Regulation of yeast glycogen phosphorylase by the cyclin-dependent protein kinase Pho85p.
Yeast accumulate glycogen in response to nutrient limitation. The key enzymes of glycogen synthesis and degradation, glycogen synthase, and phosphorylase, are regulated by reversible phosphorylation. Phosphorylation inactivates glycogen synthase but activates phosphorylase. The kinases and phosphatases that control glycogen synthase are well characterized whilst the enzymes modifying phosphorylase are poorly defined. Here, we show that the cyclin-dependent protein kinase, Pho85p, which we have previously found to regulate glycogen synthase also controls the phosphorylation state of phosphorylase.
Wilson
Wayne A
WA
Department of Biochemistry and Molecular Biology, Center for Diabetes Research, Indiana University School of Medicine, Indianapolis, IN 46202, USA. wwilson@iupui.edu
Wang
Zhong
Z
Roach
Peter J
PJ
D018844:Cyclin-Dependent Kinases / Q000737:chemistry*; D015971:Gene Expression Regulation, Enzymologic; D015966:Gene Expression Regulation, Fungal; D006003:Glycogen / Q000378:metabolism*; D024981:Glycogen Phosphorylase / Q000096:biosynthesis* / Q000378:metabolism; D008954:Models, Biological; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D014532:Uridine Diphosphate Glucose
D029701:Saccharomyces cerevisiae Proteins; D006003:Glycogen; D024981:Glycogen Phosphorylase; D018844:Cyclin-Dependent Kinases; C058605:PHO85 protein, S cerevisiae; D014532:Uridine Diphosphate Glucose