Phosphorylation of the Na+,K+-ATPase in Skeletal Muscle
- 1 April 2003
- journal article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 986 (1) , 449-452
- https://doi.org/10.1111/j.1749-6632.2003.tb07228.x
Abstract
In skeletal muscle, insulin stimulation leads to phosphorylation of Na(+),K(+)-ATPase alpha-subunits on both serine/threonine and tyrosine residues, translocation of Na(+),K(+)-ATPase molecules to the plasma membrane, and increased Na(+),K(+)-ATPase activity. The molecular nature of the tyrosine kinase that phosphorylates Na(+),K(+)-ATPase is not yet identified. In vitro phosphorylation experiments show that the alpha-subunit of Na(+),K(+)-ATPase from skeletal muscle is a substrate for the tyrosine-specific protein kinase c-src. Tyrosine phosphorylation of the alpha-subunits of Na(+),K(+)-ATPase may be an important mechanism for insulin-mediated regulation of Na(+),K(+)-ATPase translocation and activity.Keywords
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