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

doi:10.1016/j.febslet.2012.10.032

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 journal › Article › Academic › peer-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 language	English
Pages (from-to)	4241-4247
Journal	Febs Letters
Volume	586
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2012.10.032
Publication status	Published - 30 Nov 2012

Keywords

Beta cell function
Glucose regulation
Metabolic regulation
Energy metabolism

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10.1016/j.febslet.2012.10.032

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

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. ",

keywords = "Beta cell function, Glucose regulation, Metabolic regulation, Energy metabolism",

author = "Luisa Garcia-Haro and {Adelaida Garcia-Gimeno}, Maria and Dietbert Neumann and Monique Beullens and Mathieu Bollen and Pascual Sanz",

year = "2012",

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T1 - Glucose-dependent regulation of AMP-activated protein kinase in MIN6 beta cells is not affected by the protein kinase A pathway

AU - Garcia-Haro, Luisa

AU - Adelaida Garcia-Gimeno, Maria

AU - Neumann, Dietbert

AU - Beullens, Monique

AU - Bollen, Mathieu

AU - Sanz, Pascual

PY - 2012/11/30

Y1 - 2012/11/30

N2 - 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.

AB - 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.

KW - Beta cell function

KW - Glucose regulation

KW - Metabolic regulation

KW - Energy metabolism

U2 - 10.1016/j.febslet.2012.10.032

DO - 10.1016/j.febslet.2012.10.032

M3 - Article

C2 - 23116618

SN - 0014-5793

VL - 586

SP - 4241

EP - 4247

JO - Febs Letters

JF - Febs Letters

IS - 23

ER -

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

Abstract

Keywords

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