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The mammalian AMP‐activated protein kinase complex mediates glucose regulation of gene expression in the yeast Saccharomyces cerevisiae
Author(s) -
Ye Tian,
Bendrioua Loubna,
Carmena David,
García-Salcedo Raúl,
Dahl Peter,
Carling David,
Hohmann Stefan
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.039
Subject(s) - ampk , derepression , protein kinase a , yeast , saccharomyces cerevisiae , amp activated protein kinase , phosphorylation , phosphatase , biochemistry , protein subunit , protein phosphatase 2 , biology , microbiology and biotechnology , snf3 , mutant , chemistry , gene , gene expression , psychological repression
The AMP‐activated protein kinase (AMPK) controls energy homeostasis in eukaryotic cells. Here we expressed hetero‐trimeric mammalian AMPK complexes in a S accharomyces cerevisiae mutant lacking all five genes encoding yeast AMPK/SNF1 components. Certain mammalian complexes complemented the growth defect of the yeast mutant on non‐fermentable carbon sources. Phosphorylation of the AMPK α1 ‐subunit was glucose‐regulated, albeit not by the Glc7‐Reg1/2 phosphatase, which performs this function on yeast AMPK/SNF1. AMPK could take over SNF1 function in glucose derepression. While indirectly acting anti‐diabetic drugs had no effect on AMPK in yeast, compound 991 stimulated α1 ‐subunit phosphorylation. Our results demonstrate a remarkable functional conservation of AMPK and that glucose regulation of AMPK may not be mediated by regulatory features of a specific phosphatase.