvear, Vladislav Belyy, Jirka Peschek, Yasin Dagdas, Javier Martinez, Sascha Martens and Alwin Köhler for their invaluable input on the manuscript. We are grateful to Life Science Editors, especially Katrina Woolcock for her useful edits and comments on the manuscript. We acknowledge funding from Austrian Science Fund (FWF-SFB F79 and FWF-W 1261) to GEK. PK acknowledges the support of the Max Perutz PhD fellowship. GAV is funded by Stand-Alone grants (P30231-B, P30415-B, P36572), Special Research Grant (SFB grant F79), and Doctoral School grant (DK grant W1261) from the Austrian Science Fund (FWF). ES and RC acknowledge support and funding by the Frankfurt Institute of Advanced Studies, the LOEWE Center for Multiscale Modelling in Life Sciences of the state of Hesse, the Collaborative Research Center 1507 “Membrane-associated Protein Assemblies, Machineries, and Supercomplexes” (Project ID 450648163), and the International Max Planck Research School on Cellular Biophysics (to RC), the Center for Scientific Computing of the Goethe University and the Jülich Supercomputing Centre for computational resources and support. article_processing_charge: Yes article_type: original author: - first_name: Paulina full_name: Kettel, Paulina last_name: Kettel - first_name: Laura full_name: Marosits, Laura last_name: Marosits - first_name: Elena full_name: Spinetti, Elena last_name: Spinetti - first_name: Michael full_name: Rechberger, Michael last_name: Rechberger - first_name: Caterina full_name: Giannini, Caterina id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4 last_name: Giannini - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Isabell full_name: Niedermoser, Isabell last_name: Niedermoser - first_name: Irmgard full_name: Fischer, Irmgard last_name: Fischer - first_name: Gijs A. full_name: Versteeg, Gijs A. last_name: Versteeg - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Roberto full_name: Covino, Roberto last_name: Covino - first_name: G. Elif full_name: Karagöz, G. Elif last_name: Karagöz citation: ama: Kettel P, Marosits L, Spinetti E, et al. Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering. EMBO Journal. 2024;43(20):4668-4698. doi:10.1038/s44318-024-00207-0 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. EMBO Journal. Embo Press. https://doi.org/10.1038/s44318-024-00207-0 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.” EMBO Journal. Embo Press, 2024. https://doi.org/10.1038/s44318-024-00207-0. ieee: P. Kettel et al., “Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering,” EMBO Journal, vol. 43, no. 20. Embo Press, pp. 4668–4698, 2024. 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. mla: Kettel, Paulina, et al. “Disordered Regions in the IRE1α ER Lumenal Domain Mediate Its Stress-Induced Clustering.” EMBO Journal, vol. 43, no. 20, Embo Press, 2024, pp. 4668–98, doi:10.1038/s44318-024-00207-0. 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. date_created: 2024-09-15T22:01:42Z date_published: 2024-10-15T00:00:00Z date_updated: 2025-09-08T09:22:11Z day: '15' ddc: - '570' department: - _id: MaLo - _id: JiFr doi: 10.1038/s44318-024-00207-0 external_id: isi: - '001306286100002' pmid: - '39232130' file: - access_level: open_access checksum: 04f4df1a561083f2846676442fc4eb3c content_type: application/pdf creator: dernst date_created: 2025-01-13T08:43:20Z date_updated: 2025-01-13T08:43:20Z file_id: '18827' file_name: 2024_Embo_Kettel.pdf file_size: 10080854 relation: main_file success: 1 file_date_updated: 2025-01-13T08:43:20Z has_accepted_license: '1' intvolume: ' 43' isi: 1 issue: '20' language: - iso: eng month: '10' oa: 1 oa_version: Published Version page: 4668-4698 pmid: 1 publication: EMBO Journal publication_identifier: eissn: - 1460-2075 issn: - 0261-4189 publication_status: published publisher: Embo Press quality_controlled: '1' scopus_import: '1' status: public title: Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 43 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '18938' 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. 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. article_number: e2317453121 article_processing_charge: No article_type: original author: - first_name: Benjamin L full_name: Springstein, Benjamin L id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083 last_name: Springstein orcid: 0000-0002-3461-5391 - first_name: Joao A. full_name: Paulo, Joao A. last_name: Paulo - first_name: Hankum full_name: Park, Hankum last_name: Park - first_name: Kemardo full_name: Henry, Kemardo last_name: Henry - first_name: Eleanor full_name: Fleming, Eleanor last_name: Fleming - first_name: Zoë full_name: Feder, Zoë last_name: Feder - first_name: J. Wade full_name: Harper, J. Wade last_name: Harper - first_name: Ann full_name: Hochschild, Ann last_name: Hochschild citation: ama: Springstein BL, Paulo JA, Park H, et al. 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. 2024;121(6). doi:10.1073/pnas.2317453121 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. Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences. https://doi.org/10.1073/pnas.2317453121 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.” Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2317453121. ieee: B. L. Springstein et al., “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, vol. 121, no. 6. National Academy of Sciences, 2024. 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. mla: Springstein, Benjamin L., et al. “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, vol. 121, no. 6, e2317453121, National Academy of Sciences, 2024, doi:10.1073/pnas.2317453121. 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). date_created: 2025-01-29T08:39:27Z date_published: 2024-02-06T00:00:00Z date_updated: 2025-05-14T11:02:52Z day: '06' ddc: - '570' department: - _id: MaLo doi: 10.1073/pnas.2317453121 external_id: pmid: - '38289956' file: - access_level: open_access checksum: 5bd62c7cb4287e3706a1d45d6ef61fd1 content_type: application/pdf creator: dernst date_created: 2025-01-29T08:43:16Z date_updated: 2025-01-29T08:43:16Z file_id: '18939' file_name: 2024_PNAS_Springstein.pdf file_size: 720902 relation: main_file success: 1 file_date_updated: 2025-01-29T08:43:16Z has_accepted_license: '1' intvolume: ' 121' issue: '6' language: - iso: eng month: '02' oa: 1 oa_version: Published Version pmid: 1 publication: Proceedings of the National Academy of Sciences of the United States of America publication_identifier: eissn: - 1091-6490 issn: - 0027-8424 publication_status: published publisher: National Academy of Sciences quality_controlled: '1' scopus_import: '1' status: public title: Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational tiling proteomics tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 121 year: '2024' ... --- _id: '14795' 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. acknowledged_ssus: - _id: Bio - _id: PreCl 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." article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Feyza N full_name: Arslan, Feyza N id: 49DA7910-F248-11E8-B48F-1D18A9856A87 last_name: Arslan orcid: 0000-0001-5809-9566 - first_name: Edouard B full_name: Hannezo, Edouard B id: 3A9DB764-F248-11E8-B48F-1D18A9856A87 last_name: Hannezo orcid: 0000-0001-6005-1561 - first_name: Jack full_name: Merrin, Jack id: 4515C308-F248-11E8-B48F-1D18A9856A87 last_name: Merrin orcid: 0000-0001-5145-4609 - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Carl-Philipp J full_name: Heisenberg, Carl-Philipp J id: 39427864-F248-11E8-B48F-1D18A9856A87 last_name: Heisenberg orcid: 0000-0002-0912-4566 citation: ama: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 2024;34(1):171-182.e8. doi:10.1016/j.cub.2023.11.067 apa: Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., & Heisenberg, C.