[{"date_created":"2026-04-26T22:01:46Z","publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"_id":"21762","title":"Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape","department":[{"_id":"MaLo"},{"_id":"FlSc"},{"_id":"GradSch"},{"_id":"EM-Fac"}],"article_processing_charge":"No","publication_status":"published","fulldoi":"https://doi.org/10.1126/science.aea6343","pmid":1,"oa_version":"None","language":[{"iso":"eng"}],"project":[{"grant_number":"101034413","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","name":"IST-BRIDGE: International postdoctoral program","call_identifier":"H2020"},{"grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb","name":"A molecular atlas of Actin filament IDentities in the cell motility machinery"}],"year":"2026","type":"journal_article","publisher":"AAAS","acknowledged_ssus":[{"_id":"Bio"},{"_id":"ScienComp"},{"_id":"EM-Fac"},{"_id":"LifeSc"}],"intvolume":"       392","date_updated":"2026-09-03T09:36:24Z","OA_type":"closed access","article_number":"eaea6343","volume":392,"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"}],"issue":"6795","author":[{"first_name":"Benjamin L","full_name":"Springstein, Benjamin L","orcid":"0000-0002-3461-5391","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083","last_name":"Springstein"},{"first_name":"Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","last_name":"Javoor"},{"last_name":"Megrian","first_name":"Daniela","full_name":"Megrian, Daniela"},{"last_name":"Hajdu","first_name":"Roman","id":"ffab949d-133f-11ed-8f02-94de21ace503","full_name":"Hajdu, Roman"},{"first_name":"Dustin M.","full_name":"Hanke, Dustin M.","last_name":"Hanke"},{"last_name":"Zens","id":"45FD126C-F248-11E8-B48F-1D18A9856A87","full_name":"Zens, Bettina","orcid":"0000-0002-9561-1239","first_name":"Bettina"},{"first_name":"Gregor L.","full_name":"Weiss, Gregor L.","last_name":"Weiss"},{"last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian Km","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian Km"},{"first_name":"Martin","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose"}],"status":"public","month":"04","quality_controlled":"1","related_material":{"record":[{"id":"22744","status":"public","relation":"dissertation_contains"}]},"publication":"Science","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1126/science.aea6343","article_type":"original","day":"16","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.).","date_published":"2026-04-16T00:00:00Z","external_id":{"pmid":["41990175"]},"corr_author":"1","scopus_import":"1","ec_funded":1,"citation":{"chicago":"Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu, Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>. AAAS, 2026. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>.","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>.","ista":"Springstein BL, Javoor M, Megrian D, Hajdu R, Hanke DM, Zens B, Weiss GL, Schur FK, Loose M. 2026. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. Science. 392(6795), eaea6343.","short":"B.L. Springstein, M. Javoor, D. Megrian, R. Hajdu, D.M. Hanke, B. Zens, G.L. Weiss, F.K. Schur, M. Loose, Science 392 (2026).","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>","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."}},{"department":[{"_id":"GradSch"},{"_id":"FlSc"},{"_id":"MiSi"}],"degree_awarded":"PhD","title":"Large-scale imaging of cellular actin networks at single filament resolution using montage cryo-electron tomography","_id":"22744","publication_identifier":{"isbn":["978-3-99078-090-9 "],"issn":["2663-337X"]},"date_created":"2026-08-21T09:11:04Z","oa_version":"None","OA_embargo":"12","fulldoi":"https://doi.org/10.15479/AT-ISTA-22744","publication_status":"published","OA_place":"publisher","article_processing_charge":"No","doi_confirm":"1","publisher":"Institute of Science and Technology Austria ","type":"dissertation","project":[{"grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb","name":"A molecular atlas of Actin filament IDentities in the cell motility machinery"},{"name":"Pushing from within: Control of cell shape, integrity and motility by cytoskeletal pushing