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Am J Physiol Endocrinol Metab 289: E474-E481, 2005. First published May 10, 2005; doi:10.1152/ajpendo.00003.2005
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Glycogen debranching enzyme association with {beta}-subunit regulates AMP-activated protein kinase activity

Hideyuki Sakoda,1 Midori Fujishiro,1 Junko Fujio,1 Nobuhiro Shojima,1 Takehide Ogihara,2 Akifumi Kushiyama,1 Yasushi Fukushima,1 Motonobu Anai,3 Hiraku Ono,3 Masatoshi Kikuchi,3 Nanao Horike,4 Amelia Y. I. Viana,4 Yasunobu Uchijima,4 Hiroki Kurihara,4 and Tomoichiro Asano4

2Division of Advanced Therapeutics for Metabolic Diseases, Center for Translational and Advanced Animal Research on Human Diseases, Tohoku University Graduate School of Medicine, Sendai; 1Department of Internal Medicine, Graduate School of Medicine; 3Institute for Adult Disease, Asahi Life Foundation; and 4Department of Physiological Chemistry and Metabolism, Graduate School of Medicine, University of Tokyo, Tokyo, Japan

Submitted 4 January 2005 ; accepted in final form 28 April 2005

AMP-activated protein kinase (AMPK) regulates both glycogen and lipid metabolism functioning as an intracellular energy sensor. In this study, we identified a 160-kDa protein in mouse skeletal muscle lysate by using a glutathione-S-transferase (GST)-AMPK fusion protein pull-down assay. Mass spectrometry and a Mascot search revealed this protein to be a glycogen debranching enzyme (GDE). The association between AMPK and GDE was observed not only in the overexpression system but also endogenously. Next, we showed the {beta}1-subunit of AMPK to be responsible for the association with GDE. Furthermore, experiments using deletion mutants of the {beta}1-subunit of AMPK revealed amino acids 68–123 of the {beta}1-subunit to be sufficient for GDE binding. W100G and K128Q, both {beta}1-subunit mutants, are reportedly incapable of binding to glycogen, but both bound GDE, indicating that the association between AMPK and GDE does not involve glycogen. Rather, the AMPK-GDE association is likely to be direct. Overexpression of amino acids 68–123 of the {beta}1-subunit inhibited the association between endogenous AMPK and GDE. Although GDE activity was unaffected, basal phosphorylation and kinase activity of AMPK, as well as phosphorylation of acetyl-CoA carboxylase, were significantly increased. Thus it is likely that the AMPK-GDE association is a novel mechanism regulating AMPK activity and the resultant fatty acid oxidation and glucose uptake.

glutathione-S transferase; pull-down assay; mass spectrometry


Address for reprint requests and other correspondence: Department of Physiological Chemistry and Metabolism, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo Bunkyo-ku, Tokyo, Japan (e-mail: asano-tky{at}umin.ac.jp)




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