Exercise-induced phospho-proteins in skeletal muscle.
Efforts to identify exercise-induced signaling events in skeletal muscle have been influenced by ground-breaking discoveries in the insulin action field. Initial discoveries demonstrating that exercise enhances insulin sensitivity raised the possibility that contraction directly modulates insulin receptor signaling events. Although the acute effects of exercise on glucose metabolism are clearly insulin-independent, the canonical insulin signaling cascade has been used as a framework by investigators in an attempt to resolve the mechanisms by which muscle contraction governs glucose metabolism. This review focuses on recent advances in our understanding of exercise-induced signaling pathways governing glucose metabolism in skeletal muscle. Particular emphasis will be placed on the characterization of AS160, a novel Akt substrate that plays a role in the regulation of glucose transport.
Deshmukh
A S
AS
Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden.
Hawley
J A
JA
Zierath
J R
JR
D000091162:AMP-Activated Protein Kinase Kinases; D000818:Animals; D015444:Exercise / Q000502:physiology*; D020690:GTPase-Activating Proteins / Q000502:physiology*; D005947:Glucose / Q000378:metabolism; D006801:Humans; D051379:Mice; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000378:metabolism / Q000502:physiology*; D011494:Protein Kinases / Q000502:physiology*; D051057:Proto-Oncogene Proteins c-akt / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology
D020690:GTPase-Activating Proteins; C518767:TBC1D4 protein, human; D011494:Protein Kinases; D051057:Proto-Oncogene Proteins c-akt; D000091162:AMP-Activated Protein Kinase Kinases; D005947:Glucose