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J. Biol. Chem., Vol. 280, Issue 14, 13584-13592, April 8, 2005

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PALS1 Specifies the Localization of Ezrin to the Apical Membrane of Gastric Parietal Cells^*

Xinwang Cao¶, Xia Ding¶, Zhen Guo, Rihong Zhou||, Fengsong Wang, Fei Long, Fang Wu, Feng Bi**, Qichen Wang, Daiming Fan**, John G. Forte||, Maikun Teng, and Xuebiao Yao||

From the School of Life Science, University of Science and Technology of China, Hefei 230027, Peoples Republic of China, the Department of Physiology, Morehouse School of Medicine, Atlanta, Georgia 30310, the ^||Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, and the ^**State Key Laboratory of Cancer Biology, Xi'jing Hospital, Fourth Military Medical University, Xi'an, Shanxi 710032, People's Republic of China

The ERM (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 protein kinase A activation cascade to regulated HCl secretion in gastric parietal cells. Here, we show that the 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 study verifies 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 study shows 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 eliminated the apical localization of ezrin. Finally, our study demonstrates 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.

Received for publication, October 20, 2004 , and in revised form, January 13, 2005.

^* This work was supported by Chinese Natural Science Foundation Grants 39925018, 30070349, and 30270654; Chinese Academy of Science Grant KSCX2-2-01; Chinese 973 Project 2002CB713700; and National Institutes of Health Grant DK-56292 (to X. Y.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Both authors contributed equally to this work.

A Georgia Cancer Coalition Distinguished Cancer Research Scholar. To whom correspondence should be addressed: School of Life Science, University of Science and Technology of China, Hefei 230027, People's Republic of China. E-mail: yaoxb{at}ustc.edu.cn

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