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J Biol Chem, Vol. 274, Issue 29, 20206-20214, July 16, 1999
From the Departments of Medicine, 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.
p90RSK Is a Serum-stimulated
Na+/H+ Exchanger Isoform-1 Kinase
REGULATORY PHOSPHORYLATION OF SERINE 703 OF
Na+/H+ EXCHANGER ISOFORM-1
,
, and Molecular
Biotechnology, § Pharmacology, and ¶ Biochemistry and
the Howard Hughes Medical Institute, University of Washington,
Seattle, Washington 98195 and the ** Center for Cardiovascular
Research, University of Rochester, Rochester, New York 14642
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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