Glycogen metabolism and signal transduction in mammals and yeast.
Mammalian glycogen synthase, with its complex multisite phosphorylation mechanisms, continues to provide interesting and novel examples of the regulation of protein function. The mammalian enzyme is phosphorylated in a hierarchal manner such that modification of certain sites requires the prior phosphorylation of other sites. Yeast contains two glycogen synthases that have extensive similarities to their mammalian counterpart but the greatest divergence in amino acid sequence is seen precisely in the regions likely to be involved in covalent control. We hope that examination of the control of the yeast glycogen synthase will be as informative as study of the mammalian enzymes, whether by revealing important parallels with the mammalian system or by uncovering major differences in mechanism.
Roach
P J
PJ
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46223.
Cao
Y
Y
Corbett
C A
CA
DePaoli-Roach
A A
AA
Farkas
I
I
Fiol
C J
CJ
Flotow
H
H
Graves
P R
PR
Hardy
T A
TA
Hrubey
T W
TW
D000595:Amino Acid Sequence; D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D005796:Genes; D014453:Glucuronosyltransferase / Q000235:genetics; D006003:Glycogen / Q000378:metabolism*; D006006:Glycogen Synthase / Q000235:genetics / Q000378:metabolism*; D006706:Homeostasis; D008322:Mammals; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D015398:Signal Transduction
D006003:Glycogen; D006006:Glycogen Synthase; D014453:Glucuronosyltransferase; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases