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

Authors :
Poulsen, Hanne
Morth, Jens Preben
Jensen, Jan Egebjerg
Nissen, Poul
Source :
Poulsen, H, Morth, J P, Jensen, J E & Nissen, P 2010, ' Phosphorylation of the Na+,K+-ATPase and the H+,K+-ATPase ', F E B S Letters, bind 584, nr. 12, s. 2589-2595 .
Publication Year :
2010

Abstract

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.

Details

Language :
Danish
Database :
OpenAIRE
Journal :
Poulsen, H, Morth, J P, Jensen, J E & Nissen, P 2010, ' Phosphorylation of the Na+,K+-ATPase and the H+,K+-ATPase ', F E B S Letters, bind 584, nr. 12, s. 2589-2595 .
Accession number :
edsair.pure.au.......5db1b0d1084d664308c8afcf42913e75