GLC3 BASIC INFORMATION
| Standard Name | GLC3 1 |
|---|---|
| Systematic Name | YEL011W |
| Alias | GHA1 |
| Feature Type | ORF, Verified |
| Description | Glycogen branching enzyme, involved in glycogen accumulation; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm in a punctate pattern (2, 3 and see Summary Paragraph)
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| Name Description | GLyCogen |
| GO Annotations | All GLC3 GO evidence and references |
|---|---|
| View Computational GO annotations for GLC3 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
| Pathways |
|---|
| Mutant Phenotype | All GLC3 Phenotype details and references |
|---|---|
| Classical genetics | |
| reduction of function | |
| Large-scale survey | |
| null |
| Interactions | GLC3 All interactions details and references |
|---|---|
| View additional details at BioGRID | |
| 7 total interaction(s) for 6 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Post-translational Modifications | PhosphoGRID | PhosphoPep Database |
|---|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
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| Primary SGDID | S000000737 |
|---|
ADDITIONAL INFORMATION for GLC3
SUMMARY PARAGRAPH for GLC3
Glycogen, a branched polymer of glucose, is a storage molecule whose accumulation is under rigorous nutritional control in many cells (4). In S. cerevisiae, glycogen biosynthesis involves three processes: nucleation, elongation, and ramification, or branching (5). GLG1 and GLG2 encode self-glucosylating glycogenin glucosyltransferases (EC:2.4.1.186) involved in glycogen nucleation (4). Both Glg1p and Glg2p are able to use UDP-glucose to produce a short alpha (1,4)-glucosyl chain covalently attached to an internal tyrosine residue (6). Glycogen synthase (EC:2.4.1.11, Gsy1p and Gsy2p) is then able to extend the linear alpha (1,4)-chains of glycogen by catalyzing the formation of alpha (1,4)-glucosidic bonds from UDP-glucose at the non-reducing ends (7). Branches can be added into the glycogen molecule by Glc3p, the glycogen branching enzyme (EC:2.4.1.18) in S. cerevisiae (2). No enzyme that releases the glycogen chain from Glg1p or Glg2p has been identified (5).
GLC3 mRNA begins to accumulate when approximately 50% of the environmental glucose is gone, and peaks when environmental glucose is exhausted, similar to other glycogen metabolism genes (8). glc3 null mutants are viable, but do not accumulate glycogen, indicating that branch formation is required for glycogen biosynthesis in S. cerevisiae (2). glc3 null mutants do not display phenotypes similar to the Glycogen Storage Disease IV that is associated with mutations in the human glycogen branching enzyme GBE1 (5).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for GLC3]
| 1) | Pringle, J. (1985) Personal Communication, Mortimer Map Edition 9 |
| 2) | Thon VJ, et al. (1992) Coordinate regulation of glycogen metabolism in the yeast Saccharomyces cerevisiae. Induction of glycogen branching enzyme. J Biol Chem 267(21):15224-8 |
| 3) | Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 |
| 4) | Cheng C, et al. (1995) Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae. Mol Cell Biol 15(12):6632-40 |
| 5) | Francois J and Parrou JL (2001) Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 25(1):125-45 |
| 6) | Mu J, et al. (1996) Initiation of glycogen synthesis in yeast. Requirement of multiple tyrosine residues for function of the self-glucosylating Glg proteins in vivo. J Biol Chem 271(43):26554-60 |
| 7) | Farkas I, et al. (1991) Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by distinct genes that are differentially controlled. J Biol Chem 266(24):15602-7 |
| 8) | Parrou JL, et al. (1999) Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations in Saccharomyces cerevisiae. Yeast 15(3):191-203 |






