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J. Biol. Chem., Vol. 276, Issue 20, 17367-17372, May 18, 2001
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From the Department of Molecular Physiology, National
Cardiovascular Center Research Institute, Fujishiro-dai 5-7-1, Suita,
Osaka 565-8565, Japan
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.
Calcineurin Homologous Protein as an Essential Cofactor
for Na+/H+ Exchangers*
, and
*
This work was supported by Grants-in-aid for Scientific
Research, 09680642 and 10470013, from the Ministry of Education,
Science, and Culture of Japan, and the Uehara Memorial Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-6-6833-5012;
Fax: 81-6-6872-7485; E-mail: wak@ri.ncvc.go.jp.
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