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

Luisa Garcia-Haro, Maria Adelaida Garcia-Gimeno, Dietbert Neumann, Monique Beullens, Mathieu Bollen, Pascual Sanz*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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 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.
Original languageEnglish
Pages (from-to)4241-4247
JournalFebs Letters
Volume586
Issue number23
DOIs
Publication statusPublished - 30 Nov 2012

Keywords

  • Beta cell function
  • Glucose regulation
  • Metabolic regulation
  • Energy metabolism

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