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J. Biol. Chem., Vol. 275, Issue 44, 34693-34700, November 3, 2000
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From the Laboratory of Membrane Biology, Neuroscience Center,
Massachusetts General Hospital, Charlestown, Massachusetts 02129
To test the hypothesis that there is cross-talk
between the protein kinase C (PKC) and protein kinase A (PKA) pathways
in the regulation of the Na,K-ATPase, we measured its phosphorylation in mammalian cell cultures. Phosphorylation of the PKC site, Ser-18, appeared to be due to the activation of the
Interaction of Protein Kinase C and
cAMP-dependent Pathways in the Phosphorylation of the
Na,K-ATPase*
isoform of the kinase. In NRK-52E and L6 cells, this phosphorylation was reduced by prior activation of a cAMP-dependent signaling pathway with
forskolin. In principle this would be consistent with direct
interaction between the two phosphorylation sites, but further
investigation suggested a more indirect mechanism. First,
phosphorylation of Ser-938, the PKA site, could not be detected despite
the presence of active PKA. Second, there was a major reduction in the
phosphorylation of unrelated phosphoproteins as a consequence of
elevation of cAMP, suggesting generalized reduction of kinase activity
or activation of phosphatase activity. In NRK-52E and L6,
phosphorylation of the Na,K-ATPase at Ser-18 paralleled this global
change. In C6 cells, in contrast, there was no cAMP effect on
Na,K-ATPase phosphorylation at Ser-18 and no global cAMP effect on
other phosphoproteins. The cross-talk is evidently mediated by events
occurring at the cellular level.
*
The work was supported by American Cancer Association Grant
IRG-173-J (to M. S. F.) and National Institutes of Health Grant RO1NS27653 (to K. J. S.).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.: 617-726-8579;
Fax: 617-726-7526; E-mail: sweadner@helix.mgh.harvard.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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