{"doi":"10.1042/bj20021152","title":"Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3zeta","abstract":"<jats:p>Proteins of the 14-3-3 family have been implicated in various physiological processes, and are thought to function as adaptors in various signal transduction pathways. In addition, 14-3-3 proteins may contribute to the reorganization of the actin cytoskeleton by interacting with as yet unidentified actin-binding proteins. Here we show that the 14-3-3ζ isoform interacts with both the actin-depolymerizing factor cofilin and its regulatory kinase, LIM (Lin-11/Isl-1/Mec-3)-domain-containing protein kinase 1 (LIMK1). In both yeast two-hybrid assays and glutathione S-transferase pull-down experiments, these proteins bound efficiently to 14-3-3ζ. Deletion analysis revealed consensus 14-3-3 binding sites on both cofilin and LIMK1. Furthermore, the C-terminal region of 14-3-3ζ inhibited the binding of cofilin to actin in co-sedimentation experiments. Upon co-transfection into COS-7 cells, 14-3-3ζ-specific immunoreactivity was redistributed into characteristic LIMK1-induced actin aggregations. Our data are consistent with 14-3-3-protein-induced changes to the actin cytoskeleton resulting from interactions with cofilin and/or LIMK1.</jats:p>","journal":"Biochemical Journal","year":2003,"id":602726,"datarank":0.6814942173405006,"base_score":4.543294782270004,"endowment":4.543294782270004,"self_citation_contribution":0.6814942173405006,"citation_network_contribution":0.0,"self_endowment_contribution":0.6814942173405006,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":93,"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":1545942,"name":"Heinrich BETZ","orcid":null,"position":1,"is_corresponding":false},{"id":1545943,"name":"Dagmar ROTH","orcid":null,"position":2,"is_corresponding":false},{"id":1545941,"name":"Jörg BIRKENFELD","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3zeta","abstract":"<jats:p>Proteins of the 14-3-3 family have been implicated in various physiological processes, and are thought to function as adaptors in various signal transduction pathways. In addition, 14-3-3 proteins may contribute to the reorganization of the actin cytoskeleton by interacting with as yet unidentified actin-binding proteins. Here we show that the 14-3-3ζ isoform interacts with both the actin-depolymerizing factor cofilin and its regulatory kinase, LIM (Lin-11/Isl-1/Mec-3)-domain-containing protein kinase 1 (LIMK1). In both yeast two-hybrid assays and glutathione S-transferase pull-down experiments, these proteins bound efficiently to 14-3-3ζ. Deletion analysis revealed consensus 14-3-3 binding sites on both cofilin and LIMK1. Furthermore, the C-terminal region of 14-3-3ζ inhibited the binding of cofilin to actin in co-sedimentation experiments. Upon co-transfection into COS-7 cells, 14-3-3ζ-specific immunoreactivity was redistributed into characteristic LIMK1-induced actin aggregations. Our data are consistent with 14-3-3-protein-induced changes to the actin cytoskeleton resulting from interactions with cofilin and/or LIMK1.</jats:p>","is_dataset_classified":null,"base_score":4.543294782270004,"endowment":4.543294782270004,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"12323073","pmcid":"PMC1223062","openalex_id":"https://openalex.org/W1998361398","authors":[],"funders":[],"total_grants":0,"fwci":2.6339,"citation_percentile":0.89998595,"influential_citations":0,"citation_trend":[{"year":2012,"count":7},{"year":2013,"count":5},{"year":2014,"count":8},{"year":2015,"count":2},{"year":2017,"count":7},{"year":2018,"count":3},{"year":2019,"count":1},{"year":2022,"count":1},{"year":2023,"count":1},{"year":2025,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://portlandpress.com/biochemj/article-pdf/369/1/45/709453/bj3690045.pdf","host_type":"journal"},{"url":"https://portlandpress.com/biochemj/article-pdf/369/1/45/709453/bj3690045.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1042/bj20021152","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/12323073","host_type":"repository"},{"url":"http://edoc.mpg.de/10577","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/1223062","host_type":"repository"},{"url":"http://hdl.handle.net/11858/00-001M-0000-002E-1EFA-4","host_type":"repository"}],"fields_of_study":["14-3-3 protein interactions","Microbial Natural Products and Biosynthesis","Ubiquitin and proteasome pathways","14-3-3 Proteins","Actin Depolymerizing Factors","Animals","Base Sequence","COS Cells","Cell Line","DNA Primers","DNA-Binding Proteins","Humans","Immunohistochemistry","Lim Kinases","Microfilament Proteins","Protein Binding","Protein Kinases","Protein Serine-Threonine Kinases","Rats","Two-Hybrid System Techniques","Tyrosine 3-Monooxygenase"],"mesh_terms":["Animals","Base Sequence","Cell Line","DNA-Binding Proteins","Humans","Immunohistochemistry","Microfilament Proteins","Protein Binding","Protein Kinases","Tyrosine 3-Monooxygenase","Protein Serine-Threonine Kinases","DNA Primers","COS Cells","Two-Hybrid System Techniques","14-3-3 Proteins","Actin Depolymerizing Factors","Rats","Lim Kinases"],"keywords":["Cofilin","Actin cytoskeleton","Actin-binding protein","Cell biology","Biology","Actin","Cytoskeleton","Biochemistry","Cell"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life below water"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T20:10:11.609473Z","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":[]}