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

AuthorsGarcía-Haro, Luisa ; García-Gimeno, María Adelaida ; Neumann, Dietbert; Beullens, Monique; Bollen, Mathieu; Sanz, Pascual
KeywordsBeta cell function
Glucose regulation
Metabolic regulation
Energy metabolism
Issue Date29-Oct-2012
PublisherFederation of European Biochemical Societies
CitationFEBS Letters 586(23):4241-4247 (2012)
AbstractAMP-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.
Description7 páginas, 5 figuras, material suplementario en versión online.
Publisher version (URL)http://dx.doi.org/10.1016/j.febslet.2012.10.032
Appears in Collections:(IBV) Artículos
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