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J. Biol. Chem., Vol. 269, Issue 45, 27907-27913, 11, 1994
TA Hardy, D Huang and PJ Roach
The synthesis of glycogen in Saccharomyces cerevisiae is stimulated by
nutrient limitation and requires both glycogen synthase and the glycogen
branching enzyme. Of the two glycogen synthase genes present in yeast, GSY2
appears to be more important for the accumulation of glycogen upon entry
into stationary phase. In cells grown on glucose, GSY2 mRNA levels
increased approximately 10-fold during the transition from logarithmic to
stationary phase. Growth of cells in glycerol, however, resulted in
constitutive expression of GSY2 mRNA and the corresponding protein, GS-2,
suggestive of glucose repression of GSY2. Mutants defective in the SNF1
gene, which encodes a protein kinase important in glucose repression
mechanisms, are known not to accumulate glycogen. A modest 2-4-fold
decrease in total GS-2 level was observed, and upon entry into stationary
phase, the enzyme was blocked in the inactive, phosphorylated state in snf1
strains. The GS-2 protein is thought to be regulated by covalent
phosphorylation of three COOH- terminal sites (Hardy, T.A., and Roach, P.J.
(1993) J. Biol. Chem. 268, 23799-23805), removal of which results in
constitutively active glycogen synthase that bypasses phosphorylation
controls. Expression of COOH-terminally truncated GS-2 in snf1 cells
restored glycogen accumulation, and so we propose that the SNF1 kinase
controls the phosphorylation state of GS-2. Cyclic AMP pathways also exert
control over glycogen accumulation. In bcy1 cells, which have
constitutively active cyclic AMP-dependent protein kinase, greatly reduced
levels of both GS-2 message and protein were observed. With wild type GSY2
placed under control of the ADH1 promoter, bcy1 cells did not accumulate
glycogen despite increased GS-2. Overexpression of truncated GS-2, however,
resulted in definite though reduced glycogen accumulation; the glycogen
synthesized was structurally distinct from wild type with properties
characteristic of less branched polysaccharide. We conclude that the cAMP
pathway controls both the expression and the phosphorylation state of GS-2.
Furthermore, other factor(s) necessary for glycogen biosynthesis, such as
the branching enzyme GLC3, must also be under negative control by the cAMP
pathway. The results demonstrate interactive controls of GS-2 by the
cAMP-dependent and SNF1 protein kinases.
Interactions between cAMP-dependent and SNF1 protein kinases in the control of glycogen accumulation in Saccharomyces cerevisiae
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
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