{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Owen LM"],"funding":["HHS | National Institutes of Health","NHGRI NIH HHS","NIGMS NIH HHS","National Science Foundation"],"pagination":["e2109329119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8915792"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(10)"],"pubmed_abstract":["SignificanceTalin is a mechanosensitive adaptor protein that links integrins to the actin cytoskeleton at cell-extracellular matrix adhesions. Although the C-terminal actin-binding domain ABS3 of talin is required for function, it binds weakly to actin in solution. We show that ABS3 binds actin strongly only when subjected to mechanical forces comparable to those generated by the cytoskeleton. Moreover, the interaction between ABS3 and actin depends strongly on the direction of force in a manner predicted to organize actin to facilitate adhesion growth and efficient cytoskeletal force generation. These characteristics can explain how force sensing by talin helps to nucleate adhesions precisely when and where they are required to transmit force between the cytoskeleton and the extracellular matrix."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["The C-terminal actin-binding domain of talin forms an asymmetric catch bond with F-actin."],"pmcid":["PMC8915792"],"funding_grant_id":["R35GM131747","T32HG000044","R01GM114462","R01 GM114462","T32GM007276","R35 GM131747","T32 GM008294","GRFP","T32 GM007276","R35 GM130332","T32GM08294","R35GM130332","T32 HG000044"],"pubmed_authors":["Bax NA","Owen LM","Weis WI","Dunn AR"],"additional_accession":[]},"is_claimable":false,"name":"The C-terminal actin-binding domain of talin forms an asymmetric catch bond with F-actin.","description":"SignificanceTalin is a mechanosensitive adaptor protein that links integrins to the actin cytoskeleton at cell-extracellular matrix adhesions. Although the C-terminal actin-binding domain ABS3 of talin is required for function, it binds weakly to actin in solution. We show that ABS3 binds actin strongly only when subjected to mechanical forces comparable to those generated by the cytoskeleton. Moreover, the interaction between ABS3 and actin depends strongly on the direction of force in a manner predicted to organize actin to facilitate adhesion growth and efficient cytoskeletal force generation. These characteristics can explain how force sensing by talin helps to nucleate adhesions precisely when and where they are required to transmit force between the cytoskeleton and the extracellular matrix.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-04T14:49:57.068Z","creation":"2025-04-04T14:49:57.068Z"},"accession":"S-EPMC8915792","cross_references":{"pubmed":["35245171"],"doi":["10.1073/pnas.2109329119"]}}