Journal
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
Volume 457, Issue 3, Pages 635-644Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00424-008-0470-0
Keywords
Na/K-ATPase; Tyrosine kinase; Protein phosphorylation; Receptor; Protein kinase
Categories
Funding
- NIH, National Heart, Lung and Blood Institute [HL-36573, HL-67963]
- NIH, National Institute of General Medical Sciences [GM-78565]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL067963, P01HL036573] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM078565] Funding Source: NIH RePORTER
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The Na/K-ATPase was discovered by Skou in 1957. Since then, the efforts of numerous investigators have led to the following conclusions: (a) This enzyme is indeed the molecular machine for the ATP-dependent and -coupled transport of Na+ and K+ across the plasma membrane of a living cell in which such a process (sodium pump) is detected. (b) The Na/K-ATPase is also an important signal transducer that not only interacts and regulates protein kinases, but also functions as a scaffold, capable of bringing the affector and effectors together to form functional signalosomes. This minireview discusses the interaction between the Na/K-ATPase and Src to illustrate how a P-type ATPase can act as a receptor, converting a ligand-binding signal to the activation of protein kinase cascades and the generation of second messengers.
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