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J Biol Chem, Vol. 274, Issue 29, 20206-20214, July 16, 1999

p90RSK Is a Serum-stimulated Na+/H+ Exchanger Isoform-1 Kinase
REGULATORY PHOSPHORYLATION OF SERINE 703 OF Na+/H+ EXCHANGER ISOFORM-1

Eiichi Takahashi, Jun-ichi Abe, Byron Gallis, Ruedi AebersoldDagger , Denise J. Spring§, Edwin G. Krebs§parallel , and Bradford C. Berk**

From the Departments of Medicine, Dagger  Molecular Biotechnology, § Pharmacology, and  Biochemistry and the parallel  Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195 and the ** Center for Cardiovascular Research, University of Rochester, Rochester, New York 14642

The Na+/H+ exchanger isoform-1 (NHE-1) is the key member of a family of exchangers that regulates intracellular pH and cell volume. Activation of NHE-1 by growth factors is rapid, correlates with increased NHE-1 phosphorylation and cell alkalinization, and plays a role in cell cycle progression. By two-dimensional tryptic peptide mapping of immunoprecipitated NHE-1, we identify serine 703 as the major serum-stimulated amino acid. Mutation of serine 703 to alanine had no effect on acid-stimulated Na+/H+ exchange but completely prevented the growth factor-mediated increase in NHE-1 affinity for H+. In addition, we show that p90 ribosomal S6 kinase (p90RSK) is a key NHE-1 kinase since p90RSK phosphorylates NHE-1 serine 703 stoichiometrically in vitro, and transfection with kinase-inactive p90RSK inhibits serum-induced phosphorylation of NHE-1 serine 703 in transfected 293 cells. These findings establish p90RSK as a serum-stimulated NHE-1 kinase and a mediator of increased Na+/H+ exchange in vivo.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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