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Glutathione S-Transferases Interact with AMP-Activated Protein Kinase: Evidence for S-Glutathionylation and Activation In Vitro.

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Klaus, Anna Zorman, Sarah Berthier, Alexandre Polge, Cécile Ramirez, Sacnicte Vertommen, Didier [UCL] Rider, Mark H. [UCL] Schlattner, Uwe

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.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès libre
Publication date 2013
Language Anglais
Journal information "PLoS One" - Vol. 8, no.5, p. e62497 (2013)
Peer reviewed yes
Publisher Public Library of Science ((United States) [S.l.])
issn 1932-6203
Publication status Publié
Affiliation UCL - SSS/DDUV - Institut de Duve
Links
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Bibliographic reference Klaus, Anna ; Zorman, Sarah ; Berthier, Alexandre ; Polge, Cécile ; Ramirez, Sacnicte ; et. al. Glutathione S-Transferases Interact with AMP-Activated Protein Kinase: Evidence for S-Glutathionylation and Activation In Vitro.. In: PLoS One, Vol. 8, no.5, p. e62497 (2013)
Permanent URL http://hdl.handle.net/2078.1/130072