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

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

89 Citationer (Scopus)

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.

Originalsprog	Dansk
Tidsskrift	FEBS Letters
Vol/bind	584
Nummer	12
Sider (fra-til)	2589-2595
ISSN	0014-5793
Status	Udgivet - 2010

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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",

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journal = "FEBS Letters",

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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 -