Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.

Article Details

Citation

Pang T, Su X, Wakabayashi S, Shigekawa M

Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.

J Biol Chem. 2001 May 18;276(20):17367-72. Epub 2001 Feb 28.

PubMed ID
11350981 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Sodium/hydrogen exchanger 1P19634Details
Calcineurin B homologous protein 1Q99653Details