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Phosphorylation of the Na + ,K + ‐ATPase and the H + ,K + ‐ATPase
Author(s) -
Poulsen Hanne,
Morth Preben,
Egebjerg Jan,
Nissen Poul
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.035
Subject(s) - phosphorylation , atpase , chemistry , ion pump , enzyme , membrane , protein kinase a , biophysics , ion , biochemistry , biology , organic chemistry
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.