The regulation of AMP-activated protein kinase by phosphorylation.

@article{Stein2000TheRO,
  title={The regulation of AMP-activated protein kinase by phosphorylation.},
  author={Sherman C Stein and Anne Woods and Natasha A Jones and Matthew D. Davison and David Carling},
  journal={The Biochemical journal},
  year={2000},
  volume={345 Pt 3},
  pages={437-43}
}
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