-P. J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2023.11.067 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.” Current Biology. Elsevier, 2024. https://doi.org/10.1016/j.cub.2023.11.067. 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,” Current Biology, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024. 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. mla: Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell Contacts.” Current Biology, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8, doi:10.1016/j.cub.2023.11.067. short: F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current Biology 34 (2024) 171–182.e8. corr_author: '1' date_created: 2024-01-14T23:00:56Z date_published: 2024-01-08T00:00:00Z date_updated: 2025-09-04T11:39:10Z day: '08' ddc: - '570' department: - _id: CaHe - _id: EdHa - _id: MaLo - _id: NanoFab doi: 10.1016/j.cub.2023.11.067 ec_funded: 1 external_id: isi: - '001154500400001' pmid: - '38134934' file: - access_level: open_access checksum: 51220b76d72a614208f84bdbfbaf9b72 content_type: application/pdf creator: dernst date_created: 2024-01-16T10:53:31Z date_updated: 2024-01-16T10:53:31Z file_id: '14813' file_name: 2024_CurrentBiology_Arslan.pdf file_size: 5183861 relation: main_file success: 1 file_date_updated: 2024-01-16T10:53:31Z has_accepted_license: '1' intvolume: ' 34' isi: 1 issue: '1' language: - iso: eng month: '01' oa: 1 oa_version: Published Version page: 171-182.e8 pmid: 1 project: - _id: 260F1432-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '742573' name: Interaction and feedback between cell mechanics and fate specification in vertebrate gastrulation publication: Current Biology publication_identifier: eissn: - 1879-0445 issn: - 0960-9822 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 34 year: '2024' ... --- _id: '14834' 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. 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. article_number: '151380' article_processing_charge: Yes article_type: review author: - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 citation: ama: 'Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. 2024;103(1). doi:10.1016/j.ejcb.2023.151380' apa: '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. Elsevier. https://doi.org/10.1016/j.ejcb.2023.151380' 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.” European Journal of Cell Biology. Elsevier, 2024. https://doi.org/10.1016/j.ejcb.2023.151380.' ieee: 'P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches,” European Journal of Cell Biology, vol. 103, no. 1. Elsevier, 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.” European Journal of Cell Biology, vol. 103, no. 1, 151380, Elsevier, 2024, doi:10.1016/j.ejcb.2023.151380.' short: P. Radler, M. Loose, European Journal of Cell Biology 103 (2024). corr_author: '1' date_created: 2024-01-18T08:16:43Z date_published: 2024-03-01T00:00:00Z date_updated: 2025-09-04T11:45:31Z day: '01' ddc: - '570' department: - _id: MaLo doi: 10.1016/j.ejcb.2023.151380 external_id: isi: - '001166216800001' pmid: - '38218128' file: - access_level: open_access checksum: 5d170abbc87585205c010657e4552360 content_type: application/pdf creator: dernst date_created: 2024-07-16T12:07:20Z date_updated: 2024-07-16T12:07:20Z file_id: '17265' file_name: 2024_EJCB_Radler.pdf file_size: 9995304 relation: main_file success: 1 file_date_updated: 2024-07-16T12:07:20Z has_accepted_license: '1' intvolume: ' 103' isi: 1 issue: '1' keyword: - Cell Biology - General Medicine - Histology - Pathology and Forensic Medicine language: - iso: eng month: '03' oa: 1 oa_version: Published Version pmid: 1 project: - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division publication: European Journal of Cell Biology publication_identifier: issn: - 0171-9335 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: 'A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches' tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 103 year: '2024' ... --- OA_place: publisher OA_type: hybrid _id: '15330' 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. acknowledged_ssus: - _id: EM-Fac - _id: LifeSc - _id: Bio acknowledgement: "Nataliia Gnyliukh was partially funded by the European Union’s Horizon 2020 research and\r\ninnovation program (2018-2020) under the Marie Sklodowska-Curie Grant (agreement no.\r\n665385). Taif University Researchers Supporting Project: TURSP-HC2022/02. and Austrian\r\nScience Fund (FWF): I 6123-B.We thank Prof. Eileen Lafer and Liping Wang for their suggestions regarding the optimisation of protein expression and purification. We thank Prof. Sebastian Y. Bednarek for the useful comments and constructive criticism of the project. We thank Maciek Adamowski for providing genetic material. This research was supported by the Scientific Service Units (SSU) of IST-Austria through resources provided by the Electron microscopy (EMF), Lab Support Facility (LSF) (particularly Dorota Jaworska) and the Bioimaging Facility (BIF)." article_number: jcs.261720 article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Nataliia full_name: Gnyliukh, Nataliia id: 390C1120-F248-11E8-B48F-1D18A9856A87 last_name: Gnyliukh orcid: 0000-0002-2198-0509 - first_name: Alexander J full_name: Johnson, Alexander J id: 46A62C3A-F248-11E8-B48F-1D18A9856A87 last_name: Johnson orcid: 0000-0002-2739-8843 - first_name: MK full_name: Nagel, MK last_name: Nagel - first_name: Aline full_name: Monzer, Aline id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425 last_name: Monzer - first_name: David full_name: Babic, David id: db566d23-f6e0-11ea-865d-e6f270e968e7 last_name: Babic - first_name: Annamaria full_name: Hlavata, Annamaria id: 36062FEC-F248-11E8-B48F-1D18A9856A87 last_name: Hlavata - first_name: SS full_name: Alotaibi, SS last_name: Alotaibi - first_name: E full_name: Isono, E last_name: Isono - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 citation: ama: Gnyliukh N, Johnson AJ, Nagel M, et al. