Evidence against regulation of AMP-activated protein kinase and LKB1/STRAD/MO25 activity by creatine phosphate.

@article{Taylor2006EvidenceAR,
  title={Evidence against regulation of AMP-activated protein kinase and LKB1/STRAD/MO25 activity by creatine phosphate.},
  author={Eric B. Taylor and William J. Ellingson and Jeremy D Lamb and David G. Chesser and Cori L Compton and William W. Winder},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2006},
  volume={290 4},
  pages={
          E661-9
        }
}
Muscle contraction results in phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an AMPK kinase (AMPKK). LKB1/STRAD/MO25 (LKB1) is the major AMPKK in skeletal muscle; however, the activity of LKB1 is not increased by muscle contraction. This finding suggests that phosphorylation of AMPK by LKB1 is regulated by allosteric mechanisms. Creatine phosphate is depleted during skeletal muscle contraction to replenish ATP. Thus the concentration of creatine phosphate is an… Expand
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