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Phosphorylation of the Na+,K+‐ATPase in Skeletal Muscle

Abstract: In skeletal muscle, insulin stimulation leads to phosphorylation of Na+,K+‐ATPase α‐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 α‐subunit of Na+,K+‐ATPase from skeletal muscle is a substrate for the tyrosine‐specific protein kinase c‐src. Tyrosine phosphorylation of the α‐subunits of Na+,K+‐ATPase may be an important mechanism for insulin‐mediated regulation of Na+,K+‐ATPase translocation and activity.