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| Biochem. Biophys. Res. Commun. Feb (1998); 243(3):874-7 | |
| Mapping of ezrin dimerization using yeast two-hybrid screening. | |
| Bhartur SG, Goldenring JR | |
| Department of Medicine, Medical College of Georgia, Augusta, USA. | |
| 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. | |
| [PUBMED: 9501018] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |