RGD Reference Report - Glutathione S-transferases interact with AMP-activated protein kinase: evidence for S-glutathionylation and activation in vitro. - Rat Genome Database

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

Authors: Klaus, A  Zorman, S  Berthier, A  Polge, C  Ramirez, S  Michelland, S  Seve, M  Vertommen, D  Rider, M  Lentze, N  Auerbach, D  Schlattner, U 
Citation: Klaus A, etal., PLoS One. 2013 May 31;8(5):e62497. doi: 10.1371/journal.pone.0062497. Print 2013.
RGD ID: 10401936
Pubmed: PMID:23741294   (View Abstract at PubMed)
PMCID: PMC3669356   (View Article at PubMed Central)
DOI: DOI:10.1371/journal.pone.0062497   (Journal Full-text)

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 beta-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.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Gstm1  (glutathione S-transferase mu 1)
Gstp1  (glutathione S-transferase pi 1)
Prkab2  (protein kinase AMP-activated non-catalytic subunit beta 2)


Additional Information