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Physiology 21: 48-60, 2006; doi:10.1152/physiol.00044.2005
1548-9213/06 $8.00
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Physiology, Vol. 21, No. 1, 48-60, February 2006
© 2006 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

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

D. Grahame Hardie1 and Kei Sakamoto2

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.




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