安普克
蛋白激酶A
细胞生物学
AMP活化蛋白激酶
激酶
化学
生物
作者
Anna Klaus,Sarah Zorman,Alexandre Berthier,Cécile Polge,Sacnicte Ramirez,Sylvie Michelland,Michel Sève,Didier Vertommen,Mark H. Rider,Nicolas Lentze,Daniel Auerbach,Uwe Schlattner
出处
期刊:PLOS ONE
[Public Library of Science]
日期:2013-05-31
卷期号:8 (5): e62497-e62497
被引量:65
标识
DOI:10.1371/journal.pone.0062497
摘要
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.
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