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal of Cell Science. 2024;137(8). doi:10.1242/jcs.261720 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. Journal of Cell Science. The Company of Biologists. https://doi.org/10.1242/jcs.261720 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.” Journal of Cell Science. The Company of Biologists, 2024. https://doi.org/10.1242/jcs.261720. ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana,” Journal of Cell Science, vol. 137, no. 8. The Company of Biologists, 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. mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Arabidopsis Thaliana.” Journal of Cell Science, vol. 137, no. 8, jcs. 261720, The Company of Biologists, 2024, doi:10.1242/jcs.261720. 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). corr_author: '1' date_created: 2024-04-19T09:54:59Z date_published: 2024-04-01T00:00:00Z date_updated: 2025-09-04T13:49:45Z day: '01' ddc: - '570' department: - _id: MaLo - _id: JiFr - _id: CaBe doi: 10.1242/jcs.261720 ec_funded: 1 external_id: isi: - '001266917100005' pmid: - '38506228' file: - access_level: open_access checksum: 6dc023f0cc7052ad3cf0a42589d2e30f content_type: application/pdf creator: dernst date_created: 2025-01-09T08:41:16Z date_updated: 2025-01-09T08:41:16Z file_id: '18792' file_name: 2024_JourCellScience_Gnyliukh.pdf file_size: 25845948 relation: main_file success: 1 file_date_updated: 2025-01-09T08:41:16Z has_accepted_license: '1' intvolume: ' 137' isi: 1 issue: '8' language: - iso: eng month: '04' oa: 1 oa_version: Published Version pmid: 1 project: - _id: 2564DBCA-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '665385' name: International IST Doctoral Program - _id: bd76d395-d553-11ed-ba76-f678c14f9033 grant_number: I06123 name: Peptide receptors for auxin canalization in Arabidopsis publication: Journal of Cell Science publication_identifier: eissn: - 1477-9137 issn: - 0021-9533 publication_status: published publisher: The Company of Biologists quality_controlled: '1' related_material: record: - id: '14591' relation: earlier_version status: public scopus_import: '1' status: public title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 137 year: '2024' ... --- _id: '15374' abstract: - lang: eng 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. 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.' article_number: '114195' article_processing_charge: Yes article_type: original author: - first_name: Maciek full_name: Adamowski, Maciek id: 45F536D2-F248-11E8-B48F-1D18A9856A87 last_name: Adamowski orcid: 0000-0001-6463-5257 - first_name: Marek full_name: Randuch, Marek id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae last_name: Randuch - first_name: Ivana full_name: Matijevic, Ivana id: 83c17ce3-15b2-11ec-abd3-f486545870bd last_name: Matijevic - first_name: Madhumitha full_name: Narasimhan, Madhumitha id: 44BF24D0-F248-11E8-B48F-1D18A9856A87 last_name: Narasimhan orcid: 0000-0002-8600-0671 - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 citation: ama: Adamowski M, Randuch M, Matijevic I, Narasimhan M, Friml J. SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. Cell Reports. 2024;43(5). doi:10.1016/j.celrep.2024.114195 apa: Adamowski, M., Randuch, M., Matijevic, I., Narasimhan, M., & Friml, J. (2024). SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. Cell Reports. Cell Press. https://doi.org/10.1016/j.celrep.2024.114195 chicago: Adamowski, Maciek, Marek Randuch, Ivana Matijevic, Madhumitha Narasimhan, and Jiří Friml. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors for Clathrin-Mediated Endocytosis.” Cell Reports. Cell Press, 2024. https://doi.org/10.1016/j.celrep.2024.114195. ieee: M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, and J. Friml, “SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis,” Cell Reports, vol. 43, no. 5. Cell Press, 2024. 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. mla: Adamowski, Maciek, et al. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors for Clathrin-Mediated Endocytosis.” Cell Reports, vol. 43, no. 5, 114195, Cell Press, 2024, doi:10.1016/j.celrep.2024.114195. short: M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, J. Friml, Cell Reports 43 (2024). corr_author: '1' date_created: 2024-05-12T22:01:01Z date_published: 2024-05-28T00:00:00Z date_updated: 2025-09-08T07:23:07Z day: '28' ddc: - '580' department: - _id: JiFr - _id: MaLo doi: 10.1016/j.celrep.2024.114195 external_id: isi: - '001240362800001' pmid: - '38717900' file: - access_level: open_access checksum: a06bb85be4fc765c51554d27ee2da802 content_type: application/pdf creator: dernst date_created: 2024-05-13T12:11:22Z date_updated: 2024-05-13T12:11:22Z file_id: '15387' file_name: 2024_CellReports_Adamowski.pdf file_size: 5698598 relation: main_file success: 1 file_date_updated: 2024-05-13T12:11:22Z has_accepted_license: '1' intvolume: ' 43' isi: 1 issue: '5' language: - iso: eng month: '05' oa: 1 oa_version: Published Version pmid: 1 project: - _id: 26538374-B435-11E9-9278-68D0E5697425 call_identifier: FWF grant_number: I03630 name: Molecular mechanisms of endocytic cargo recognition in plants publication: Cell Reports publication_identifier: eissn: - 2211-1247 publication_status: published publisher: Cell Press quality_controlled: '1' scopus_import: '1' status: public title: SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 43 year: '2024' ... --- APC_amount: 12348 EUR OA_place: publisher OA_type: hybrid _id: '17460' abstract: - lang: eng 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. acknowledgement: We thank I. Palaia (ISTA) for useful discussions and K. Lim and R. W. Wong (WPI-Nano Life Science Institute, Kanazawa University) for providing access to HS-AFM. We would like to thank B. Prats Mateu (MSD Austria, Vienna) for providing the HS-AFM data. This work was supported by the Royal Society (grant no. UF160266; C.V.-C. and A.Š.), the European Union’s Horizon 2020 Research and Innovation Programme (grant no. 802960; A.Š.), the Austrian Science Fund (FWF) Stand-Alone P34607 (M.L.) and a Wellcome Trust and Royal Society Sir Henry Dale Fellowship (grant no. 206670/Z/17/Z; S.H. and K.D.W.). article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Christian Eduardo full_name: Vanhille-Campos, Christian Eduardo id: 3adeca52-9313-11ed-b1ac-c170b2505714 last_name: Vanhille-Campos - first_name: Kevin D. full_name: Whitley, Kevin D. last_name: Whitley - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Séamus full_name: Holden, Séamus last_name: Holden - first_name: Anđela full_name: Šarić, Anđela id: bf63d406-f056-11eb-b41d-f263a6566d8b last_name: Šarić orcid: 0000-0002-7854-2139 citation: 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. Nature Physics. 