{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Costache V"],"funding":["NIGMS NIH HHS"],"pagination":["110868"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9210446"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["39(9)"],"pubmed_abstract":["Actin network architecture and dynamics play a central role in cell contractility and tissue morphogenesis. RhoA-driven pulsed contractions are a generic mode of actomyosin contractility, but the mechanisms underlying how their specific architecture emerges and how this architecture supports the contractile function of the network remain unclear. Here we show that, during pulsed contractions, the actin network is assembled by two subpopulations of formins: a functionally inactive population (recruited) and formins actively participating in actin filament elongation (elongating). We then show that elongating formins assemble a polar actin network, with barbed ends pointing out of the pulse. Numerical simulations demonstrate that this geometry favors rapid network contraction. Our results sh"],"journal":["Cell reports"],"pubmed_title":["Rapid assembly of a polar network architecture drives efficient actomyosin contractility."],"pmcid":["PMC9210446"],"funding_grant_id":["R01 GM126256"],"pubmed_authors":["Kim T","Li J","Plancke CN","Suman SK","Begnaud S","Costache V","Reymann AC","Robin FB","Prigent Garcia S"],"additional_accession":[]},"is_claimable":false,"name":"Rapid assembly of a polar network architecture drives efficient actomyosin contractility.","description":"Actin network architecture and dynamics play a central role in cell contractility and tissue morphogenesis. RhoA-driven pulsed contractions are a generic mode of actomyosin contractility, but the mechanisms underlying how their specific architecture emerges and how this architecture supports the contractile function of the network remain unclear. Here we show that, during pulsed contractions, the actin network is assembled by two subpopulations of formins: a functionally inactive population (recruited) and formins actively participating in actin filament elongation (elongating). We then show that elongating formins assemble a polar actin network, with barbed ends pointing out of the pulse. Numerical simulations demonstrate that this geometry favors rapid network contraction. Our results sh","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-26T23:31:32.315Z","creation":"2025-04-06T17:33:51.13Z"},"accession":"S-EPMC9210446","cross_references":{"pubmed":["35649363"],"doi":["10.1016/j.celrep.2022.110868"]}}