Glycogen debranching enzyme association with beta-subunit regulates AMP-activated protein kinase activity.

@article{Sakoda2005GlycogenDE,
  title={Glycogen debranching enzyme association with beta-subunit regulates AMP-activated protein kinase activity.},
  author={Hideyuki Sakoda and Midori Fujishiro and Junko Fujio and Nobuhiro Shojima and Takehide Ogihara and Akifumi Kushiyama and Yasushi Fukushima and Motonobu Anai and Hiraku Ono and Masatoshi Kikuchi and Nanao Horike and Amelia Y I Viana and Yasunobu Uchijima and Hiroki Kurihara and Tomoichiro Asano},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2005},
  volume={289 3},
  pages={E474-81}
}
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… CONTINUE READING

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Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism

  • HA Wiatrowski, BJ Van Denderen, CD Berkey, BE Kemp, D Stapleton, M. Carlson
  • Mol Cell Biol
  • 2004

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