{"doi":"10.1016/j.cub.2003.11.051","title":"Coordinated Regulation of Actin Filament Turnover by a High-Molecular-Weight Srv2/CAP Complex, Cofilin, Profilin, and Aip1","abstract":null,"journal":"Current Biology","year":2003,"id":679284,"datarank":0.7878410142069946,"base_score":5.25227342804663,"endowment":5.25227342804663,"self_citation_contribution":0.7878410142069946,"citation_network_contribution":0.0,"self_endowment_contribution":0.7878410142069946,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":190,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1774806,"name":"Anya L. Goodman","orcid":null,"position":1,"is_corresponding":false},{"id":336535,"name":"Avital A. Rodal","orcid":"0000-0002-2051-8304","position":2,"is_corresponding":false},{"id":81640,"name":"Ellen Smith","orcid":null,"position":3,"is_corresponding":false},{"id":1774808,"name":"Jamie Kugler","orcid":null,"position":4,"is_corresponding":false},{"id":481126,"name":"John E. Heuser","orcid":"0000-0002-3593-8846","position":5,"is_corresponding":false},{"id":459665,"name":"Bruce L. Goode","orcid":"0000-0002-6443-5893","position":6,"is_corresponding":false},{"id":1774805,"name":"Heath I. Balcer","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Coordinated Regulation of Actin Filament Turnover by a High-Molecular-Weight Srv2/CAP Complex, Cofilin, Profilin, and Aip1","abstract":"<h4>Background</h4>Dynamic remodeling of the actin cytoskeleton requires rapid turnover of actin filaments, which is regulated in part by the actin filament severing/depolymerization factor cofilin/ADF. Two factors that cooperate with cofilin are Srv2/CAP and Aip1. Human CAP enhances cofilin-mediated actin turnover in vitro, but its biophysical properties have not been defined, and there has been no in vivo evidence reported for its role in turnover. Xenopus Aip1 forms a cofilin-dependent cap at filament barbed ends. It has been unclear how these diverse activities are coordinated in vivo.<h4>Results</h4>Purified native yeast Srv2/CAP forms a high molecular weight structure comprised solely of actin and Srv2. The complex is linked to actin filaments via the SH3 domain of Abp1. Srv2 complex catalytically accelerates cofilin-dependent actin turnover by releasing cofilin from ADP-actin monomers and enhances the ability of profilin to stimulate nucleotide exchange on ADP-actin. Yeast Aip1 forms a cofilin-dependent filament barbed end cap, disrupted by the cof1-19 mutant. Genetic analyses show that specific combinations of activities mediated by cofilin, Srv2, Aip1, and capping protein are required in vivo.<h4>Conclusions</h4>We define two genetically and biochemically separable functions for cofilin in actin turnover. One is formation of an Aip1-cofilin cap at filament barbed ends. The other is cofilin-mediated severing/depolymerization of filaments, accelerated indirectly by Srv2 complex. We show that the Srv2 complex is a large multimeric structure and functions as an intermediate in actin monomer processing, converting cofilin bound ADP-actin monomers to profilin bound ATP-actin monomers and recycling cofilin for new rounds of filament depolymerization.","is_dataset_classified":null,"base_score":5.25227342804663,"endowment":5.25227342804663,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"14680631","pmcid":null,"openalex_id":"https://openalex.org/W2094462142","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"GM29647","title":null},{"funder_name":"March of Dimes Foundation","grant_id":"GM63691","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM063691","title":null},{"funder_name":"American Heart Association","grant_id":"","title":null}],"total_grants":4,"fwci":3.2821,"citation_percentile":0.92183227,"influential_citations":0,"citation_trend":[{"year":2012,"count":8},{"year":2013,"count":4},{"year":2014,"count":6},{"year":2015,"count":13},{"year":2016,"count":6},{"year":2017,"count":6},{"year":2018,"count":10},{"year":2019,"count":9},{"year":2020,"count":7},{"year":2021,"count":6},{"year":2022,"count":6},{"year":2023,"count":5},{"year":2024,"count":5},{"year":2025,"count":6},{"year":2026,"count":1}],"oa_status":"bronze","license":"http://www.elsevier.com/open-access/userlicense/1.0/","oa_locations":[{"url":"http://www.cell.com/article/S0960982203009072/pdf","host_type":"journal"},{"url":"http://www.cell.com/article/S0960982203009072/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0960982203009072?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0960982203009072?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.cub.2003.11.051","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/14680631","host_type":"repository"}],"fields_of_study":["Cellular Mechanics and Interactions","Skin and Cellular Biology Research","Cardiomyopathy and Myosin Studies"],"mesh_terms":["Chromatography, Gel","Contractile Proteins","Cytoskeletal Proteins","Electrophoresis, Polyacrylamide Gel","Microfilament Proteins","Actin Cytoskeleton","Microscopy, Electron","Models, Molecular","Saccharomyces cerevisiae","Serine Endopeptidases","Immunoblotting","Gene Transfer Techniques","Cell Cycle Proteins","src Homology Domains","Saccharomyces cerevisiae Proteins","Xenopus Proteins","Adaptor Proteins, Signal Transducing","Profilins","Actin Depolymerizing Factors"],"keywords":["Cofilin","Actin remodeling","Profilin","Cell biology","Biology","Actin-binding protein","Actin","MDia1","Actin cytoskeleton","Biochemistry","Cytoskeleton","Cell"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T12:45:22.794597Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}