GPH1/YPR160W Summary Help

GPH1 BASIC INFORMATION

Standard Name GPH1
Systematic Name YPR160W
Feature Type ORF, Verified
Description Non-essential glycogen phosphorylase required for the mobilization of glycogen, activity is regulated by cyclic AMP-mediated phosphorylation, expression is regulated by stress-response elements and by the HOG MAP kinase pathway (1, 2, 3 and see Summary Paragraph)
Name Description Glycogen PHosphorylase 1
GO Annotations All GPH1 GO evidence and references
    View Computational GO annotations for GPH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Pathways
Mutant Phenotype All GPH1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions GPH1 All interactions details and references
37 total interaction(s) for 35 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 13
  • Two-hybrid: 2

Genetic Interactions
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 1

Sequence Information
ChrXVI:861302 to 864010 | ORF Map | GBrowse
This feature contains embedded feature(s): YPR160C-A | YPR160W-A
Gbrowse
Last Update Coordinates: 2004-07-21 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2709 861302..864010 2004-07-21 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000006364

GPH1 RESOURCES

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Expression Summary histogram

SUMMARY PARAGRAPH for GPH1

Glycogen is a branched polysaccharide of high molecular mass that is used as a storage carbohydrate. In S. cerevisiae, glycogen is typically catabolized to glucose-1-phosphate and glucose by the Gph1p glycogen phosphorylase and the Gdb1p debranching enzyme (4). However, during sporulation, glycogen is rapidly catabolized to glucose by the Sga1p glucoamylase (4).

The Gph1p glycogen phosphorylase (EC 2.4 1.1) catalyzes the sequential phosphorolysis of alpha-1,4-linked glucose units in glycogen until two or three glucose units remain before an alpha-1,6-branch point (1, 5). At that point, Gph1p is not able to degrade glycogen further until the branch is resolved into a chain of linear alpha (1,4)-glucosidic bonds by debranching enzyme Gdb1p. Gph1p is then able to resume degrading the glycogen molecule into glucose-1-phosphate (4).

The N-terminus of Gph1p is involved in determining the quaternary structure, and possibly the activity, of the enzyme (6). The activity of Gph1p is also regulated by cyclic AMP-mediated phosphorylation (1). GPH1 expression is regulated by stress-response elements and the Hog1p-mitogen-activated protein (MAP) kinase-dependent pathway (2), and is induced during late exponential growth phase (1). gph1 null mutants are viable, but display increased accumulation of glycogen (1). No phenotypes corresponding to the mammalian glycogen storage disease VI, which is associated with mutations in human glycogen phosphorylase (PYGL), have been found for S. cerevisiae gph1 null mutants (4).

Last updated: 2005-08-25

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GPH1]

1) Hwang PK, et al.  (1989) Molecular analysis of GPH1, the gene encoding glycogen phosphorylase in Saccharomyces cerevisiae. Mol Cell Biol 9(4):1659-66
2) Sunnarborg SW, et al.  (2001) Expression of the yeast glycogen phosphorylase gene is regulated by stress-response elements and by the HOG MAP kinase pathway. Yeast 18(16):1505-14
3) Perez-Torrado R, et al.  (2002) Wine yeast strains engineered for glycogen overproduction display enhanced viability under glucose deprivation conditions. Appl Environ Microbiol 68(7):3339-44
4) Francois J and Parrou JL  (2001) Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 25(1):125-45
5) Teste MA, et al.  (2000) The Saccharomyces cerevisiae YPR184w gene encodes the glycogen debranching enzyme. FEMS Microbiol Lett 193(1):105-10
6) Lin K, et al.  (1995) Mechanism of regulation in yeast glycogen phosphorylase. J Biol Chem 270(45):26833-9