Bypassing AMPK Phosphorylation

作者:Viollet Benoit*; Foretz Marc; Schlattner Uwe
来源:Chemistry & Biology, 2014, 21(5): 567-569.
DOI:10.1016/j.chembiol.2014.05.003

摘要

AMP-activated protein kinase (AMPK) functions as a signaling hub to balance energy supply with demand. Phosphorylation of activation loop Thr172 has been considered as an essential step in AMPK activation. In this issue of Chemistry & Biology, Scott and colleagues show that the small molecule direct AMPK activator, A-769662, bypasses this phosphorylation event and acts synergistically with AMP on naive AMPK.

  • 出版日期2014-5-22