[{"publication":"Science","citation":{"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.","chicago":"Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu, Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>. AAAS, 2026. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>.","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).","ama":"Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. 2026;392(6795). doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>","ieee":"B. L. Springstein <i>et al.</i>, “Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape,” <i>Science</i>, vol. 392, no. 6795. AAAS, 2026.","apa":"Springstein, B. L., Javoor, M., Megrian, D., Hajdu, R., Hanke, D. M., Zens, B., … Loose, M. (2026). Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. AAAS. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>","mla":"Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>, vol. 392, no. 6795, eaea6343, AAAS, 2026, doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>."},"abstract":[{"text":"Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal system named CorMR with a function in cell shape control rather than DNA segregation. Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed that CorM formed dynamically unstable, antiparallel double-stranded filaments that were recruited to the membrane by CorR through an amphipathic helix conserved in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which excluded them from the poles and division plane. Comparative genomics indicated that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity, highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.","lang":"eng"}],"date_published":"2026-04-16T00:00:00Z","article_number":"eaea6343","month":"04","date_updated":"2026-04-28T13:29:05Z","issue":"6795","title":"Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape","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.).","language":[{"iso":"eng"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"ScienComp"},{"_id":"EM-Fac"},{"_id":"LifeSc"}],"publisher":"AAAS","type":"journal_article","pmid":1,"doi":"10.1126/science.aea6343","article_processing_charge":"No","publication_identifier":{"eissn":["1095-9203"],"issn":["0036-8075"]},"corr_author":"1","status":"public","date_created":"2026-04-26T22:01:46Z","external_id":{"pmid":["41990175"]},"intvolume":"       392","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Springstein, Benjamin L","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","orcid":"0000-0002-3461-5391","last_name":"Springstein","first_name":"Benjamin L"},{"full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","orcid":"0000-0003-2311-2112","first_name":"Manjunath","last_name":"Javoor"},{"full_name":"Megrian, Daniela","last_name":"Megrian","first_name":"Daniela"},{"last_name":"Hajdu","first_name":"Roman","id":"ffab949d-133f-11ed-8f02-94de21ace503","full_name":"Hajdu, Roman"},{"last_name":"Hanke","first_name":"Dustin M.","full_name":"Hanke, Dustin M."},{"last_name":"Zens","first_name":"Bettina","orcid":"0000-0002-9561-1239","full_name":"Zens, Bettina","id":"45FD126C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Gregor L.","last_name":"Weiss","full_name":"Weiss, Gregor L."},{"first_name":"Florian Km","last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian Km","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"oa_version":"None","volume":392,"ec_funded":1,"project":[{"call_identifier":"H2020","name":"IST-BRIDGE: International postdoctoral program","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413"},{"_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb","grant_number":"101076260","name":"A molecular atlas of Actin filament IDentities in the cell motility machinery"}],"publication_status":"published","scopus_import":"1","department":[{"_id":"MaLo"},{"_id":"FlSc"},{"_id":"GradSch"},{"_id":"EM-Fac"}],"quality_controlled":"1","OA_type":"closed access","day":"16","year":"2026","_id":"21762"},{"title":"Files for \"Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape\"","file_date_updated":"2025-07-02T08:10:21Z","ec_funded":1,"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","project":[{"call_identifier":"H2020","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","name":"IST-BRIDGE: International postdoctoral program"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb"}],"publisher":"Institute of Science and Technology Austria","type":"research_data","user_id":"68b8ca59-c5b3-11ee-8790-cd641c68093d","oa_version":"Published Version","author":[{"id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","full_name":"Springstein, Benjamin L","orcid":"0000-0002-3461-5391","first_name":"Benjamin L","last_name":"Springstein"}],"citation":{"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.","short":"B.L. Springstein, (2025).","ama":"Springstein BL. Files for “Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape.” 2025. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:19915\">10.15479/AT:ISTA:19915</a>","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. <a href=\"https://doi.org/10.15479/AT:ISTA:19915\">https://doi.org/10.15479/AT:ISTA:19915</a>.","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, <a href=\"https://doi.org/10.15479/AT:ISTA:19915\">10.15479/AT:ISTA:19915</a>.","mla":"Springstein, Benjamin L. <i>Files for “Evolutionary Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cyanobacterial Cell Shape.”</i> Institute of Science and Technology Austria, 2025, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:19915\">10.15479/AT:ISTA:19915</a>.","apa":"Springstein, B. L. (2025). 