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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

DIE2  -  dolichyl-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP...

Saccharomyces cerevisiae S288c

Synonyms: ALG10, Alpha-1,2-glucosyltransferase ALG10-A, Alpha-2-glucosyltransferase ALG10, Asparagine-linked glycosylation protein 10, Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase, ...
 
 
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High impact information on DIE2

  • Gene-disruption experiments revealed that DIE1 was essential for the expression of ITR1 but that DIE2 was not [1].
  • Experiments involving lacZ fusion genes showed that multicopy DIE2 resulted in an increase in the expression of both ITR1 and INO1 [1].
  • DIE2 is more effective for ITR1 expression than DIE1 [1].
  • Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrates that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase [2].
  • The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation [2].
 

Associations of DIE2 with chemical compounds

  • However, the growth defect of the hac1-alg10 double disrupted was partially, but significantly, suppressed by the addition of inositol to the medium [3].

References

  1. Isolation and characterization of genes that promote the expression of inositol transporter gene ITR1 in Saccharomyces cerevisiae. Nikawa, J., Hosaka, K. Mol. Microbiol. (1995) [Pubmed]
  2. The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Burda, P., Aebi, M. Glycobiology (1998) [Pubmed]
  3. Effects of N-glycosylation and inositol on the ER stress response in yeast Saccharomyces cerevisiae. Uchimura, S., Sugiyama, M., Nikawa, J. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
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