forces","_id":"bd91e723-d553-11ed-ba76-fe7eeb2185fd","grant_number":"101071793"}],"year":"2026","language":[{"iso":"eng"}],"page":"121","date_updated":"2026-09-03T09:36:24Z","file":[{"checksum":"f9c2847df9f1ac5a3d60c06b3b81a450","content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","file_id":"22767","creator":"mjavoor","file_name":"2026_Javoor_Manjunath_Thesis.docx","access_level":"closed","relation":"source_file","date_updated":"2026-08-27T12:48:42Z","date_created":"2026-08-26T12:02:47Z","file_size":27430796},{"file_name":"2026_Javoor_Manjunath_Thesis.pdf","access_level":"closed","date_updated":"2026-08-26T12:02:46Z","relation":"main_file","embargo_to":"open_access","creator":"mjavoor","content_type":"application/pdf","checksum":"8e9b4c0fcafbccf5c3796eacc9134a08","file_id":"22768","file_size":19489230,"date_created":"2026-08-26T12:02:46Z","embargo":"2027-08-21"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"EM-Fac"},{"_id":"ScienComp"},{"_id":"LifeSc"}],"related_material":{"record":[{"id":"12334","status":"public","relation":"part_of_dissertation"},{"id":"21762","status":"public","relation":"part_of_dissertation"},{"id":"19795","status":"public","relation":"part_of_dissertation"},{"id":"12421","status":"public","relation":"part_of_dissertation"}]},"status":"public","month":"08","ddc":["570"],"author":[{"last_name":"Javoor","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","first_name":"Manjunath"}],"day":"21","supervisor":[{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","full_name":"Schur, Florian KM","orcid":"0000-0003-4790-8078","first_name":"Florian KM","last_name":"Schur"},{"id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","first_name":"Michael K","last_name":"Sixt"}],"keyword":["Actin cytoskeleton","Cell migration","cryo-electron tomography"],"alternative_title":["ISTA Thesis"],"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","doi":"10.15479/AT-ISTA-22744","corr_author":"1","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)"},"date_published":"2026-08-21T00:00:00Z","file_date_updated":"2026-08-27T12:48:42Z","has_accepted_license":"1","acknowledgement":"This work was supported by the ERC StG grant ActinID (PRA01221F1049A) awarded to Florian\r\nSchur, the ERC-SyG grant Pushing from within (P01071793) awarded to Michael Sixt, and by ISTA.\r\nI would like to thank the Scientific Service Units at ISTA for their essential support throughout\r\nthis work. In particular, I am grateful to the Electron Microscopy Facility, Imaging and Optics\r\nFacility, Zebrafish Facility, Scientific Computing Facility, and Lab Support Facility for their services,\r\nand technical support, all of which were important for the successful completion of this project.","citation":{"ista":"Javoor M. 2026. Large-scale imaging of cellular actin networks at single filament resolution using montage cryo-electron tomography. Institute of Science and Technology Austria .","apa":"Javoor, M. (2026). <i>Large-scale imaging of cellular actin networks at single filament resolution using montage cryo-electron tomography</i>. Institute of Science and Technology Austria . <a href=\"https://doi.org/10.15479/AT-ISTA-22744\">https://doi.org/10.15479/AT-ISTA-22744</a>","short":"M. Javoor, Large-Scale Imaging of Cellular Actin Networks at Single Filament Resolution Using Montage Cryo-Electron Tomography, Institute of Science and Technology Austria , 2026.","mla":"Javoor, Manjunath. <i>Large-Scale Imaging of Cellular Actin Networks at Single Filament Resolution Using Montage Cryo-Electron Tomography</i>. Institute of Science and Technology Austria , 2026, doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22744\">10.15479/AT-ISTA-22744</a>.","chicago":"Javoor, Manjunath. “Large-Scale Imaging of Cellular Actin Networks at Single Filament Resolution Using Montage Cryo-Electron Tomography.” Institute of Science and Technology Austria , 2026. <a href=\"https://doi.org/10.15479/AT-ISTA-22744\">https://doi.org/10.15479/AT-ISTA-22744</a>.","ieee":"M. Javoor, “Large-scale imaging of cellular actin networks at single filament resolution using montage cryo-electron tomography,” Institute of Science and Technology Austria , 2026.","ama":"Javoor M. Large-scale imaging of cellular actin networks at single filament resolution using montage cryo-electron tomography. 