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L","last_name":"Springstein"},{"last_name":"Javoor","first_name":"Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","contributor_type":"researcher"},{"first_name":"Daniela","last_name":"Megrian","contributor_type":"researcher"},{"contributor_type":"researcher","id":"ffab949d-133f-11ed-8f02-94de21ace503","first_name":"Roman","last_name":"Hajdu"},{"contributor_type":"researcher","first_name":"Dustin M","last_name":"Hanke"},{"contributor_type":"researcher","orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian KM","last_name":"Schur"},{"first_name":"Martin","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","contributor_type":"supervisor"}],"date_created":"2025-06-27T07:34:52Z","_id":"19915","status":"public","doi":"10.15479/AT:ISTA:19915","tmp":{"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)","image":"/images/cc_by_nc_nd.png","short":"CC BY-NC-ND (4.0)"},"article_processing_charge":"No","department":[{"_id":"MaLo"}],"corr_author":"1"},{"OA_place":"publisher","publisher":"AAAS","DOAJ_listed":"1","type":"journal_article","pmid":1,"issue":"38","title":"Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization","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.).","language":[{"iso":"eng"}],"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."}],"citation":{"mla":"Carpentier, Rémi, et al. “Structure of the Huntingtin F-Actin Complex Reveals Its Role in Cytoskeleton Organization.” <i>Science Advances</i>, vol. 11, no. 38, eadw4124, AAAS, 2025, doi:<a href=\"https://doi.org/10.1126/sciadv.adw4124\">10.1126/sciadv.adw4124</a>.","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. <i>Science Advances</i>. AAAS. <a href=\"https://doi.org/10.1126/sciadv.adw4124\">https://doi.org/10.1126/sciadv.adw4124</a>","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).","ama":"Carpentier R, Kim J, Capizzi M, et al. Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization. <i>Science Advances</i>. 2025;11(38). doi:<a href=\"https://doi.org/10.1126/sciadv.adw4124\">10.1126/sciadv.adw4124</a>","ieee":"R. Carpentier <i>et al.</i>, “Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization,” <i>Science Advances</i>, 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.","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.” <i>Science Advances</i>. AAAS, 2025. <a href=\"https://doi.org/10.1126/sciadv.adw4124\">https://doi.org/10.1126/sciadv.adw4124</a>."},"oa":1,"date_updated":"2026-05-20T08:20:27Z","date_published":"2025-09-19T00:00:00Z","month":"09","article_number":"eadw4124","publication":"Science Advances","external_id":{"isi":["001575751700013"],"pmid":["40971423"]},"date_created":"2025-09-22T08:00:52Z","status":"public","APC_amount":"1395,61 EUR","PlanS_conform":"1","corr_author":"1","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"doi":"10.1126/sciadv.adw4124","article_processing_charge":"Yes","publication_identifier":{"issn":["2375-2548"]},"project":[{"_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","grant_number":"P33367","name":"Structure and isoform diversity of the Arp2/3 complex"},{"grant_number":"E435","_id":"7bd318a1-9f16-11ee-852c-cc9217763180","name":"In Situ Actin Structures via Hybrid Cryo-electron Microscopy"},{"grant_number":"CZI01","_id":"62909c6f-2b32-11ec-9570-e1476aab5308","name":"CryoMinflux-guided in-situ molecular census and structure determination"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb","grant_number":"101076260"},{"name":"FWF Open Access Fund","_id":"3AC91DDA-15DF-11EA-824D-93A3E7B544D1","call_identifier":"FWF"}],"publication_status":"published","file_date_updated":"2025-09-23T07:57:51Z","volume":11,"oa_version":"Published Version","author":[{"first_name":"Rémi","last_name":"Carpentier","full_name":"Carpentier, Rémi"},{"full_name":"Kim, Jaesung","last_name":"Kim","first_name":"Jaesung"},{"full_name":"Capizzi, Mariacristina","first_name":"Mariacristina","last_name":"Capizzi"},{"first_name":"Hyeongju","last_name":"Kim","full_name":"Kim, Hyeongju"},{"last_name":"Fäßler","first_name":"Florian","id":"404F5528-F248-11E8-B48F-1D18A9856A87","full_name":"Fäßler, Florian","orcid":"0000-0001-7149-769X"},{"orcid":"0000-0001-7967-2085","full_name":"Hansen, Jesse","id":"1063c618-6f9b-11ec-9123-f912fccded63","last_name":"Hansen","first_name":"Jesse"},{"first_name":"Min Jeong","last_name":"Kim","full_name":"Kim, Min Jeong"},{"first_name":"Eric","last_name":"Denarier","full_name":"Denarier, Eric"},{"last_name":"Blot","first_name":"Béatrice","full_name":"Blot, Béatrice"},{"last_name":"Degennaro","first_name":"Marine","full_name":"Degennaro, Marine"},{"full_name":"Labou, Sophia","first_name":"Sophia","last_name":"Labou"},{"first_name":"Isabelle","last_name":"Arnal","full_name":"Arnal, Isabelle"},{"full_name":"Marcaida, Maria J.","last_name":"Marcaida","first_name":"Maria J."},{"first_name":"Matteo Dal","last_name":"Peraro","full_name":"Peraro, Matteo Dal"},{"last_name":"Kim","first_name":"Doory","full_name":"Kim, Doory"},{"orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian KM","last_name":"Schur"},{"full_name":"Song, Ji-Joon","last_name":"Song","first_name":"Ji-Joon"},{"first_name":"Sandrine","last_name":"Humbert","full_name":"Humbert, Sandrine"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","file":[{"checksum":"4e2407bdabf8d53f399eb8a20d86218e","file_size":3599137,"relation":"main_file","file_id":"20372","date_updated":"2025-09-23T07:57:51Z","success":1,"content_type":"application/pdf","access_level":"open_access","file_name":"2025_ScienceAdvance_Carpentier.pdf","date_created":"2025-09-23T07:57:51Z","creator":"dernst"}],"article_type":"original","intvolume":"        11","year":"2025","ddc":["570"],"_id":"20370","day":"19","isi":1,"OA_type":"gold","quality_controlled":"1","scopus_import":"1","department":[{"_id":"FlSc"}]}]