NHE3 regulatory complexes

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

Research output: Contribution to journalReview articlepeer-review

80 Scopus citations


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 viaezrin 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.

Original languageEnglish (US)
Pages (from-to)1638-1646
Number of pages9
JournalJournal of Experimental Biology
Issue number11
StatePublished - Jun 1 2009


  • Na/H exchange
  • Protein complexes
  • Signal transduction

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Physiology
  • Aquatic Science
  • Animal Science and Zoology
  • Molecular Biology
  • Insect Science


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