2024;20:1670-1678. doi:10.1038/s41567-024-02597-8 apa: Vanhille-Campos, C. E., Whitley, K. D., Radler, P., Loose, M., Holden, S., & Šarić, A. (2024). Self-organization of mortal filaments and its role in bacterial division ring formation. Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-024-02597-8 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.” Nature Physics. Springer Nature, 2024. https://doi.org/10.1038/s41567-024-02597-8. 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,” Nature Physics, vol. 20. Springer Nature, pp. 1670–1678, 2024. 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. mla: Vanhille-Campos, Christian Eduardo, et al. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” Nature Physics, vol. 20, Springer Nature, 2024, pp. 1670–78, doi:10.1038/s41567-024-02597-8. short: C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić, Nature Physics 20 (2024) 1670–1678. corr_author: '1' date_created: 2024-08-25T22:01:08Z date_published: 2024-10-01T00:00:00Z date_updated: 2025-09-08T09:02:20Z day: '01' ddc: - '570' department: - _id: AnSa - _id: MaLo doi: 10.1038/s41567-024-02597-8 ec_funded: 1 external_id: isi: - '001289394500005' pmid: - '39416851' file: - access_level: open_access checksum: c4842152e2b90d67f48ea8c9ed7c473b content_type: application/pdf creator: dernst date_created: 2025-04-14T06:06:35Z date_updated: 2025-04-14T06:06:35Z file_id: '19556' file_name: 2024_NaturePhysics_VanhilleCampos.pdf file_size: 8058249 relation: main_file success: 1 file_date_updated: 2025-04-14T06:06:35Z has_accepted_license: '1' intvolume: ' 20' isi: 1 language: - iso: eng month: '10' oa: 1 oa_version: Published Version page: 1670-1678 pmid: 1 project: - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 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' publication: Nature Physics publication_identifier: eissn: - 1745-2481 issn: - 1745-2473 publication_status: published publisher: Springer Nature quality_controlled: '1' scopus_import: '1' status: public title: Self-organization of mortal filaments and its role in bacterial division ring formation tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 20 year: '2024' ... --- _id: '15118' 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. acknowledged_ssus: - _id: LifeSc 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. article_processing_charge: No article_type: original author: - first_name: Phillip full_name: Nußbaum, Phillip last_name: Nußbaum - first_name: Danguole full_name: Kureisaite-Ciziene, Danguole last_name: Kureisaite-Ciziene - first_name: Dom full_name: Bellini, Dom last_name: Bellini - first_name: Chris full_name: Van Der Does, Chris last_name: Van Der Does - first_name: Marko full_name: Kojic, Marko id: 73e7ecd4-dc85-11ea-9058-88a16394b160 last_name: Kojic orcid: 0000-0001-7244-8128 - first_name: Najwa full_name: Taib, Najwa last_name: Taib - first_name: Anna full_name: Yeates, Anna last_name: Yeates - first_name: Maxime full_name: Tourte, Maxime last_name: Tourte - first_name: Simonetta full_name: Gribaldo, Simonetta last_name: Gribaldo - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Jan full_name: Löwe, Jan last_name: Löwe - first_name: Sonja Verena full_name: Albers, Sonja Verena last_name: Albers citation: ama: Nußbaum P, Kureisaite-Ciziene D, Bellini D, et al. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. Nature Microbiology. 2024;9(3):698-711. doi:10.1038/s41564-024-01600-5 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. Nature Microbiology. Springer Nature. https://doi.org/10.1038/s41564-024-01600-5 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.” Nature Microbiology. Springer Nature, 2024. https://doi.org/10.1038/s41564-024-01600-5. ieee: P. Nußbaum et al., “Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division,” Nature Microbiology, vol. 9, no. 3. Springer Nature, pp. 698–711, 2024. 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.” Nature Microbiology, vol. 9, no. 3, Springer Nature, 2024, pp. 698–711, doi:10.1038/s41564-024-01600-5. 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. date_created: 2024-03-17T23:00:58Z date_published: 2024-03-04T00:00:00Z date_updated: 2026-04-07T12:27:57Z day: '04' department: - _id: MaLo doi: 10.1038/s41564-024-01600-5 external_id: isi: - '001183270800021' pmid: - '38443575' intvolume: ' 9' isi: 1 issue: '3' language: - iso: eng month: '03' oa_version: None page: 698-711 pmid: 1 project: - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division publication: Nature Microbiology publication_identifier: eissn: - 2058-5276 publication_status: published publisher: Springer Nature quality_controlled: '1' related_material: record: - id: '20741' relation: dissertation_contains status: public scopus_import: '1' status: public title: Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 9 year: '2024' ... --- _id: '12163' abstract: - lang: eng text: Small GTPases play essential roles in the organization of eukaryotic cells. In recent years, it has become clear that their intracellular functions result from intricate biochemical networks of the GTPase and their regulators that dynamically bind to a membrane surface. Due to the inherent complexities of their interactions, however, revealing the underlying mechanisms of action is often difficult to achieve from in vivo studies. This review summarizes in vitro reconstitution approaches developed to obtain a better mechanistic understanding of how small GTPase activities are regulated in space and time. acknowledgement: The authors acknowledge support from IST Austria and helpful comments from the anonymous reviewers that helped to improve this manuscript. We apologize to the authors of primary literature and outstanding research not cited here due to space restraints. article_processing_charge: Yes (via OA deal) article_type: review author: - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Albert full_name: Auer, Albert id: 3018E8C2-F248-11E8-B48F-1D18A9856A87 last_name: Auer orcid: 0000-0002-3580-2906 - first_name: Gabriel full_name: Brognara, Gabriel id: D96FFDA0-A884-11E9-9968-DC26E6697425 last_name: Brognara - first_name: Hanifatul R full_name: Budiman, Hanifatul R id: 55380f95-15b2-11ec-abd3-aff8e230696b last_name: Budiman - first_name: Lukasz M full_name: Kowalski, Lukasz M id: e3a512e2-4bbe-11eb-a68a-e3857a7844c2 last_name: Kowalski - first_name: Ivana full_name: Matijevic, Ivana id: 83c17ce3-15b2-11ec-abd3-f486545870bd last_name: Matijevic citation: ama: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. In vitro reconstitution of small GTPase regulation. FEBS Letters. 