AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle

D. Grahame Hardie 1 and Kei Sakamoto 2 1 Division of Molecular Physiology and 2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland d.g.hardie{at}dundee.ac.uk Contraction induces marked metabolic changes in muscle, and the AMP-activated protein kinase (AMPK) is a good candidate...

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Veröffentlicht in:	Physiology (Bethesda, Md.) Md.), 2006-02, Vol.21 (1), p.48-60
Hauptverfasser:	Hardie, D. Grahame, Sakamoto, Kei
Format:	Artikel
Sprache:	eng
Schlagworte:	AMP-Activated Protein Kinase Kinases AMP-Activated Protein Kinases Animals Energy Metabolism Glucose - metabolism Glycogen - physiology Humans Mice Mice, Knockout Mice, Transgenic Multienzyme Complexes - genetics Multienzyme Complexes - physiology Muscle Contraction Muscle, Skeletal - enzymology Muscle, Skeletal - physiology Mutation Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - physiology Signal Transduction
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Beschreibung
Zusammenfassung:	D. Grahame Hardie 1 and Kei Sakamoto 2 1 Division of Molecular Physiology and 2 MRC Protein Phosphorylation Unit, University of Dundee, Dundee, Scotland d.g.hardie{at}dundee.ac.uk 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.
ISSN:	1548-9213 1548-9221
DOI:	10.1152/physiol.00044.2005