2026. doi:<a href=\"https://doi.org/10.15479/AT-ISTA-22744\">10.15479/AT-ISTA-22744</a>"}},{"publication_status":"published","OA_place":"publisher","oa_version":"Published Version","fulldoi":"https://doi.org/10.1016/j.bpr.2025.100211","DOAJ_listed":"1","oa":1,"article_processing_charge":"Yes","title":"Image-based 3D active sample stabilization on the nanometer scale for optical microscopy","_id":"19795","department":[{"_id":"JoDa"},{"_id":"GradSch"},{"_id":"FlSc"},{"_id":"EM-Fac"}],"date_created":"2025-06-08T22:01:22Z","publication_identifier":{"eissn":["2667-0747"]},"volume":5,"article_number":"100211","abstract":[{"lang":"eng","text":"Super-resolution microscopy often entails long acquisition times of minutes to hours. Since drifts during the acquisition adversely affect data quality, active sample stabilization is commonly used for some of these techniques to reach their full potential. Although drifts in the lateral plane can often be corrected after acquisition, this is not always possible or may come with drawbacks. Therefore, it is appealing to stabilize sample position in three dimensions (3D) during acquisition. Various schemes for active sample stabilization have been demonstrated previously, with some reaching sub-nanometer stability in 3D. Here, we present a scheme for active drift correction that delivers the nanometer-scale 3D stability demanded by state-of-the-art super-resolution techniques and is straightforward to implement compared to previous schemes capable of reaching this level of stabilization precision. Using a refined algorithm that can handle various types of reference structure, without sparse signal peaks being mandatory, we stabilized sample position to ∼1 nm in 3D using objective lenses both with high and low numerical aperture. Our implementation requires only the addition of a simple widefield imaging path and we provide an open-source control software with graphical user interface to facilitate easy adoption of the module. Finally, we demonstrate how this has the potential to enhance data collection for diffraction-limited and super-resolution imaging techniques using single-molecule localization microscopy and cryo-confocal imaging as showcases."}],"file":[{"date_updated":"2025-06-10T07:24:46Z","relation":"main_file","access_level":"open_access","file_name":"2025_BiophysicalReports_Vorlaufer.pdf","file_id":"19802","content_type":"application/pdf","checksum":"4018c833f25a3ad3b57e3577fed70334","creator":"dernst","date_created":"2025-06-10T07:24:46Z","file_size":7238179,"success":1}],"acknowledged_ssus":[{"_id":"M-Shop"},{"_id":"EM-Fac"},{"_id":"LifeSc"}],"OA_type":"gold","date_updated":"2026-09-03T09:36:24Z","intvolume":"         5","year":"2025","project":[{"grant_number":"CZI01","name":"CryoMinflux-guided in-situ molecular census and structure determination","_id":"62909c6f-2b32-11ec-9570-e1476aab5308"},{"_id":"6285a163-2b32-11ec-9570-8e204ca2dba5","name":"Studying Organelle Structure and Function at Nanoscale Resolution with Expansion Microscopy","grant_number":"26137"},{"_id":"2564DBCA-B435-11E9-9278-68D0E5697425","name":"International IST Doctoral Program","call_identifier":"H2020","grant_number":"665385"},{"call_identifier":"FWF","name":"Molecular Drug Targets","_id":"26AA4EF2-B435-11E9-9278-68D0E5697425","grant_number":"W1232-B24"},{"name":"High-speed 3D-nanoscopy to study the role of adhesion during 3D cell migration","_id":"2668BFA0-B435-11E9-9278-68D0E5697425","grant_number":"LT00057"}],"language":[{"iso":"eng"}],"publisher":"Elsevier","type":"journal_article","day":"11","article_type":"original","doi":"10.1016/j.bpr.2025.100211","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","related_material":{"record":[{"id":"20206","relation":"dissertation_contains","status":"public"},{"status":"public","relation":"dissertation_contains","id":"22744"}]},"publication":"Biophysical