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FEBS Lett. 2012 Nov 30;586(23):4241-7. doi: 10.1016/j.febslet.2012.10.032. Epub 2012 Oct 29.

Glucose-dependent regulation of AMP-activated protein kinase in MIN6 beta cells is not affected by the protein kinase A pathway.

Author information

1
Instituto de Biomedicina de Valencia, CSIC and Centro de Investigación en Red de Enfermecedes Raras (CIBERER), Jaime Roig 11, 46010 Valencia, Spain.

Abstract

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 AMPKα 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 AMPKα by PKA either. Thus, although phosphorylation of Thr172 and Ser485/Ser497 are inversely correlated in response to glucose, they follow an independent regulation.

PMID:
23116618
DOI:
10.1016/j.febslet.2012.10.032
[Indexed for MEDLINE]
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