Journal
FEBS LETTERS
Volume 586, Issue 23, Pages 4241-4247Publisher
WILEY
DOI: 10.1016/j.febslet.2012.10.032
Keywords
Beta cell function; Glucose regulation; Metabolic regulation; Energy metabolism
Funding
- Spanish Ministry of Education and Science [SAF2011-27442]
- Generalitat Valenciana [Prometeo 2009/051]
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AMP-activated protein kinase (AMPK) is a sensor of cellular energy status. In pancreatic beta cells, glucose induces the dephosphorylation of Thr172 within the catalytic subunit and the inactivation of the AMPK complex. Here we demonstrate that glucose also activates protein kinase A (PKA), leading to the phosphorylation of AMPK alpha at Ser485 and Ser497. However, these modifications do not impair the phosphorylation of Thr172 by upstream kinases, and phosphorylation of Thr172 does not affect the phosphorylation of AMPK alpha by PKA either. Thus, although phosphorylation of Thr172 and Ser485/Ser497 are inversely correlated in response to glucose, they follow an independent regulation. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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