Journal
FEBS LETTERS
Volume 584, Issue 12, Pages 2589-2595Publisher
WILEY
DOI: 10.1016/j.febslet.2010.04.035
Keywords
Phosphorylation; Na+,K+-ATPase; H+,K+-ATPase; cAMP activated protein kinase; Protein kinase C
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Phosphorylation is a widely used, reversible means of regulating enzymatic activity. Among the important phosphorylation targets are the Na+,K+- and H+,K+-ATPases that pump ions against their chemical gradients to uphold ionic concentration differences over the plasma membrane. The two pumps are very homologous, and at least one of the phosphorylation sites is conserved, namely a cAMP activated protein kinase (PKA) site, which is important for regulating pumping activity, either by changing the cellular distribution of the ATPases or by directly altering the kinetic properties as supported by electrophysiological results presented here. We further review the other proposed pump phosphorylations. (C)2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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