2023;597(6):762-777. doi:10.1002/1873-3468.14540 apa: Loose, M., Auer, A., Brognara, G., Budiman, H. R., Kowalski, L. M., & Matijevic, I. (2023). In vitro reconstitution of small GTPase regulation. FEBS Letters. Wiley. https://doi.org/10.1002/1873-3468.14540 chicago: Loose, Martin, Albert Auer, Gabriel Brognara, Hanifatul R Budiman, Lukasz M Kowalski, and Ivana Matijevic. “In Vitro Reconstitution of Small GTPase Regulation.” FEBS Letters. Wiley, 2023. https://doi.org/10.1002/1873-3468.14540. ieee: M. Loose, A. Auer, G. Brognara, H. R. Budiman, L. M. Kowalski, and I. Matijevic, “In vitro reconstitution of small GTPase regulation,” FEBS Letters, vol. 597, no. 6. Wiley, pp. 762–777, 2023. ista: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. 2023. In vitro reconstitution of small GTPase regulation. FEBS Letters. 597(6), 762–777. mla: Loose, Martin, et al. “In Vitro Reconstitution of Small GTPase Regulation.” FEBS Letters, vol. 597, no. 6, Wiley, 2023, pp. 762–77, doi:10.1002/1873-3468.14540. short: M. Loose, A. Auer, G. Brognara, H.R. Budiman, L.M. Kowalski, I. Matijevic, FEBS Letters 597 (2023) 762–777. corr_author: '1' date_created: 2023-01-12T12:09:58Z date_published: 2023-03-01T00:00:00Z date_updated: 2024-10-09T21:03:42Z day: '01' ddc: - '570' department: - _id: MaLo doi: 10.1002/1873-3468.14540 external_id: isi: - '000891573000001' pmid: - '36448231' file: - access_level: open_access checksum: 7492244d3f9c5faa1347ef03f6e5bc84 content_type: application/pdf creator: dernst date_created: 2023-08-16T08:31:04Z date_updated: 2023-08-16T08:31:04Z file_id: '14063' file_name: 2023_FEBSLetters_Loose.pdf file_size: 3148143 relation: main_file success: 1 file_date_updated: 2023-08-16T08:31:04Z has_accepted_license: '1' intvolume: ' 597' isi: 1 issue: '6' keyword: - Cell Biology - Genetics - Molecular Biology - Biochemistry - Structural Biology - Biophysics language: - iso: eng month: '03' oa: 1 oa_version: Published Version page: 762-777 pmid: 1 publication: FEBS Letters publication_identifier: eissn: - 1873-3468 issn: - 0014-5793 publication_status: published publisher: Wiley quality_controlled: '1' scopus_import: '1' status: public title: In vitro reconstitution of small GTPase regulation tmp: image: /images/cc_by_nc_nd.png legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) short: CC BY-NC-ND (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 597 year: '2023' ... --- _id: '14039' 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. 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. article_processing_charge: Yes (via OA deal) article_type: original author: - first_name: Thomas A. full_name: Leonard, Thomas A. last_name: Leonard - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 - first_name: Sascha full_name: Martens, Sascha last_name: Martens citation: ama: Leonard TA, Loose M, Martens S. The membrane surface as a platform that organizes cellular and biochemical processes. Developmental Cell. 2023;58(15):1315-1332. doi:10.1016/j.devcel.2023.06.001 apa: Leonard, T. A., Loose, M., & Martens, S. (2023). The membrane surface as a platform that organizes cellular and biochemical processes. Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2023.06.001 chicago: Leonard, Thomas A., Martin Loose, and Sascha Martens. “The Membrane Surface as a Platform That Organizes Cellular and Biochemical Processes.” Developmental Cell. Elsevier, 2023. https://doi.org/10.1016/j.devcel.2023.06.001. ieee: T. A. Leonard, M. Loose, and S. Martens, “The membrane surface as a platform that organizes cellular and biochemical processes,” Developmental Cell, vol. 58, no. 15. Elsevier, pp. 1315–1332, 2023. ista: Leonard TA, Loose M, Martens S. 2023. The membrane surface as a platform that organizes cellular and biochemical processes. Developmental Cell. 58(15), 1315–1332. mla: Leonard, Thomas A., et al. “The Membrane Surface as a Platform That Organizes Cellular and Biochemical Processes.” Developmental Cell, vol. 58, no. 15, Elsevier, 2023, pp. 1315–32, doi:10.1016/j.devcel.2023.06.001. short: T.A. Leonard, M. Loose, S. Martens, Developmental Cell 58 (2023) 1315–1332. corr_author: '1' date_created: 2023-08-13T22:01:12Z date_published: 2023-08-07T00:00:00Z date_updated: 2024-10-22T11:40:18Z day: '07' ddc: - '570' department: - _id: MaLo doi: 10.1016/j.devcel.2023.06.001 external_id: isi: - '001059110400001' pmid: - '37419118' file: - access_level: open_access checksum: d8c5dc97cd40c26da2ec98ae723ab368 content_type: application/pdf creator: dernst date_created: 2023-08-14T07:57:55Z date_updated: 2023-08-14T07:57:55Z file_id: '14049' file_name: 2023_DevelopmentalCell_Leonard.pdf file_size: 3184217 relation: main_file success: 1 file_date_updated: 2023-08-14T07:57:55Z has_accepted_license: '1' intvolume: ' 58' isi: 1 issue: '15' language: - iso: eng month: '08' oa: 1 oa_version: Published Version page: 1315-1332 pmid: 1 project: - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division - _id: bd6ae2ca-d553-11ed-ba76-a4aa239da5ee grant_number: '101045340' name: Synthetic and structural biology of Rab GTPase networks publication: Developmental Cell publication_identifier: eissn: - 1878-1551 issn: - 1534-5807 publication_status: published publisher: Elsevier quality_controlled: '1' scopus_import: '1' status: public title: The membrane surface as a platform that organizes cellular and biochemical processes tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 58 year: '2023' ... --- _id: '14785' abstract: - lang: eng 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 Synechocystis 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. 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" article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Fabian full_name: Nies, Fabian last_name: Nies - first_name: Tanita full_name: Wein, Tanita last_name: Wein - first_name: Dustin M. full_name: Hanke, Dustin M. last_name: Hanke - first_name: Benjamin L full_name: Springstein, Benjamin L id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083 last_name: Springstein orcid: 0000-0002-3461-5391 - first_name: Jaime full_name: Alcorta, Jaime last_name: Alcorta - first_name: Claudia full_name: Taubenheim, Claudia last_name: Taubenheim - first_name: Tal full_name: Dagan, Tal last_name: Dagan citation: 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. Environmental Microbiology Reports. 2023;15(6):656-668. doi:10.1111/1758-2229.13203 apa: Nies, F., Wein, T., Hanke, D. M., Springstein, B. L., 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. Wiley. https://doi.org/10.1111/1758-2229.13203 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.” Environmental Microbiology Reports. Wiley, 2023. https://doi.org/10.1111/1758-2229.13203. ieee: F. Nies et al., “Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803,” Environmental Microbiology Reports, vol. 15, no. 6. Wiley, pp. 656–668, 2023. 