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XB-ART-9048
J Biol Chem 2001 May 18;27620:17367-72. doi: 10.1074/jbc.M100296200.
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Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.

Pang T , Su X , Wakabayashi S , Shigekawa M .


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The Na+/H+ exchangers (NHEs) comprise a family of transporters that catalyze cell functions such as regulation of the pH and volume of a cell and epithelial absorption of Na+ and bicarbonate. Ubiquitous calcineurin B homologous protein (CHP or p22) is co-localized and co-immunoprecipitated with expressed NHE1, NHE2, or NHE3 independently of its myristoylation and Ca2+ binding, and its binding site was identified as the juxtamembrane region within the carboxyl-terminal cytoplasmic domain of exchangers. CHP binding-defective mutations of NHE1-3 or CHP depletion by injection of the competitive CHP-binding region of NHE1 into Xenopus oocytes resulted in a dramatic reduction (>90%) in the Na+/H+ exchange activity. The data suggest that CHP serves as an essential cofactor, which supports the physiological activity of NHE family members.

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Species referenced: Xenopus laevis
Genes referenced: chp1 ppp3ca rhov slc9a1 slc9a3 slc9a4