The yeast Mig1 transcriptional repressor is dephosphorylated by glucose-dependent and -independent mechanisms
Introductory text in journal, 2017

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.

Mig1

Dephosphorylation

Phosphatases

Inhibitors

Glucose repression

Author

Sviatlana Shashkova

University of Gothenburg

University of York

Adam J.M. Wollman

University of York

Mark C. Leake

University of York

Stefan Hohmann

Chalmers, Biology and Biological Engineering

FEMS Microbiology Letters

0378-1097 (ISSN)

Vol. 364 14

Subject Categories

Microbiology

DOI

10.1093/femsle/fnx133

More information

Latest update

5/25/2020