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AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits.
Department of Human Physiology, Institute of Exercise and Sport Sciences, Copenhagen Muscle Research Centre, University of Copenhagen, Copenhagen, Denmark.
Department of Molecular Medicine and Surgery, Section Integrative Physiology, Karolinska Institute, Stockholm, Sweden.
Department of Molecular Medicine and Surgery, Section Integrative Physiology, Karolinska Institute, Stockholm, Sweden.
Department of Human Physiology, Institute of Exercise and Sport Sciences, Copenhagen Muscle Research Centre, University of Copenhagen, Copenhagen, Denmark.
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2006 (English)In: Diabetes, ISSN 0012-1797, E-ISSN 1939-327X, Vol. 55, no 7, 2051-2058 p.Article in journal (Refereed) Published
Abstract [en]

AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates glucose transport mediated by cellular stress or pharmacological agonists such as 5-aminoimidazole-4-carboxamide 1 beta-D-ribonucleoside (AICAR). AS160, a Rab GTPase-activating protein, provides a mechanism linking AMPK signaling to glucose uptake. We show that AICAR increases AMPK, acetyl-CoA carboxylase, and AS160 phosphorylation by insulin-independent mechanisms in isolated skeletal muscle. Recombinant AMPK heterotrimeric complexes (alpha 1 beta 1 gamma l and alpha 2 beta 2 gamma 1) phosphorylate AS160 in a cell-free assay. In mice deficient in AMPK signaling (alpha 2 AMPK knockout [KO], alpha 2 AMPK kinase dead [KD], and gamma 3 AMPK KO), AICAR effects on AS160 phosphorylation were severely blunted, highlighting that complexes containing alpha 2 and gamma 3 are necessary for AICAR-stimulated AS160 phosphorylation in intact skeletal muscle. Contraction-mediated AS160 phosphorylation was also impaired in alpha 2 AMPK KO and KD but not gamma 3 AMPK KO mice. Our results implicate AS160 as a downstream target of AMPK.

Place, publisher, year, edition, pages
2006. Vol. 55, no 7, 2051-2058 p.
Keyword [en]
Adenylate Kinase/deficiency/genetics/*metabolism, Aminoimidazole Carboxamide/analogs & derivatives/pharmacology, Animals, Biological Transport, Catalysis, GTPase-Activating Proteins/*metabolism, Glucose/metabolism, Insulin/pharmacology, Kinetics, Mice, Mice; Knockout, Muscle; Skeletal/*enzymology, Phosphorylation, Protein Subunits/metabolism, Ribonucleotides/pharmacology
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Endocrinology and Diabetes
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URN: urn:nbn:se:uu:diva-22548DOI: 10.2337/db06-0175ISI: 000238764600019PubMedID: 16804075OAI: oai:DiVA.org:uu-22548DiVA: diva2:50321
Available from: 2007-01-19 Created: 2007-01-19 Last updated: 2017-12-07Bibliographically approved

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