Reports","issue":"2","ddc":["570"],"month":"06","status":"public","author":[{"last_name":"Vorlaufer","first_name":"Jakob","orcid":"0009-0000-7590-3501","full_name":"Vorlaufer, Jakob","id":"937696FA-C996-11E9-8C7C-CF13E6697425"},{"id":"e64d39c7-72ef-11ef-b75a-ee3046860d1b","full_name":"Semenov, Nikolai","first_name":"Nikolai","last_name":"Semenov"},{"last_name":"Kreuzinger","id":"382077BA-F248-11E8-B48F-1D18A9856A87","full_name":"Kreuzinger, Caroline","first_name":"Caroline"},{"last_name":"Javoor","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","first_name":"Manjunath"},{"id":"45FD126C-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-9561-1239","full_name":"Zens, Bettina","first_name":"Bettina","last_name":"Zens"},{"last_name":"Agudelo Duenas","id":"40E7F008-F248-11E8-B48F-1D18A9856A87","full_name":"Agudelo Duenas, Nathalie","first_name":"Nathalie"},{"id":"3A0A06F4-F248-11E8-B48F-1D18A9856A87","full_name":"Tavakoli, Mojtaba","orcid":"0000-0002-7667-6854","first_name":"Mojtaba","last_name":"Tavakoli"},{"first_name":"Marek","id":"EE8452B8-C26A-11E9-B157-E80CE6697425","full_name":"Suplata, Marek","last_name":"Suplata"},{"last_name":"Jahr","full_name":"Jahr, Wiebke","orcid":"0000-0003-0201-2315","id":"425C1CE8-F248-11E8-B48F-1D18A9856A87","first_name":"Wiebke"},{"last_name":"Lyudchik","first_name":"Julia","full_name":"Lyudchik, Julia","id":"46E28B80-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Wartak","first_name":"Andreas","id":"60aaa06c-3de5-11eb-9e53-baa88e955dcb","full_name":"Wartak, Andreas"},{"first_name":"Florian Km","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian Km","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur"},{"first_name":"Johann G","full_name":"Danzl, Johann G","orcid":"0000-0001-8559-3973","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87","last_name":"Danzl"}],"citation":{"ama":"Vorlaufer J, Semenov N, Kreuzinger C, et al. Image-based 3D active sample stabilization on the nanometer scale for optical microscopy. <i>Biophysical Reports</i>. 2025;5(2). doi:<a href=\"https://doi.org/10.1016/j.bpr.2025.100211\">10.1016/j.bpr.2025.100211</a>","ieee":"J. Vorlaufer <i>et al.</i>, “Image-based 3D active sample stabilization on the nanometer scale for optical microscopy,” <i>Biophysical Reports</i>, vol. 5, no. 2. Elsevier, 2025.","chicago":"Vorlaufer, Jakob, Nikolai Semenov, Caroline Kreuzinger, Manjunath Javoor, Bettina Zens, Nathalie Agudelo Duenas, Mojtaba Tavakoli, et al. “Image-Based 3D Active Sample Stabilization on the Nanometer Scale for Optical Microscopy.” <i>Biophysical Reports</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.bpr.2025.100211\">https://doi.org/10.1016/j.bpr.2025.100211</a>.","apa":"Vorlaufer, J., Semenov, N., Kreuzinger, C., Javoor, M., Zens, B., Agudelo Duenas, N., … Danzl, J. G. (2025). Image-based 3D active sample stabilization on the nanometer scale for optical microscopy. <i>Biophysical Reports</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.bpr.2025.100211\">https://doi.org/10.1016/j.bpr.2025.100211</a>","short":"J. Vorlaufer, N. Semenov, C. Kreuzinger, M. Javoor, B. Zens, N. Agudelo Duenas, M. Tavakoli, M. Suplata, W. Jahr, J. Lyudchik, A. Wartak, F.K. Schur, J.G. Danzl, Biophysical Reports 5 (2025).","ista":"Vorlaufer J, Semenov N, Kreuzinger C, Javoor M, Zens B, Agudelo Duenas N, Tavakoli M, Suplata M, Jahr W, Lyudchik J, Wartak A, Schur FK, Danzl JG. 2025. Image-based 3D active sample stabilization on the nanometer scale for optical microscopy. Biophysical Reports. 5(2), 100211.","mla":"Vorlaufer, Jakob, et al. “Image-Based 3D Active Sample Stabilization on the Nanometer Scale for Optical Microscopy.” <i>Biophysical Reports</i>, vol. 5, no. 2, 100211, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.bpr.2025.100211\">10.1016/j.bpr.2025.100211</a>."},"scopus_import":"1","ec_funded":1,"corr_author":"1","has_accepted_license":"1","acknowledgement":"We acknowledge expert support by ISTA’s scientific service units, including the Miba Machine Shop, the Electron Microscopy Facility, and the Lab Support Facility. This work has been made possible in part by CZI grant DAF2021-234754 and grant DOI: https://doi.org/10.37921/812628ebpcwg from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community Foundation (funder DOI: https://doi.org/10.13039/100014989) (F.K.M.S. and J.G.D.). We further gratefully acknowledge funding by the following sources: Austrian Science Fund (FWF) grant DK W1232 (M.R.T. and J.G.D.); Austrian Academy of Sciences DOC fellowship 