Mapping of ezrin dimerization using yeast two-hybrid screening.

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.
Mesh Terms:
Animals, Cytoskeletal Proteins, DNA-Binding Proteins, Dimerization, Gene Transfer Techniques, Histidine, Humans, Parietal Cells, Gastric, Phosphoproteins, Rabbits, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Transcription Factors, beta-Galactosidase
Biochem. Biophys. Res. Commun.
Date: Feb. 24, 1998
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