--- 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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_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: '20370' abstract: - lang: eng text: The Huntingtin protein (HTT), named for its role in Huntington’s disease, has been best understood as a scaffolding protein that promotes vesicle transport by molecular motors along microtubules. Here, we show that HTT also interacts with the actin cytoskeleton, and its loss of function disturbs the morphology and function of the axonal growth cone. We demonstrate that HTT organizes F-actin into bundles. Cryo–electron tomography (cryo-ET) and subtomogram averaging (STA) structural analyses reveal that HTT’s N-terminal HEAT and Bridge domains wrap around F-actin, while the C-terminal HEAT domain is displaced; furthermore, HTT dimerizes via the N-HEAT domain to bridge parallel actin filaments separated by ~20 nanometers. Our study provides the structural basis for understanding how HTT interacts with and organizes the actin cytoskeleton. acknowledgement: 'We thank C. Cuveillier, J. Delaroche, T. Ferraro, and A. Zanchi for help with TIRF experiments, electron microscopy preparation, data analysis, and cell cultures, respectively; A. Antkowiak, C. Bosc, C. Fassier, A. Fourest-Lieuvin, and V. Brandt for helpful discussions. We acknowledge the contribution of the Photonic Imaging Center of Grenoble Institute Neuroscience which is part of the ISdV core facility and certified by the IBiSA label and ICM.Quant (RRID:SCR_026393) core facility of the Paris Brain Institute (ICM); the AniRA lentivector production facility from the CELPHEDIA Infrastructure and SFR Biosciences (UAR3444/CNRS, US8/Inserm, ENS de Lyon, UCBL); the Scientific Service Units (SSUs) of ISTA through resources provided by Scientific Computing (SciComp, A. Schloegl and S. Elefante); and the Electron Microscopy Facility (EMF, V.V. Hodirnau). The software programs used for the processing were supported by SBGrid (www.sbgrid.org). This work was supported by the Agence Nationale pour la Recherche (AXYON: ANR-18-CE16-0009-01, S.H.), Austrian Science Fund (FWF) grants (P33367, F.K.M.S.; E435, J.M.H.), ChanZuckerberg Initiative (CZI) grant (DAF2021-234754, F.K.M.S.), Hereditary Disease Foundation Research Grant (HDF 990846, M.C.), European Union (ERC: ActinID 101076260, F.K.M.S.), Fondation pour la Recherche Médicale (FRM: équipe labellisée DEQ202203014675, S.H.; PhD fellowship, FDT202001010865, R.C.), Korea Health Industry Development Institute (KHIDI) (Korea-Switzerland global research support grant: RS-2023-00266300, J.-J.S.), National Research Foundation (NRF) of Korea (Korea-Austria collaborative grant NRF-2019K1A3A1A181160, J.-J.S. and F.K.M.S.; NRF-2020R1A2B5B03001517 and RS-2024-00333346 and RS-2024-00436173, J.-J.S.; 2021R1C1C1006700, D.K.).' article_number: eadw4124 article_processing_charge: Yes article_type: original author: - first_name: Rémi full_name: Carpentier, Rémi last_name: Carpentier - first_name: Jaesung full_name: Kim, Jaesung last_name: Kim - first_name: Mariacristina full_name: Capizzi, Mariacristina last_name: Capizzi - first_name: Hyeongju full_name: Kim, Hyeongju last_name: Kim - first_name: Florian full_name: Fäßler, Florian id: 404F5528-F248-11E8-B48F-1D18A9856A87 last_name: Fäßler orcid: 0000-0001-7149-769X - first_name: Jesse full_name: Hansen, Jesse id: 1063c618-6f9b-11ec-9123-f912fccded63 last_name: Hansen orcid: 0000-0001-7967-2085 - first_name: Min Jeong full_name: Kim, Min Jeong last_name: Kim - first_name: Eric full_name: Denarier, Eric last_name: Denarier - first_name: Béatrice full_name: Blot, Béatrice last_name: Blot - first_name: Marine full_name: Degennaro, Marine