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. mla: Nies, Fabian, et al. “Role of Natural Transformation in the Evolution of Small Cryptic Plasmids in Synechocystis Sp. PCC 6803.” Environmental Microbiology Reports, vol. 15, no. 6, Wiley, 2023, pp. 656–68, doi:10.1111/1758-2229.13203. short: F. Nies, T. Wein, D.M. Hanke, B.L. Springstein, J. Alcorta, C. Taubenheim, T. Dagan, Environmental Microbiology Reports 15 (2023) 656–668. date_created: 2024-01-10T10:41:07Z date_published: 2023-12-01T00:00:00Z date_updated: 2024-01-16T09:46:12Z day: '01' ddc: - '570' department: - _id: MaLo doi: 10.1111/1758-2229.13203 external_id: isi: - '001080203100001' pmid: - '37794696' file: - access_level: open_access checksum: d09ebb68fee61f4e2e09ec286c9cf1d3 content_type: application/pdf creator: dernst date_created: 2024-01-16T09:42:10Z date_updated: 2024-01-16T09:42:10Z file_id: '14810' file_name: 2023_EnvirMicroBiolReports_Nies.pdf file_size: 1518350 relation: main_file success: 1 file_date_updated: 2024-01-16T09:42:10Z has_accepted_license: '1' intvolume: ' 15' isi: 1 issue: '6' keyword: - Agricultural and Biological Sciences (miscellaneous) - Ecology - Evolution - Behavior and Systematics language: - iso: eng month: '12' oa: 1 oa_version: Published Version page: 656-668 pmid: 1 publication: Environmental Microbiology Reports publication_identifier: eissn: - 1758-2229 publication_status: published publisher: Wiley quality_controlled: '1' status: public title: Role of natural transformation in the evolution of small cryptic plasmids in Synechocystis sp. PCC 6803 tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 volume: 15 year: '2023' ... --- _id: '13116' abstract: - lang: eng text: 'The emergence of large-scale order in self-organized systems relies on local interactions between individual components. During bacterial cell division, FtsZ -- a prokaryotic homologue of the eukaryotic protein tubulin -- polymerizes into treadmilling filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments can form dynamic chiral assemblies. However, how the active and passive properties of individual filaments relate to these large-scale self-organized structures remains poorly understood. Here, we connect single filament properties with the mesoscopic scale by combining minimal active matter simulations and biochemical reconstitution experiments. We show that density and flexibility of active chiral filaments define their global order. At intermediate densities, curved, flexible filaments organize into chiral rings and polar bands. An effectively nematic organization dominates for high densities and for straight, mutant filaments with increased rigidity. Our predicted phase diagram captures these features quantitatively, demonstrating how the flexibility, density and chirality of active filaments affect their collective behaviour. Our findings shed light on the fundamental properties of active chiral matter and explain how treadmilling FtsZ filaments organize during bacterial cell division. ' acknowledged_ssus: - _id: Bio - _id: LifeSc acknowledgement: 'This work was supported by the European Research Council through grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM collaborative research program. Z.D. has received funding from Doctoral Programme of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria), Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments on the manuscript. We are also thankful for the support by the Scientific Service Units (SSU) of IST Austria through resources provided by the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF). ' article_processing_charge: No author: - first_name: Zuzana full_name: Dunajova, Zuzana id: 4B39F286-F248-11E8-B48F-1D18A9856A87 last_name: Dunajova - first_name: Batirtze full_name: Prats Mateu, Batirtze id: 299FE892-F248-11E8-B48F-1D18A9856A87 last_name: Prats Mateu - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Keesiang full_name: Lim, Keesiang last_name: Lim - first_name: Dörte full_name: Brandis, Dörte last_name: Brandis - first_name: Philipp full_name: Velicky, Philipp id: 39BDC62C-F248-11E8-B48F-1D18A9856A87 last_name: Velicky orcid: 0000-0002-2340-7431 - first_name: Johann G full_name: Danzl, Johann G id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87 last_name: Danzl orcid: 0000-0001-8559-3973 - first_name: Richard W. full_name: Wong, Richard W. last_name: Wong - first_name: Jens full_name: Elgeti, Jens last_name: Elgeti - first_name: Edouard B full_name: Hannezo, Edouard B id: 3A9DB764-F248-11E8-B48F-1D18A9856A87 last_name: Hannezo orcid: 0000-0001-6005-1561 - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 citation: ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible active filaments. 2023. doi:10.15479/AT:ISTA:13116 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. https://doi.org/10.15479/AT:ISTA:13116 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. https://doi.org/10.15479/AT:ISTA:13116. ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments.” Institute of Science and Technology Austria, 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, 10.15479/AT:ISTA:13116. mla: Dunajova, Zuzana, et al. Chiral and Nematic Phases of Flexible Active Filaments. Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:13116. 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). corr_author: '1' date_created: 2023-06-02T12:30:40Z date_published: 2023-07-26T00:00:00Z date_updated: 2026-03-17T12:02:11Z day: '26' ddc: - '539' department: - _id: MaLo - _id: EdHa - _id: JoDa doi: 10.15479/AT:ISTA:13116 ec_funded: 1 file: - access_level: open_access checksum: 4b4ec5d4df7672b3af5ba23b126b171b content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document creator: pradler date_created: 2023-08-08T11:17:28Z date_updated: 2023-08-08T11:17:28Z file_id: '13983' file_name: ReadMe File.docx file_size: 13111 relation: main_file success: 1 - access_level: open_access checksum: 6f1673d6ae4f547cd49cfe7f87d9ab7e content_type: application/octet-stream creator: pradler date_created: 2023-07-25T06:55:43Z date_updated: 2023-07-25T06:55:43Z file_id: '13298' file_name: TIRF_FtsZ WT 0.625µM.7z.001 file_size: 1499504777 relation: main_file success: 1 - access_level: open_access checksum: bc0dea871af164f7419ac838a34a4162 content_type: application/octet-stream creator: pradler date_created: 2023-07-25T08:31:07Z date_updated: 2023-07-25T08:31:07Z file_id: '13306' file_name: TIRF_FtsZ WT 0.900µM.7z.001 file_size: 3986437211 relation: main_file success: 1 - 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access_level: open_access checksum: 848456b4230c086e8999f57d57dba7f1 content_type: text/csv creator: mloose date_created: 2023-08-03T19:51:54Z date_updated: 2023-08-03T19:51:54Z file_id: '13952' file_name: Fig3a_F200.csv file_size: 59166206 relation: main_file success: 1 file_date_updated: 