{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rahman MM"],"funding":["Canadian Federation of University Women","Canadian Institutes of Health Research"],"pagination":["110646"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12494564"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["301(10)"],"pubmed_abstract":["Ezrin, radixin, and moesin (ERM) proteins regulate assembly of actin-based structures, link membrane-spanning proteins to cortical actin, and are part of cell signaling hubs. The chloride intracellular channel (CLIC) 5A protein is very abundant in radixin-dependent inner ear hair cell stereocilia and in ezrin-dependent kidney glomerular podocyte foot processes and is essential for the structural integrity of these actin-based cellular projections. The functional relationship between ERM proteins and CLIC5A is incompletely understood and whether CLIC5A functions as a chloride channel is controversial. We determined whether CLIC5A is membrane-spanning protein and sought direct CLIC5A binding partners. While CLIC5A localized predominantly to the dorsal plasma membrane domain, we found CLIC5A "],"journal":["The Journal of biological chemistry"],"pubmed_title":["CLIC5A binds to and stabilizes the open and active conformation of ezrin."],"pmcid":["PMC12494564"],"funding_grant_id":["169172"],"pubmed_authors":["Rahman MM","Feisal MR","Tavasoli M","Ballermann BJ","Mak KYL","Li L","Wang Z","Kim JS","Hwang PM"],"additional_accession":[]},"is_claimable":false,"name":"CLIC5A binds to and stabilizes the open and active conformation of ezrin.","description":"Ezrin, radixin, and moesin (ERM) proteins regulate assembly of actin-based structures, link membrane-spanning proteins to cortical actin, and are part of cell signaling hubs. The chloride intracellular channel (CLIC) 5A protein is very abundant in radixin-dependent inner ear hair cell stereocilia and in ezrin-dependent kidney glomerular podocyte foot processes and is essential for the structural integrity of these actin-based cellular projections. The functional relationship between ERM proteins and CLIC5A is incompletely understood and whether CLIC5A functions as a chloride channel is controversial. We determined whether CLIC5A is membrane-spanning protein and sought direct CLIC5A binding partners. While CLIC5A localized predominantly to the dorsal plasma membrane domain, we found CLIC5A ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-04T04:23:29.981Z","creation":"2026-05-04T03:14:26.299Z"},"accession":"S-EPMC12494564","cross_references":{"pubmed":["40885385"],"doi":["10.1016/j.jbc.2025.110646"]}}