Journal article

Mutations in the Gal83 glycogen-binding domain activate the Snf1/Gal83 kinase pathway by a glycogen-independent mechanism

HA Wiatrowski, BJW van Denderen, CD Berkey, BE Kemp, D Stapleton, M Carlson

Molecular and Cellular Biology | AMER SOC MICROBIOLOGY | Published : 2004

Abstract

The yeast Snf1 kinase and its mammalian ortholog, AMP-activated protein kinase (AMPK), regulate responses to metabolic stress. Previous studies identified a glycogen-binding domain in the AMPK beta1 subunit, and the sequence is conserved in the Snf1 kinase beta subunits Gal83 and Sip2. Here we use genetic analysis to assess the role of this domain in vivo. Alteration of Gal83 at residues that are important for glycogen binding of AMPK beta1 abolished glycogen binding in vitro and caused diverse phenotypes in vivo. Various Snf1/Gal83-dependent processes were upregulated, including glycogen accumulation, expression of RNAs encoding glycogen synthase, haploid invasive growth, the transcriptiona..

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University of Melbourne Researchers