26137 (M.R.T.); Marie Skłodowska-Curie Actions Fellowship GA no. 665385 under the EU Horizon 2020 program (J.L.); ISTA postdoctoral fellowship IST fellow (A.W.); and Human Frontier Science Program postdoctoral fellowship LT000557/2018 (W.J.).","file_date_updated":"2025-06-10T07:24:46Z","date_published":"2025-06-11T00:00:00Z","tmp":{"image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"}},{"type":"journal_article","publisher":"Portland Press","language":[{"iso":"eng"}],"year":"2023","project":[{"grant_number":"P33367","name":"Structure and isoform diversity of the Arp2/3 complex","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A"}],"intvolume":"        51","date_updated":"2026-09-03T09:36:24Z","file":[{"access_level":"open_access","file_name":"2023_BioChemicalSocietyTransactions_Faessler.pdf","date_updated":"2023-03-16T07:58:16Z","relation":"main_file","creator":"dernst","content_type":"application/pdf","checksum":"4e7069845e3dad22bb44fb71ec624c60","file_id":"12728","file_size":10045006,"date_created":"2023-03-16T07:58:16Z","success":1}],"abstract":[{"text":"The actin cytoskeleton plays a key role in cell migration and cellular morphodynamics in most eukaryotes. The ability of the actin cytoskeleton to assemble and disassemble in a spatiotemporally controlled manner allows it to form higher-order structures, which can generate forces required for a cell to explore and navigate through its environment. It is regulated not only via a complex synergistic and competitive interplay between actin-binding proteins (ABP), but also by filament biochemistry and filament geometry. The lack of structural insights into how geometry and ABPs regulate the actin cytoskeleton limits our understanding of the molecular mechanisms that define actin cytoskeleton remodeling and, in turn, impact emerging cell migration characteristics. With the advent of cryo-electron microscopy (cryo-EM) and advanced computational methods, it is now possible to define these molecular mechanisms involving actin and its interactors at both atomic and ultra-structural levels in vitro and in cellulo. In this review, we will provide an overview of the available cryo-EM methods, applicable to further our understanding of the actin cytoskeleton, specifically in the context of cell migration. We will discuss how these methods have been employed to elucidate ABP- and geometry-defined regulatory mechanisms in initiating, maintaining, and disassembling cellular actin networks in migratory protrusions.","lang":"eng"}],"page":"87-99","volume":51,"publication_identifier":{"issn":["0300-5127"],"eissn":["1470-8752"]},"date_created":"2023-01-27T10:08:19Z","department":[{"_id":"FlSc"}],"_id":"12421","title":"Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM","article_processing_charge":"No","oa":1,"pmid":1,"fulldoi":"https://doi.org/10.1042/bst20220221","oa_version":"Published Version","publication_status":"published","date_published":"2023-02-01T00:00:00Z","tmp":{"image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"file_date_updated":"2023-03-16T07:58:16Z","acknowledgement":"We apologize for not being able to mention and cite additional excellent work that would have fit the scope of this review, due to space restraints. We thank Jesse Hansen for comments on the manuscript. We acknowledge support from the Austrian Science Fund (FWF): P33367 and the Institute of Science and Technology Austria.","has_accepted_license":"1","corr_author":"1","external_id":{"isi":["000926043100001"],"pmid":["36695514"]},"scopus_import":"1","citation":{"ama":"Fäßler F, Javoor M, Schur FK. Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. <i>Biochemical Society Transactions</i>. 2023;51(1):87-99. doi:<a href=\"https://doi.org/10.1042/bst20220221\">10.1042/bst20220221</a>","ieee":"F. Fäßler, M. Javoor, and F. K. Schur, “Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM,” <i>Biochemical Society Transactions</i>, vol. 51, no. 1. Portland Press, pp. 87–99, 2023.","mla":"Fäßler, Florian, et al. “Deciphering the Molecular Mechanisms of Actin Cytoskeleton Regulation in Cell Migration Using Cryo-EM.” <i>Biochemical Society Transactions</i>, vol. 51, no. 1, Portland Press, 2023, pp. 87–99, doi:<a href=\"https://doi.org/10.1042/bst20220221\">10.1042/bst20220221</a>.","ista":"Fäßler F, Javoor M, Schur FK. 2023. Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. Biochemical Society Transactions. 51(1), 87–99.","short":"F. Fäßler, M. Javoor, F.K. Schur, Biochemical Society Transactions 51 (2023) 87–99.","apa":"Fäßler, F., Javoor, M., &#38; Schur, F. K. (2023). Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. <i>Biochemical Society Transactions</i>. Portland Press. <a href=\"https://doi.org/10.1042/bst20220221\">https://doi.org/10.1042/bst20220221</a>","chicago":"Fäßler, Florian, Manjunath Javoor, and Florian KM Schur. “Deciphering the Molecular Mechanisms of Actin Cytoskeleton Regulation in Cell Migration Using Cryo-EM.” <i>Biochemical Society Transactions</i>. Portland Press, 2023. <a href=\"https://doi.org/10.1042/bst20220221\">https://doi.org/10.1042/bst20220221</a>."},"author":[{"last_name":"Fäßler","id":"404F5528-F248-11E8-B48F-1D18A9856A87","full_name":"Fäßler, Florian","orcid":"0000-0001-7149-769X","first_name":"Florian"},{"first_name":"Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","last_name":"Javoor"},{"first_name":"Florian KM","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur"}],"month":"02","ddc":["570"],"isi":1,"status":"public","issue":"1","publication":"Biochemical Society Transactions","quality_controlled":"1","related_material":{"record":[{"id":"22744","relation":"dissertation_contains","status":"public"}]},"keyword":["Biochemistry"],"doi":"10.1042/bst20220221","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","day":"01"},{"day":"20","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1126/sciadv.add6495","keyword":["Multidisciplinary"],"quality_controlled":"1","related_material":{"record":[{"relation":"research_data","status":"public","id":"14562"},{"relation":"dissertation_contains","status":"public","id":"22744"},{"id":"18766","status":"public","relation":"dissertation_contains"}]},"publication":"Science Advances","issue":"3","month":"01","isi":1,"status":"public","ddc":["570"],"author":[{"first_name":"Florian","id":"404F5528-F248-11E8-B48F-1D18A9856A87","full_name":"Fäßler, Florian","orcid":"0000-0001-7149-769X","last_name":"Fäßler"},{"last_name":"Javoor","first_name":"Manjunath","orcid":"0000-0003-2311-2112","full_name":"Javoor, Manjunath","id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2"},{"first_name":"Julia","full_name":"Datler, Julia","orcid":"0000-0002-3616-8580","id":"3B12E2E6-F248-11E8-B48F-1D18A9856A87","last_name":"Datler"},{"last_name":"Döring","full_name":"Döring, Hermann","first_name":"Hermann"},{"first_name":"Florian","id":"b9d234ba-9e33-11ed-95b6-cd561df280e6","full_name":"Hofer, Florian","last_name":"Hofer"},{"full_name":"Dimchev, Georgi A","orcid":"0000-0001-8370-6161","id":"38C393BE-F248-11E8-B48F-1D18A9856A87","first_name":"Georgi A","last_name":"Dimchev"},{"last_name":"Hodirnau","full_name":"Hodirnau, Victor-Valentin","orcid":"0000-0003-3904-947X","id":"3661B498-F248-11E8-B48F-1D18A9856A87","first_name":"Victor-Valentin"},{"first_name":"Jan","full_name":"Faix, Jan","last_name":"Faix"},{"full_name":"Rottner, Klemens","first_name":"Klemens","last_name":"Rottner"},{"orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","first_name":"Florian KM","last_name":"Schur"}],"citation":{"mla":"Fäßler, Florian, et al. “ArpC5 Isoforms Regulate Arp2/3 Complex–Dependent Protrusion through Differential Ena/VASP Positioning.” <i>Science Advances</i>, vol. 9, no. 3, add6495, American Association for the Advancement of Science, 2023, doi:<a href=\"https://doi.org/10.1126/sciadv.add6495\">10.1126/sciadv.add6495</a>.","short":"F. Fäßler, M. Javoor, J. Datler, H. Döring, F. Hofer, G.A. Dimchev, V.-V. Hodirnau, J. Faix, K. Rottner, F.K. Schur, Science Advances 9 (2023).","apa":"Fäßler, F., Javoor, M., Datler, J., Döring, H., Hofer, F., Dimchev, G. A., … Schur, F. K. (2023). ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential Ena/VASP positioning. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.add6495\">https://doi.org/10.1126/sciadv.add6495</a>","ista":"Fäßler F, Javoor M, Datler J, Döring H, Hofer F, Dimchev GA, Hodirnau V-V, Faix J, Rottner K, Schur FK. 2023. ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential Ena/VASP positioning. Science Advances. 9(3), add6495.","chicago":"Fäßler, Florian, Manjunath Javoor, Julia Datler, Hermann Döring, Florian Hofer, Georgi A Dimchev, Victor-Valentin Hodirnau, Jan Faix, Klemens Rottner, and Florian KM Schur. “ArpC5 Isoforms Regulate Arp2/3 Complex–Dependent Protrusion through Differential Ena/VASP Positioning.” <i>Science Advances</i>. American Association for the Advancement of Science, 2023. <a href=\"https://doi.org/10.1126/sciadv.add6495\">https://doi.org/10.1126/sciadv.add6495</a>.","ieee":"F. Fäßler <i>et al.</i>, “ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential Ena/VASP positioning,” <i>Science Advances</i>, vol. 9, no. 3. American Association for the Advancement of Science, 2023.","ama":"Fäßler F, Javoor M, Datler J, et al. ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential Ena/VASP positioning. <i>Science Advances</i>. 2023;9(3). doi:<a href=\"https://doi.org/10.1126/sciadv.add6495\">10.1126/sciadv.add6495</a>"},"scopus_import":"1","external_id":{"pmid":["36662867"],"isi":["000964550100015"]},"corr_author":"1","acknowledgement":"We would like to thank K. von Peinen and B. Denker (Helmholtz Centre for Infection Research, Braunschweig, Germany) for experimental and technical assistance, respectively.\r\nThis research was supported by the Scientific Service Units (SSUs) of ISTA through resources provided by Scientific Computing (SciComp), the Life Science Facility (LSF), the Imaging and Optics facility (IOF), and the Electron Microscopy Facility (EMF). We acknowledge support from ISTA and from the Austrian Science Fund (FWF) (P33367) to F.K.M.S., from the Research Training Group GRK2223 and the Helmholtz Society to K.R,. and from the Deutsche Forschungsgemeinschaft (DFG) to J.F. and K.R.","has_accepted_license":"1","file_date_updated":"2023-01-23T07:45:54Z","tmp":{"image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"date_published":"2023-01-20T00:00:00Z","publication_status":"published","oa_version":"Published Version","fulldoi":"https://doi.org/10.1126/sciadv.add6495","pmid":1,"oa":1,"article_processing_charge":"No","title":"ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential Ena/VASP positioning","_id":"12334","department":[{"_id":"FlSc"},{"_id":"EM-Fac"}],"date_created":"2023-01-23T07:26:42Z","publication_identifier":{"issn":["2375-2548"]},"volume":9,"article_number":"add6495","abstract":[{"text":"Regulation of the Arp2/3 complex is required for productive nucleation of branched actin networks. An emerging aspect of regulation is the incorporation of subunit isoforms into the Arp2/3 complex. Specifically, both ArpC5 subunit isoforms, ArpC5 and ArpC5L, have been reported to fine-tune nucleation activity and branch junction stability. We have combined reverse genetics and cellular structural biology to describe how ArpC5 and ArpC5L differentially affect cell migration. Both define the structural stability of ArpC1 in branch junctions and, in turn, by determining protrusion characteristics, affect protein dynamics and actin network ultrastructure. ArpC5 isoforms also affect the positioning of members of the Ena/Vasodilator-stimulated phosphoprotein (VASP) family of actin filament elongators, which mediate ArpC5 isoform–specific effects on the actin assembly level. Our results suggest that ArpC5 and Ena/VASP proteins are part of a signaling pathway enhancing cell migration.</jats:p>","lang":"eng"}],"file":[{"relation":"main_file","date_updated":"2023-01-23T07:45:54Z","access_level":"open_access","file_name":"2023_ScienceAdvances_Faessler.pdf","file_id":"12335","content_type":"application/pdf","checksum":"ce81a6d0b84170e5e8c62f6acfa15d9e","creator":"dernst","date_created":"2023-01-23T07:45:54Z","file_size":1756234,"success":1}],"acknowledged_ssus":[{"_id":"ScienComp"},{"_id":"LifeSc"},{"_id":"Bio"},{"_id":"EM-Fac"}],"date_updated":"2026-10-02T11:21:19Z","intvolume":"         9","project":[{"name":"Structure and isoform diversity of the Arp2/3 complex","_id":"9B954C5C-BA93-11EA-9121-9846C619BF3A","grant_number":"P33367"}],"year":"2023","language":[{"iso":"eng"}],"publisher":"American Association for the Advancement of Science","type":"journal_article"}]