The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

GPH1  -  Gph1p

Saccharomyces cerevisiae S288c

Synonyms: Glycogen phosphorylase, P9584.1, YPR160W
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of GPH1


High impact information on GPH1


Biological context of GPH1

  • Thus, deletion of GPH1 partially reversed the loss of glycogen accumulation in autophagy mutants [6].
  • Haploid cells disrupted in GPH1 lacked phosphorylase activity and attained higher levels of intracellular glycogen but otherwise were similar to wild-type cells [7].
  • Increases in phosphorylase activity of 10- to 40-fold were detected in cells carrying multiple copies of GPH1-containing 2 microns plasmid [7].
  • GPH1 was found not to be an essential gene in yeast cells [7].
  • To assess the role of glycogen and phosphorylase-catalyzed glycogenolysis in the yeast life cycle, yeast strains lacking a functional GPH1 gene or containing multiple copies of the gene were constructed [7].

Anatomical context of GPH1


Associations of GPH1 with chemical compounds

  • GPH1 did not appear to be under formal glucose repression, since transcriptional induction occurred well in advance of glucose depletion from the medium [7].
  • Absence of functional GPH1 did not impair cells from synthesizing and storing trehalose [7].
  • Uncouplers, but not a nitrogen source, also induced an activation of glycogen phosphorylase and an inactivation of glycogen synthase when added to the cdc35 mutant incubated at the restrictive temperature of 35 degrees C without affecting cyclic AMP concentration [9].
  • Glycogen phosphorylase from Saccharomyces cerevisiae is activated by the covalent phosphorylation of a single threonine residue in the N terminus of the protein [10].
  • The location and role of the active-site arginyl residues in the beta 2 subunit and in two other enzymes which contain pyridoxal phosphate, aspartate aminotransferase and glycogen phosphorylase, are compared [11].

Other interactions of GPH1


Analytical, diagnostic and therapeutic context of GPH1


  1. Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Burwinkel, B., Bakker, H.D., Herschkovitz, E., Moses, S.W., Shin, Y.S., Kilimann, M.W. Am. J. Hum. Genet. (1998) [Pubmed]
  2. Accelerated protein aggregation induced by macrophage migration inhibitory factor under heat stress conditions. Cherepkova, O.A., Lyutova, E.M., Eronina, T.B., Gurvits, B.Y. Biochemistry Mosc. (2006) [Pubmed]
  3. A protein phosphorylation switch at the conserved allosteric site in GP. Lin, K., Rath, V.L., Dai, S.C., Fletterick, R.J., Hwang, P.K. Science (1996) [Pubmed]
  4. GAC1 may encode a regulatory subunit for protein phosphatase type 1 in Saccharomyces cerevisiae. François, J.M., Thompson-Jaeger, S., Skroch, J., Zellenka, U., Spevak, W., Tatchell, K. EMBO J. (1992) [Pubmed]
  5. Control by phosphorylation. Johnson, L.N., O'Reilly, M. Curr. Opin. Struct. Biol. (1996) [Pubmed]
  6. Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p. Wang, Z., Wilson, W.A., Fujino, M.A., Roach, P.J. Mol. Cell. Biol. (2001) [Pubmed]
  7. Molecular analysis of GPH1, the gene encoding glycogen phosphorylase in Saccharomyces cerevisiae. Hwang, P.K., Tugendreich, S., Fletterick, R.J. Mol. Cell. Biol. (1989) [Pubmed]
  8. Identification of glycogen phosphorylase and creatine kinase as calpain substrates in skeletal muscle. Purintrapiban, J., Wang, M., Forsberg, N.E. Int. J. Biochem. Cell Biol. (2001) [Pubmed]
  9. The control of glycogen metabolism in yeast. 1. Interconversion in vivo of glycogen synthase and glycogen phosphorylase induced by glucose, a nitrogen source or uncouplers. François, J., Villanueva, M.E., Hers, H.G. Eur. J. Biochem. (1988) [Pubmed]
  10. Purification and crystallization of glycogen phosphorylase from Saccharomyces cerevisiae. Rath, V.L., Hwang, P.K., Fletterick, R.J. J. Mol. Biol. (1992) [Pubmed]
  11. L-serine binds to arginine-148 of the beta 2 subunit of Escherichia coli tryptophan synthase. Tanizawa, K., Miles, E.W. Biochemistry (1983) [Pubmed]
  12. Expression of the yeast glycogen phosphorylase gene is regulated by stress-response elements and by the HOG MAP kinase pathway. Sunnarborg, S.W., Miller, S.P., Unnikrishnan, I., LaPorte, D.C. Yeast (2001) [Pubmed]
  13. DNA sequence analysis of a 10.4 kbp region on the right arm of yeast chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two novel tRNA genes. Roemer, T., Fortin, N., Bussey, H. Yeast (1994) [Pubmed]
  14. Wine yeast strains engineered for glycogen overproduction display enhanced viability under glucose deprivation conditions. Pérez-Torrado, R., Gimeno-Alcañiz, J.V., Matallana, E. Appl. Environ. Microbiol. (2002) [Pubmed]
  15. Mechanism of stimulation of endogenous fermentation in yeast by carbonyl cyanide m-chlorophenylhydrazone. Noshiro, A., Purwin, C., Laux, M., Nicolay, K., Scheffers, W.A., Holzer, H. J. Biol. Chem. (1987) [Pubmed]
  16. Regulation of yeast glycogen phosphorylase by the cyclin-dependent protein kinase Pho85p. Wilson, W.A., Wang, Z., Roach, P.J. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  17. Glycogen phosphorylase in Dictyostelium discoideum: demonstration of two developmentally regulated forms, purification to homogeneity, immunochemical analysis, cAMP induction, in vitro translation, and molecular cloning. Rutherford, C.L., Naranan, V., Brickey, D.A., Sucic, J.F., Rogers, P.V., Selmin, O. Dev. Genet. (1988) [Pubmed]
WikiGenes - Universities