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First published online May 15, 2009
Journal of Experimental Biology 212, 1638-1646 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.028605
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Review Article

NHE3 regulatory complexes

Mark Donowitz*, Sachin Mohan, Cindy Xinjun Zhu, Tian-E Chen, Rong Lin, Boyoung Cha, Nicholas C. Zachos, Rakhilya Murtazina, Rafiquel Sarker and Xuhang Li

Johns Hopkins University School of Medicine, 720 Rutland Avenue Baltimore, MD 21205, USA

* Author for correspondence (e-mail: mdonowit{at}jhmi.edu)

Accepted 12 February 2009

The epithelial brush border Na/H exchanger NHE3 is active under basal conditions and functions as part of neutral NaCl absorption in the intestine and renal proximal tubule, where it accounts for the majority of total Na absorbed. NHE3 is highly regulated. Both stimulation and inhibition occur post-prandially. This digestion related regulation of NHE3 is mimicked by multiple extracellular agonists and intracellular second messengers. The regulation of NHE3 depends on its C-terminal cytoplasmic domain, which acts as a scaffold to bind multiple regulatory proteins and links NHE3 to the cytoskeleton. The cytoskeletal association occurs by both direct binding to ezrin and by indirect binding via ezrin binding to the C-terminus of the multi-PDZ domain containing proteins NHERF1 and NHERF2. This is a review of the domain structure of NHE3 and of the scaffolding function and role in the regulation of NHE3 of the NHE3 C-terminal domain.

Key words: Na/H exchange, protein complexes, signal transduction


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JEB 2009 212: i. [Full Text]  





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