AMPK: a key sensor of fuel and energy status in skeletal muscle.
Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate to explain these effects. Recent work using a muscle-specific knockout of the upstream kinase, LKB1, has confirmed that the LKB1-->AMPK cascade is the signaling pathway responsible for many of these effects.
Hardie
D Grahame
DG
Division of Molecular Physiology, University of Dundee, Dundee, Scotland. d.g.hardie@dundee.ac.uk
Sakamoto
Kei
K
D000091162:AMP-Activated Protein Kinase Kinases; D055372:AMP-Activated Protein Kinases; D000818:Animals; D004734:Energy Metabolism; D005947:Glucose / Q000378:metabolism; D006003:Glycogen / Q000502:physiology; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D008822:Mice, Transgenic; D009097:Multienzyme Complexes / Q000235:genetics / Q000502:physiology*; D009119:Muscle Contraction; D018482:Muscle, Skeletal / Q000201:enzymology* / Q000502:physiology*; D009154:Mutation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000502:physiology*; D015398:Signal Transduction
D009097:Multienzyme Complexes; D006003:Glycogen; D017346:Protein Serine-Threonine Kinases; C109790:STK11 protein, human; C491654:Stk11 protein, mouse; C488755:Stk11 protein, rat; D000091162:AMP-Activated Protein Kinase Kinases; D055372:AMP-Activated Protein Kinases; D005947:Glucose