ALG8 BASIC INFORMATION
| Standard Name | ALG8 1 |
|---|---|
| Systematic Name | YOR067C |
| Alias | YOR29-18 |
| Feature Type | ORF, Verified |
| Description | Glucosyl transferase, involved in N-linked glycosylation; adds glucose to the dolichol-linked oligosaccharide precursor prior to transfer to protein during lipid-linked oligosaccharide biosynthesis; similar to Alg6p (1, 2 and see Summary Paragraph)
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| Name Description | Asparagine-Linked Glycosylation 1, 2 |
| GO Annotations | All ALG8 GO evidence and references |
|---|---|
| View Computational GO annotations for ALG8 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Pathways |
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| Interactions | ALG8 All interactions details and references |
|---|---|
| 87 total interaction(s) for 50 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000005593 |
|---|
ADDITIONAL INFORMATION for ALG8
SUMMARY PARAGRAPH for ALG8
During N-linked glycosylation of proteins, oligosaccharide chains are assembled on the carrier molecule dolichyl pyrophosphate in the following order: 2 molecules of N-acetylglucosamine (GlcNAc), 9 molecules of mannose, and 3 molecules of glucose. These 14-residue oligosaccharide cores are then transferred to asparagine residues on nascent polypeptide chains in the endoplasmic reticulum (ER). As proteins progress through the Golgi apparatus, the oligosaccharide cores are modified by trimming and extension to generate a diverse array of glycosylated proteins (reviewed in 3, 4).
ALG8 encodes an ER-membrane-bound alpha 1,3 glucosyltransferase that catalyzes the addition of the second of three glucose moieties (2) to growing lipid-linked oligosaccharides (LLO's) in the lumen of the endoplasmic reticulum. The first and third glucose residues are added by Alg6p (a close homolog of Alg8p) and Die2p (also known as Alg10p), respectively. Mutants lacking Alg8p produce truncated LLO's with only one glucose residue (5) that are able to be transferred to proteins with reduced efficiency (2). Mutations in human ALG8 (OMIM) have been implicated in the
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for ALG8]
| 1) | Stagljar I, et al. (1994) New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc Natl Acad Sci U S A 91(13):5977-81 |
| 2) | Runge KW and Robbins PW (1986) A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J Biol Chem 261(33):15582-90 |
| 3) | Herscovics A and Orlean P (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50 |
| 4) | Burda P and Aebi M (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57 |
| 5) | Munoz MD, et al. (1994) Glycosylation of yeast exoglucanase sequons in alg mutants deficient in the glucosylation steps of the lipid-linked oligosaccharide. Presence of glucotriose unit in Dol-PP-GlcNAc2Man9Glc3 influences both glycosylation efficiency and selection of N-linked sites. Biochim Biophys Acta 1201(3):361-6 |
| 6) | Chantret I, et al. (2003) A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J Biol Chem 278(11):9962-71 |
| 7) | Schollen E, et al. (2004) Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). J Med Genet 41(7):550-6 |




