Mapping of ezrin dimerization using yeast two-hybrid screening

Abstract

Ezrin, a membrane-cytoskeleton linker protein, is involved in the recruitment of H+/K(+)-ATPase-containing tubulovesicles to the canalicular membrane during acid secretion in the parietal cell. Ezrin exists as monomers and head-to-tail dimers in vivo, and oligomerization is presumably important for activation. In this study, we mapped regions of ezrin-ezrin interaction using the yeast two-hybrid assay. We observed that the N-terminal 283 amino acids are sufficient for interaction with the carboxyl terminal 140 amino acids. The region 333.446 inhibits this association. However, the inclusion of amino acids 283-310 appears to release the inhibition. These specific interactions may play a critical role in the formation of dimerization-competent ezrin molecules.