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

Hanne Poulsen; Jens Preben Morth; Jan Egebjerg Jensen; Poul Nissen

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

Hanne Poulsen, Jens Preben Morth, Jan Egebjerg Jensen, Poul Nissen

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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.

Original language	Danish
Journal	FEBS Letters
Volume	584
Issue	12
Pages (from-to)	2589-2595
ISSN	0014-5793
Publication status	Published - 2010

Cite this

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title = "Phosphorylation of the Na+,K+-ATPase and the H+,K+-ATPase",

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.",

author = "Hanne Poulsen and Morth, {Jens Preben} and Jensen, {Jan Egebjerg} and Poul Nissen",

year = "2010",

language = "Dansk",

volume = "584",

pages = "2589--2595",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd.",

number = "12",

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TY - JOUR

T1 - Phosphorylation of the Na+,K+-ATPase and the H+,K+-ATPase

AU - Poulsen, Hanne

AU - Morth, Jens Preben

AU - Jensen, Jan Egebjerg

AU - Nissen, Poul

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

M3 - Tidsskriftartikel

SN - 0014-5793

VL - 584

SP - 2589

EP - 2595

JO - FEBS Letters

JF - FEBS Letters

IS - 12

ER -