Ezrin Controls the Macromolecular Complexes Formed between an Adapter Protein Na+/H+ Exchanger Regulatory Factor and the Cystic Fibrosis Transmembrane Conductance Regulator

• DOI: 10.1074/jbc.m502305200
• Publication Date: 2005-08-30T00:12:41Z
• Authors: Jianquan Li; Zhongping Dai; Deirdre Jana; David J.E. Callaway; Zimei Bu
• Keywords: Adapter (computing)

Na(+)/H(+) exchanger regulatory factor (NHERF) is an adapter protein that responsible for organizing a number of cell receptors and channels. NHERF contains two amino-terminal PDZ (postsynaptic density 95/disk-large/zonula occluden-1) domains bind to the cytoplasmic membrane channels or receptors. The carboxyl terminus interacts with FERM domain (a shared by 4.1, ezrin, radixin, moesin) family actin-binding proteins, ezrin-radixin-moesin. was shown previously be capable enhancing channel activities cystic fibrosis transmembrane conductance regulator (CFTR). Here we show binding ezrin regulates cooperative bring tails CFTR into spatial proximity each other. We find activates second interact (C-CFTR), so as form specific 2:1:1 (C-CFTR)(2).NHERF.ezrin ternary complex. Without binding, tail only strongly first 1:1 C-CFTR.NHERF Immunoprecipitation immunoblotting confirm interactions full-length in vivo. Because concentrated distribution apical regions epithelial cells diverse partners domains, regulation may employed general mechanism assemble cytoskeleton.