Glutathione S-transferases interact with AMP-activated protein kinase: evidence for S-glutathionylation and activation in vitro

AMP-activated protein kinase (AMPK) is a cellular and whole body energy sensor with manifold functions in regulating energy homeostasis, cell morphology and proliferation in health and disease. Here we apply multiple, complementary in vitro and in vivo interaction assays to identify several isoforms...

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Published in:	PloS one Vol. 8; no. 5; p. e62497
Main Authors:	Klaus, Anna, Zorman, Sarah, Berthier, Alexandre, Polge, Cécile, Ramirez, Sacnicte, Michelland, Sylvie, Sève, Michel, Vertommen, Didier, Rider, Mark, Lentze, Nicolas, Auerbach, Daniel, Schlattner, Uwe
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 31-05-2013 Public Library of Science (PLoS)
Subjects:	Activation AMP AMP-activated protein kinase AMP-Activated Protein Kinases - genetics AMP-Activated Protein Kinases - metabolism Animals Binding Sites Bioenergetics Biology Cell morphology Complex formation Cytology Energy balance Energy Metabolism - genetics Enzyme Activation Enzymes Gene Expression Glutathione Glutathione - metabolism Glutathione transferase Glutathione Transferase - genetics Glutathione Transferase - metabolism GSTM1 protein Helminth Proteins - genetics Helminth Proteins - metabolism Homeostasis Humans Isoenzymes - genetics Isoenzymes - metabolism Isoforms Kinases Laboratories Life Sciences Liver - chemistry Liver - enzymology Mammals Metabolism Oxidation-Reduction Oxidative Stress Phosphorylation Physiology Protein Binding Protein Structure, Tertiary Protein Subunits - genetics Protein Subunits - metabolism Proteins Rats Recombinant Proteins - genetics Recombinant Proteins - metabolism Rodents Schistosoma japonicum - chemistry Schistosoma japonicum - enzymology Signal Transduction France
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Summary:	AMP-activated protein kinase (AMPK) is a cellular and whole body energy sensor with manifold functions in regulating energy homeostasis, cell morphology and proliferation in health and disease. Here we apply multiple, complementary in vitro and in vivo interaction assays to identify several isoforms of glutathione S-transferase (GST) as direct AMPK binding partners: Pi-family member rat GSTP1 and Mu-family members rat GSTM1, as well as Schistosoma japonicum GST. GST/AMPK interaction is direct and involves the N-terminal domain of the AMPK β-subunit. Complex formation of the mammalian GSTP1 and -M1 with AMPK leads to their enzymatic activation and in turn facilitates glutathionylation and activation of AMPK in vitro. GST-facilitated S-glutathionylation of AMPK may be involved in rapid, full activation of the kinase under mildly oxidative physiological conditions.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Inserm, Lille, France Current address: CRI-Inserm and Université Grenoble Alpes, Institut Albert Bonniot, Grenoble, France Conceived and designed the experiments: US AK CP MS MR DA. Performed the experiments: AK AB SZ CP SR SM DV NL. Analyzed the data: AK AB SZ CP SR SM DV US. Contributed reagents/materials/analysis tools: DA. Wrote the paper: US AK DV MR. Current address: INRA, CRNH Auvergne, Clermont-Ferrand, France Competing Interests: Two of our co-authors have been (N.L.) or are still (D.A.) employed by the small company Dualsystems Biotech AG. They provided methodological expertise, but were not involved in data analysis and interpretation. Their presence as co-authors does not alter our adherence to all the PLOS ONE policies on sharing data and materials.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0062497