Shashkova Sviatlana, Wollman Adam J M, Leake Mark C, Hohmann Stefan
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Göteborg, Sweden.
Biological Physical Sciences Institute, University of York, York YO10 5DD, UK.
FEMS Microbiol Lett. 2017 Aug 1;364(14). doi: 10.1093/femsle/fnx133.
A yeast Saccharomyces cerevisiae Snf1 kinase, an analog of mammalian AMPK, regulates glucose derepression of genes required for utilization of alternative carbon sources through the transcriptional repressor Mig1. It has been suggested that the Glc7-Reg1 phosphatase dephosphorylates Mig1. Here we report that Mig1 is dephosphorylated by Glc7-Reg1 in an apparently glucose-dependent mechanism but also by a mechanism independent of glucose and Glc7-Reg1. In addition to serine/threonine phosphatases another process including tyrosine phosphorylation seems crucial for Mig1 regulation. Taken together, Mig1 dephosphorylation appears to be controlled in a complex manner, in line with the importance for rapid and sensitive regulation upon altered glucose concentrations in the growth medium.
酵母酿酒酵母Snf1激酶是哺乳动物AMPK的类似物，它通过转录阻遏物Mig1调节利用替代碳源所需基因的葡萄糖去阻遏作用。有人提出Glc7-Reg1磷酸酶使Mig1去磷酸化。在此我们报告，Mig1通过一种明显依赖葡萄糖的机制被Glc7-Reg1去磷酸化，但也通过一种独立于葡萄糖和Glc7-Reg1的机制。除了丝氨酸/苏氨酸磷酸酶外，另一个包括酪氨酸磷酸化的过程似乎对Mig1的调节至关重要。综上所述，Mig1的去磷酸化似乎以一种复杂的方式受到控制，这与在生长培养基中葡萄糖浓度改变时进行快速和敏感调节的重要性相一致。
