Phosphorylation of the Na +,K +-ATPase and the H +,K +-ATPase

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...

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Bibliographic Details
Published in:FEBS letters 2010-06, Vol.584 (12), p.2589-2595
Main Authors: Poulsen, Hanne, Morth, Preben, Egebjerg, Jan, Nissen, Poul
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites
cAMP activated protein kinase
Crystallography, X-Ray
Electrophysiological Phenomena
H +,K +-ATPase
H(+)-K(+)-Exchanging ATPase - chemistry
H(+)-K(+)-Exchanging ATPase - genetics
H(+)-K(+)-Exchanging ATPase - metabolism
Humans
Models, Biological
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Na +,K +-ATPase
Phosphorylation
Protein kinase C
Protein Subunits
Sequence Homology, Amino Acid
Sodium-Potassium-Exchanging ATPase - chemistry
Sodium-Potassium-Exchanging ATPase - genetics
Sodium-Potassium-Exchanging ATPase - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2010.04.035