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Papers In Press, published online ahead of print January 27, 2005
J. Biol. Chem, 10.1074/jbc.M411941200
Submitted on October 20, 2004
Revised on January 13, 2005
Accepted on January 27, 2005

PALS1 specifies the localization of ezrin to the apical membrane of gastric parietal cells

Xinwang Cao, Xia Ding, Zhen Guo, Rihong Zhou, Fengsong Wang, Vannes Fog, Fei Long, Feng Bi, Daimin Fan, John G. Forte, Ben Margolis, Maikun Teng, and Xuebiao Yao

Department of Molecular and Cell Biology, Morehouse School of Medicine, Atlanta, GA 30310

Corresponding Author: xyao{at}msm.edu

The ezrin-radixin-moesin proteins provide a regulated linkage between membrane proteins and the cortical cytoskeleton, and also participate in signal-transduction pathways. Ezrin is localized to the apical membrane of parietal cells and couples the cAMP-dependent protein kinase activation cascade to the regulated HCl secretion in gastric parietal cells. Here we show that integrity of ezrin is essential for parietal cell activation and provide the first evidence that ezrin interacts with PALS1, an evolutionarily conserved PDZ and SH3 domain-containing protein. Our biochemical studies verify that ezrin binds to PALS1 via its N-terminus and is co-localized with PALS1 to the apical membrane of gastric parietal cells. Furthermore, our studies show that PALS1 is essential for the apical localization of ezrin as either suppression of PALS1 protein accumulation or deletion of the PALS1-binding domain of ezrin eliminates the apical localization of ezrin. Finally, our studies demonstrate the essential role of ezrin-PALS1 interaction in the apical membrane remodeling associated with parietal cell secretion. Taken together, these results define a novel molecular mechanism linking ezrin to the conserved apical polarity complexes and their roles in polarized epithelial secretion of gastric parietal cells.


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