CLIC5A binds to and stabilizes the open and active conformation of ezrin.

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

SUBMITTER: Rahman MM 

PROVIDER: S-EPMC12494564 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature