{"doi":"10.1073/pnas.1110109108","title":"Remodeling of actin filaments by ADF/cofilin proteins","abstract":"<jats:p>Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2011,"id":660020,"datarank":0.8233406589235032,"base_score":5.488937726156687,"endowment":5.488937726156687,"self_citation_contribution":0.8233406589235032,"citation_network_contribution":0.0,"self_endowment_contribution":0.8233406589235032,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":241,"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":591879,"name":"Albina Orlova","orcid":"0000-0002-7836-5785","position":1,"is_corresponding":false},{"id":241042,"name":"Dmitri S. 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We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model.</jats:p>","is_dataset_classified":null,"base_score":5.488937726156687,"endowment":5.488937726156687,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22158895","pmcid":null,"openalex_id":"https://openalex.org/W2008061143","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM077190","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM081303","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM077190","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM081303","title":null}],"total_grants":4,"fwci":8.8797,"citation_percentile":0.9859077,"influential_citations":0,"citation_trend":[{"year":2012,"count":15},{"year":2013,"count":17},{"year":2014,"count":16},{"year":2015,"count":24},{"year":2016,"count":19},{"year":2017,"count":16},{"year":2018,"count":23},{"year":2019,"count":19},{"year":2020,"count":15},{"year":2021,"count":10},{"year":2022,"count":11},{"year":2023,"count":14},{"year":2024,"count":19},{"year":2025,"count":15},{"year":2026,"count":8}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://pnas.org/doi/pdf/10.1073/pnas.1110109108","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.1110109108","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22158895","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3251117","host_type":"repository"},{"url":"http://juser.fz-juelich.de/search?p=id:%22PreJuSER-19044%22","host_type":"repository"}],"fields_of_study":["Force Microscopy Techniques and Applications","Cellular Mechanics and Interactions","Cardiomyopathy and Myosin Studies","Actin Depolymerizing Factors","Actins","Cofilin 2","Cryoelectron Microscopy","Cytoskeleton","Gene Library","Humans","Microscopy, Electron","Models, Molecular","Molecular Conformation","Muscle, Skeletal","Polymers","Protein Conformation","Protein Structure, Secondary"],"mesh_terms":["Actins","Cytoskeleton","Humans","Microscopy, Electron","Models, Molecular","Molecular Conformation","Polymers","Protein Conformation","Gene Library","Protein Structure, Secondary","Muscle, Skeletal","Cryoelectron Microscopy","Actin Depolymerizing Factors","Cofilin 2"],"keywords":["Cofilin","Actin remodeling","Actin","Actin-binding protein","Cell biology","Protein filament","MDia1","Actin remodeling of neurons","Biology","Biophysics","Actin cytoskeleton","Chemistry","Biochemistry","Cytoskeleton","Cell"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T08:13:22.425112Z","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":[]}