The regulation of AMP-activated protein kinase by phosphorylation.

@article{Stein2000TheRO,
  title={The regulation of AMP-activated protein kinase by phosphorylation.},
  author={S. Stein and A. Woods and N. Jones and M. Davison and D. Carling},
  journal={The Biochemical journal},
  year={2000},
  volume={345 Pt 3},
  pages={
          437-43
        }
}
  • S. Stein, A. Woods, +2 authors D. Carling
  • Published 2000
  • Biology, Medicine
  • The Biochemical journal
  • The AMP-activated protein kinase (AMPK) cascade is activated by an increase in the AMP/ATP ratio within the cell. AMPK is regulated allosterically by AMP and by reversible phosphorylation. Threonine-172 within the catalytic subunit (alpha) of AMPK (Thr(172)) was identified as the major site phosphorylated by the AMP-activated protein kinase kinase (AMPKK) in vitro. We have used site-directed mutagenesis to study the role of phosphorylation of Thr(172) on AMPK activity. Mutation of Thr(172) to… CONTINUE READING
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