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

被引：12

作者：

Garcia-Haro, Luisa ^{[1
,2
]}

Adelaida Garcia-Gimeno, Maria ^{[1
,2
]}

Neumann, Dietbert ^{[3
]}

Beullens, Monique ^{[4
]}

Bollen, Mathieu ^{[4
]}

Sanz, Pascual ^{[1
,2
]}

机构：

[1] CSIC, Inst Biomed Valencia, Valencia 46010, Spain

[2] Ctr Invest Red Enfermecedes Raras CIBERER, Valencia 46010, Spain

[3] Cardiovasc Res Inst Maastricht, Dept Mol Genet, NL-6229 ER Maastricht, Netherlands

[4] Univ Louvain, Dept Cellular & Mol Med, Lab Biosignaling & Therapeut, B-3000 Louvain, Belgium

来源：

FEBS LETTERS | 2012年 / 586卷 / 23期

关键词：

Beta cell function; Glucose regulation; Metabolic regulation; Energy metabolism; INSULIN-SECRETION; PHOSPHORYLATION; ROLES; CAMP; MECHANISMS; ALPHA; PKA;

D O I：

10.1016/j.febslet.2012.10.032

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：4241 / 4247

页数：7

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