{"doi":"10.1083/jcb.202409067","title":"Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation","abstract":"Actin is a conserved protein with crucial roles in cell polarity, division, and muscle contraction. Its function is regulated in part by posttranslational modifications, one of which is N-terminal arginylation. What is the structure of arginylated-β-actin (R-β-actin), and how does it regulate F-actin function? Here we report the 3.6 Å structures of ADP-R-β-actin filaments, which are nearly identical to that of non-arginylated F-actin. In vitro assays reveal that the interaction between myosin-II and actin is altered upon actin arginylation, characterized by frequent detachment of R-actin filaments from myosin-II. In vivo, replacement of the only actin gene in Schizosaccharomyces pombe with a synthetic gene encoding R-Sp-actin reduces Arp2/3-based actin patches while thickening formin-induced actin cables. Consistent with defective interactions between myosin-II and R-actin filaments, assembly and constriction of the cytokinetic actomyosin ring are perturbed in R-Sp-actin cells. Thus, despite structural similarity of arginylated and non-arginylated actin filaments, actin arginylation affects F-actin assortment into distinct subcellular structures and its interaction with myosin-II.","journal":"The Journal of Cell Biology","year":2025,"id":548523,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":1,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9518,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2025-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":668970,"name":"Saskia E. Bakker","orcid":"0000-0003-3958-4421","position":1,"is_corresponding":false},{"id":582525,"name":"Andrejus Suchenko","orcid":"0000-0002-4832-1642","position":2,"is_corresponding":false},{"id":1441716,"name":"Isabella M. Kolodny","orcid":"0009-0005-8895-3934","position":3,"is_corresponding":false},{"id":1441717,"name":"Hamdi Hussain","orcid":"0000-0003-3126-4263","position":4,"is_corresponding":false},{"id":582523,"name":"Tomoyuki Hatano","orcid":"0000-0002-9092-3989","position":5,"is_corresponding":false},{"id":1441718,"name":"Karuna Sampath","orcid":"0000-0002-0729-1977","position":6,"is_corresponding":false},{"id":668113,"name":"Krishna Chinthalapudi","orcid":"0000-0003-3669-561X","position":7,"is_corresponding":false},{"id":411445,"name":"Sarah M. Heissler","orcid":"0000-0002-6972-7940","position":8,"is_corresponding":false},{"id":1441719,"name":"Masanori Mishima","orcid":"0000-0002-8908-7485","position":9,"is_corresponding":false},{"id":582526,"name":"Mohan K. Balasubramanian","orcid":"0000-0002-1292-8602","position":10,"is_corresponding":false},{"id":1441715,"name":"Clyde S. Pinto","orcid":"0009-0002-7827-9139","position":0,"is_corresponding":true}],"reference_count":67,"raw_metadata":null,"created_at":"2026-07-19T02:53:58.530220Z","pmid":"41236477","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":[]}