last_name: Degennaro - first_name: Sophia full_name: Labou, Sophia last_name: Labou - first_name: Isabelle full_name: Arnal, Isabelle last_name: Arnal - first_name: Maria J. full_name: Marcaida, Maria J. last_name: Marcaida - first_name: Matteo Dal full_name: Peraro, Matteo Dal last_name: Peraro - first_name: Doory full_name: Kim, Doory last_name: Kim - 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: Ji-Joon full_name: Song, Ji-Joon last_name: Song - first_name: Sandrine full_name: Humbert, Sandrine last_name: Humbert citation: ama: Carpentier R, Kim J, Capizzi M, et al. Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization. Science Advances. 2025;11(38). doi:10.1126/sciadv.adw4124 apa: Carpentier, R., Kim, J., Capizzi, M., Kim, H., Fäßler, F., Hansen, J., … Humbert, S. (2025). Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization. Science Advances. AAAS. https://doi.org/10.1126/sciadv.adw4124 chicago: Carpentier, Rémi, Jaesung Kim, Mariacristina Capizzi, Hyeongju Kim, Florian Fäßler, Jesse Hansen, Min Jeong Kim, et al. “Structure of the Huntingtin F-Actin Complex Reveals Its Role in Cytoskeleton Organization.” Science Advances. AAAS, 2025. https://doi.org/10.1126/sciadv.adw4124. ieee: R. Carpentier et al., “Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization,” Science Advances, vol. 11, no. 38. AAAS, 2025. ista: Carpentier R, Kim J, Capizzi M, Kim H, Fäßler F, Hansen J, Kim MJ, Denarier E, Blot B, Degennaro M, Labou S, Arnal I, Marcaida MJ, Peraro MD, Kim D, Schur FK, Song J-J, Humbert S. 2025. Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization. Science Advances. 11(38), eadw4124. mla: Carpentier, Rémi, et al. “Structure of the Huntingtin F-Actin Complex Reveals Its Role in Cytoskeleton Organization.” Science Advances, vol. 11, no. 38, eadw4124, AAAS, 2025, doi:10.1126/sciadv.adw4124. short: R. Carpentier, J. Kim, M. Capizzi, H. Kim, F. Fäßler, J. Hansen, M.J. Kim, E. Denarier, B. Blot, M. Degennaro, S. Labou, I. Arnal, M.J. Marcaida, M.D. Peraro, D. Kim, F.K. Schur, J.-J. Song, S. Humbert, Science Advances 11 (2025). corr_author: '1' date_created: 2025-09-22T08:00:52Z date_published: 2025-09-19T00:00:00Z date_updated: 2026-02-16T11:45:54Z day: '19' ddc: - '570' department: - _id: FlSc doi: 10.1126/sciadv.adw4124 external_id: isi: - '001575751700013' pmid: - '40971423' file: - access_level: open_access checksum: 4e2407bdabf8d53f399eb8a20d86218e content_type: application/pdf creator: dernst date_created: 2025-09-23T07:57:51Z date_updated: 2025-09-23T07:57:51Z file_id: '20372' file_name: 2025_ScienceAdvance_Carpentier.pdf file_size: 3599137 relation: main_file success: 1 file_date_updated: 2025-09-23T07:57:51Z has_accepted_license: '1' intvolume: ' 11' isi: 1 issue: '38' language: - iso: eng month: '09' oa: 1 oa_version: Published Version pmid: 1 project: - _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A grant_number: P33367 name: Structure and isoform diversity of the Arp2/3 complex - _id: 7bd318a1-9f16-11ee-852c-cc9217763180 grant_number: E435 name: In Situ Actin Structures via Hybrid Cryo-electron Microscopy - _id: 62909c6f-2b32-11ec-9570-e1476aab5308 grant_number: CZI01 name: CryoMinflux-guided in-situ molecular census and structure determination - _id: bd980d18-d553-11ed-ba76-ceaa645c97eb grant_number: '101076260' name: A molecular atlas of Actin filament IDentities in the cell motility machinery publication: Science Advances publication_identifier: issn: - 2375-2548 publication_status: published publisher: AAAS quality_controlled: '1' scopus_import: '1' status: public title: Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization 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: 11 year: '2025' ...