Cellular and Molecular Life Sciences

, Volume 65, Issue 23, pp 3737–3755

AMP-activated protein kinase in skeletal muscle: From structure and localization to its role as a master regulator of cellular metabolism



The AMP-activated protein kinase (AMPK) is a metabolite sensing serine/threonine kinase that has been termed the master regulator of cellular energy metabolism due to its numerous roles in the regulation of glucose, lipid, and protein metabolism. In this review, we first summarize the current literature on a number of important aspects of AMPK in skeletal muscle. These include the following: (1) the structural components of the three AMPK subunits (i.e. AMPKα, β, and γ), and their differential localization in response to stimulation in muscle; (2) the biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase (CaMKK), and transforming growth factor-β-activated kinase 1 (TAK1); (3) the pharmacological agents that are currently available for the activation and inhibition of AMPK; (4) the physiological stimuli that activate AMPK in muscle; and (5) the metabolic processes that AMPK regulates in skeletal muscle.


Ca2+/calmodulin-dependent protein kinase kinase carbohydrate glucose lipid LKB1 protein phosphatase transforming growth factor-β-activated kinase 1 


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Copyright information

© Birkhäuser Verlag, Basel 2008

Authors and Affiliations

  • C. A. Witczak
    • 1
  • C. G. Sharoff
    • 2
  • L. J. Goodyear
    • 1
  1. 1.Metabolism Section, Joslin Diabetes Center, Research DivisionBostonUSA
  2. 2.Department of KinesiologyUniversity of Massachusetts-AmherstAmherstUSA

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