2023-08-08T11:17:28Z has_accepted_license: '1' month: '07' oa: 1 oa_version: Published Version project: - _id: 2595697A-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '679239' name: Self-Organization of the Bacterial Cell - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division - _id: 34d75525-11ca-11ed-8bc3-89b6307fee9d grant_number: '26360' name: Motile active matter models of migrating cells and chiral filaments publisher: Institute of Science and Technology Austria related_material: record: - id: '13314' relation: used_in_publication status: public - id: '21423' relation: used_in_publication status: public status: public title: Chiral and nematic phases of flexible active filaments tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: research_data user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87 year: '2023' ... --- _id: '13314' abstract: - lang: eng text: The emergence of large-scale order in self-organized systems relies on local interactions between individual components. During bacterial cell division, FtsZ—a prokaryotic homologue of the eukaryotic protein tubulin—polymerizes into treadmilling filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments can form dynamic chiral assemblies. However, how the active and passive properties of individual filaments relate to these large-scale self-organized structures remains poorly understood. Here we connect single-filament properties with the mesoscopic scale by combining minimal active matter simulations and biochemical reconstitution experiments. We show that the density and flexibility of active chiral filaments define their global order. At intermediate densities, curved, flexible filaments organize into chiral rings and polar bands. An effectively nematic organization dominates for high densities and for straight, mutant filaments with increased rigidity. Our predicted phase diagram quantitatively captures these features, demonstrating how the flexibility, density and chirality of the active filaments affect their collective behaviour. Our findings shed light on the fundamental properties of active chiral matter and explain how treadmilling FtsZ filaments organize during bacterial cell division. acknowledged_ssus: - _id: Bio - _id: LifeSc acknowledgement: 'This work was supported by the European Research Council through grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM collaborative research program. Z.D. has received funding from Doctoral Programme of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria), Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments on the manuscript. We are also thankful for the support by the Scientific Service Units (SSU) of IST Austria through resources provided by the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF).' article_processing_charge: Yes (in subscription journal) article_type: original author: - first_name: Zuzana full_name: Dunajova, Zuzana id: 4B39F286-F248-11E8-B48F-1D18A9856A87 last_name: Dunajova - first_name: Batirtze full_name: Prats Mateu, Batirtze id: 299FE892-F248-11E8-B48F-1D18A9856A87 last_name: Prats Mateu - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' - first_name: Keesiang full_name: Lim, Keesiang last_name: Lim - first_name: Dörte full_name: Brandis, Dörte id: 21d64d35-f128-11eb-9611-b8bcca7a12fd last_name: Brandis - first_name: Philipp full_name: Velicky, Philipp id: 39BDC62C-F248-11E8-B48F-1D18A9856A87 last_name: Velicky orcid: 0000-0002-2340-7431 - first_name: Johann G full_name: Danzl, Johann G id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87 last_name: Danzl orcid: 0000-0001-8559-3973 - first_name: Richard W. full_name: Wong, Richard W. last_name: Wong - first_name: Jens full_name: Elgeti, Jens last_name: Elgeti - first_name: Edouard B full_name: Hannezo, Edouard B id: 3A9DB764-F248-11E8-B48F-1D18A9856A87 last_name: Hannezo orcid: 0000-0001-6005-1561 - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 citation: ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible active filaments. Nature Physics. 2023;19:1916-1926. doi:10.1038/s41567-023-02218-w 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. Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-023-02218-w 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.” Nature Physics. Springer Nature, 2023. https://doi.org/10.1038/s41567-023-02218-w. ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments,” Nature Physics, vol. 19. Springer Nature, pp. 1916–1926, 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. Nature Physics. 19, 1916–1926. mla: Dunajova, Zuzana, et al. “Chiral and Nematic Phases of Flexible Active Filaments.” Nature Physics, vol. 19, Springer Nature, 2023, pp. 1916–26, doi:10.1038/s41567-023-02218-w. 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. corr_author: '1' date_created: 2023-07-27T14:44:45Z date_published: 2023-12-01T00:00:00Z date_updated: 2026-03-18T14:11:35Z day: '01' ddc: - '530' department: - _id: JoDa - _id: EdHa - _id: MaLo - _id: GradSch doi: 10.1038/s41567-023-02218-w ec_funded: 1 external_id: isi: - '001178645300041' pmid: - '38075437' file: - access_level: open_access checksum: bc7673ca07d37309013a86166577b2f7 content_type: application/pdf creator: dernst date_created: 2024-01-30T14:28:30Z date_updated: 2024-01-30T14:28:30Z file_id: '14916' file_name: 2023_NaturePhysics_Dunajova.pdf file_size: 22471673 relation: main_file success: 1 file_date_updated: 2024-01-30T14:28:30Z has_accepted_license: '1' intvolume: ' 19' isi: 1 language: - iso: eng month: '12' oa: 1 oa_version: Published Version page: 1916-1926 pmid: 1 project: - _id: 2595697A-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '679239' name: Self-Organization of the Bacterial Cell - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division - _id: 34d75525-11ca-11ed-8bc3-89b6307fee9d grant_number: '26360' name: Motile active matter models of migrating cells and chiral filaments publication: Nature Physics publication_identifier: eissn: - 1745-2481 issn: - 1745-2473 publication_status: published publisher: Springer Nature quality_controlled: '1' related_material: record: - id: '13116' relation: research_data status: public - id: '21423' relation: dissertation_contains status: public - id: '21439' relation: research_data status: public scopus_import: '1' status: public title: Chiral and nematic phases of flexible active filaments tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: journal_article user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345 volume: 19 year: '2023' ... --- OA_place: publisher _id: '14280' abstract: - lang: eng 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." acknowledged_ssus: - _id: Bio - _id: LifeSc alternative_title: - ISTA Thesis article_processing_charge: No author: - first_name: Philipp full_name: Radler, Philipp id: 40136C2A-F248-11E8-B48F-1D18A9856A87 last_name: Radler orcid: '0000-0001-9198-2182 ' citation: ama: Radler P. Spatiotemporal signaling during assembly of the bacterial divisome. 