Abstract
A major difference between the Na,K-ATPase ion pump and other P-type ATPases is its ability to bind cardiotonic steroids such as ouabain. Na,K-ATPase also interacts with many membrane and cytosolic proteins. In addition to their role in Na,K-ATPase regulation, it became apparent that some of the newly identified interactions are capable of organizing the Na,K-ATPase into various signaling complexes. This new function confers a ligand-like effect to cardiotonic steroids on cellular signal transduction. This article reviews these new developments and provides a comparison of Na,K-ATPase-mediated signal transduction with other receptors and ion transporters.
Publication types
-
Research Support, N.I.H., Extramural
-
Review
MeSH terms
-
Animals
-
Calcium / physiology
-
Cardiac Glycosides / metabolism*
-
Caveolae / metabolism
-
Cell Membrane / metabolism
-
Cytoplasm / metabolism
-
Humans
-
Ion Transport
-
Ouabain / metabolism
-
Protein Binding
-
Protein Isoforms / physiology
-
Receptors, Cell Surface / metabolism
-
Receptors, Cell Surface / physiology*
-
Signal Transduction
-
Sodium-Potassium-Exchanging ATPase / metabolism
-
Sodium-Potassium-Exchanging ATPase / physiology*
-
src-Family Kinases / metabolism
-
src-Family Kinases / physiology*
Substances
-
Cardiac Glycosides
-
Protein Isoforms
-
Receptors, Cell Surface
-
Ouabain
-
src-Family Kinases
-
Sodium-Potassium-Exchanging ATPase
-
Calcium