AMP-activated protein kinase in skeletal muscle: From structure and localization to its role as a master regulator of cellular metabolism |
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Authors: | C A Witczak C G Sharoff L J Goodyear |
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Institution: | (1) Metabolism Section, Joslin Diabetes Center, Research Division, 1 Joslin Pl, Boston, MA 02215, USA;(2) Department of Kinesiology, University of Massachusetts-Amherst, 30 Eastman Ln, Amherst, MA 01003, USA |
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Abstract: | 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.
Received 04 May 2008; received after revision 14 June 2008; accepted 14 July 2008 |
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Keywords: | " target="_blank"> Ca2+/calmodulin-dependent protein kinase kinase carbohydrate glucose lipid LKB1 protein phosphatase transforming growth factor-β -activated kinase 1 |
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