2023. doi:10.15479/at:ista:14280 apa: Radler, P. (2023). Spatiotemporal signaling during assembly of the bacterial divisome. Institute of Science and Technology Austria. https://doi.org/10.15479/at:ista:14280 chicago: Radler, Philipp. “Spatiotemporal Signaling during Assembly of the Bacterial Divisome.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/at:ista:14280. ieee: 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. mla: Radler, Philipp. Spatiotemporal Signaling during Assembly of the Bacterial Divisome. Institute of Science and Technology Austria, 2023, doi:10.15479/at:ista:14280. short: P. Radler, Spatiotemporal Signaling during Assembly of the Bacterial Divisome, Institute of Science and Technology Austria, 2023. corr_author: '1' date_created: 2023-09-06T10:58:25Z date_published: 2023-09-25T00:00:00Z date_updated: 2026-04-07T14:06:05Z day: '25' ddc: - '572' degree_awarded: PhD department: - _id: GradSch - _id: MaLo doi: 10.15479/at:ista:14280 ec_funded: 1 file: - access_level: closed checksum: 87eef11fbc5c7df0826f12a3a629b444 content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document creator: pradler date_created: 2023-10-04T10:11:53Z date_updated: 2024-10-05T22:30:03Z embargo_to: open_access file_id: '14390' file_name: PhD Thesis_Philipp Radler_20231004.docx file_size: 114932847 relation: source_file - access_level: open_access checksum: 3253e099b7126469d941fd9419d68b4f content_type: application/pdf creator: pradler date_created: 2023-10-04T10:11:21Z date_updated: 2024-10-05T22:30:03Z embargo: 2024-10-04 file_id: '14391' file_name: PhD Thesis_Philipp Radler_20231004.pdf file_size: 37838778 relation: main_file file_date_updated: 2024-10-05T22:30:03Z has_accepted_license: '1' keyword: - Cell Division - Reconstitution - FtsZ - FtsA - Divisome - E.coli language: - iso: eng month: '09' oa: 1 oa_version: Published Version page: '156' project: - _id: 2595697A-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '679239' name: Self-Organization of the Bacterial Cell - _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d grant_number: P34607 name: In vitro reconstitution of bacterial cell division - _id: 2596EAB6-B435-11E9-9278-68D0E5697425 grant_number: ALTF 2015-1163 name: Synthesis of bacterial cell wall - _id: 259B655A-B435-11E9-9278-68D0E5697425 grant_number: LT000824/2016 name: Reconstitution of bacterial cell wall synthesis publication_identifier: isbn: - 978-3-99078-033-6 issn: - 2663-337X publication_status: published publisher: Institute of Science and Technology Austria related_material: record: - id: '10934' relation: research_data status: public - id: '11373' relation: part_of_dissertation status: public - id: '7387' relation: part_of_dissertation status: public status: public supervisor: - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 title: Spatiotemporal signaling during assembly of the bacterial divisome tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: dissertation user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd year: '2023' ... --- OA_place: publisher _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. " acknowledged_ssus: - _id: EM-Fac - _id: Bio - _id: LifeSc alternative_title: - ISTA Thesis article_processing_charge: No author: - first_name: Nataliia full_name: Gnyliukh, Nataliia id: 390C1120-F248-11E8-B48F-1D18A9856A87 last_name: Gnyliukh orcid: 0000-0002-2198-0509 citation: ama: Gnyliukh N. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. 2023. doi:10.15479/at:ista:14510 apa: Gnyliukh, N. (2023). Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. Institute of Science and Technology Austria. https://doi.org/10.15479/at:ista:14510 chicago: Gnyliukh, Nataliia. “Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/at:ista:14510. ieee: N. Gnyliukh, “Mechanism of clathrin-coated vesicle  formation during endocytosis in plants,” Institute of Science and Technology Austria, 2023. ista: Gnyliukh N. 2023. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. Institute of Science and Technology Austria. mla: Gnyliukh, Nataliia. Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants. Institute of Science and Technology Austria, 2023, doi:10.15479/at:ista:14510. short: N. Gnyliukh, Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants, Institute of Science and Technology Austria, 2023. corr_author: '1' date_created: 2023-11-10T09:10:06Z date_published: 2023-11-10T00:00:00Z date_updated: 2026-04-29T22:30:32Z day: '10' ddc: - '570' degree_awarded: PhD department: - _id: GradSch - _id: JiFr - _id: MaLo doi: 10.15479/at:ista:14510 ec_funded: 1 file: - access_level: closed checksum: 3d5e680bfc61f98e308c434f45cc9bd6 content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document creator: ngnyliuk date_created: 2023-11-20T09:18:51Z date_updated: 2024-11-23T23:30:38Z embargo_to: open_access file_id: '14567' file_name: Thesis_Gnyliukh_final_08_11_23.docx file_size: 20824903 relation: source_file - access_level: open_access checksum: bfc96d47fc4e7e857dd71656097214a4 content_type: application/pdf creator: ngnyliuk date_created: 2023-11-20T09:23:11Z date_updated: 2024-11-23T23:30:38Z embargo: 2024-11-23 file_id: '14568' file_name: Thesis_Gnyliukh_final_20_11_23.pdf file_size: 24871844 relation: main_file file_date_updated: 2024-11-23T23:30:38Z has_accepted_license: '1' keyword: - Clathrin-Mediated Endocytosis - vesicle scission - Dynamin-Related Protein 2 - SH3P2 - TPLATE complex - Total internal reflection fluorescence microscopy - Arabidopsis thaliana language: - iso: eng month: '11' oa: 1 oa_version: Published Version page: '180' project: - _id: 2564DBCA-B435-11E9-9278-68D0E5697425 call_identifier: H2020 grant_number: '665385' name: International IST Doctoral Program publication_identifier: isbn: - 978-3-99078-037-4 issn: - 2663-337X publication_status: published publisher: Institute of Science and Technology Austria related_material: record: - id: '14591' relation: part_of_dissertation status: public - id: '9887' relation: part_of_dissertation status: public - id: '8139' relation: part_of_dissertation status: public status: public supervisor: - first_name: Jiří full_name: Friml, Jiří id: 4159519E-F248-11E8-B48F-1D18A9856A87 last_name: Friml orcid: 0000-0002-8302-7596 - first_name: Martin full_name: Loose, Martin id: 462D4284-F248-11E8-B48F-1D18A9856A87 last_name: Loose orcid: 0000-0001-7309-9724 title: Mechanism of clathrin-coated vesicle formation during endocytosis in plants tmp: image: /images/cc_by.png legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) short: CC BY (4.0) type: dissertation user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd year: '2023' ...