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Gene Review

ALG2  -  GDP-Man:Man(1)GlcNAc(2)-PP-dolichol alpha...

Saccharomyces cerevisiae S288c

Synonyms: Alpha-1,3/1,6-mannosyltransferase ALG2, Asparagine-linked glycosylation protein 2, GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase, GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase, GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase, ...
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Disease relevance of ALG2

  • A cell-membrane fraction isolated from Escherichia coli overexpressing thioredoxin-tagged Alg2 was used to demonstrate that this enzyme actually carries out an alpha1,3-mannosylation, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the pathway [1].

High impact information on ALG2

  • There was virtually no outer chain addition in the alg2 and alg4 mutants. alg4 was the only mutant that failed to secrete invertase [2].
  • Here we have used ALG-2 as bait in a yeast two hybrid screen of a mouse brain cDNA library [3].
  • Vito et al have shown that ALG-2 expression is required for apoptosis following a number of death stimuli,1 although nothing is known about the effectors which underlie ALG-2 function [3].
  • The Ca2+-binding Protein ALG-2 Is Recruited to Endoplasmic Reticulum Exit Sites by Sec31A and Stabilizes the Localization of Sec31A [4].
  • In addition to these Alg11-related proteins, Alg11p is also similar to Alg2p, a protein that regulates the addition of the third mannose to the core oligosaccharide [5].

Biological context of ALG2


Anatomical context of ALG2

  • Thermosensitive mutants of Saccharomyces cerevisiae, affected in the endoplasmic reticulum (ER) located glycosylation, i.e. in Dol-P-Man synthase (dpm1), in beta-1,4 mannosyl transferase (alg1) and in alpha-1,3 mannosyltransferase (alg2), were used to assess the role of GDP-Man availability for the synthesis of dolichol-linked saccharides [9].

Associations of ALG2 with chemical compounds

  • ALG2 of Saccharomyces cerevisiae encodes the glycosyltransferase that mannosylates Man2GlcNAc2-dolichol diphosphate (PP-Dol) and Man1GlcNAc2-PP-Dol to form Man3GlcNAc2-PP-Dol [6].
  • Consistent with this, rapid degradation of ALG7, ALG1 and ALG2 mRNAs was completely abolished in the presence of cycloheximide [7].
  • In addition, labeling of the wild-type yeast cells with [3H]palmitate in the presence of tunicamycin revealed the incorporation of [3H]palmitate into the same five bands as found in the alg1 and alg2 mutants at the non-permissive temperature without tunicamycin [10].
  • We present evidence indicating that, in H. polymorpha, neither isocitrate lyase activity nor the ALG2 gene product are necessary for C(1)-peroxisome degradation triggered by ethanol [11].
  • To set the basis for molecular and cellular studies of the glyoxylate cycle in methylotrophic yeasts, we isolated and characterized ALG2, the Hansenula polymorpha isocitrate lyase gene [11].

Physical interactions of ALG2

  • The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11 [12].

Other interactions of ALG2

  • The cloned cDNA under the control of the yeast GAL1 promoter complemented the temperature-sensitive (ts) growth of the alg2-1 mutant of S. cerevisiae, indicating that it represented a functional ALG2 homologue of R. pusillus [6].
  • In the alg1 and alg2 mutants, complemented with MPG1 gene, N-glycosylation of invertase was in part restored, to a degree comparable to that of the wild-type control [9].
  • The second fragment covers the 72.6 kb region between the chromosomal markers CYH2 and ALG2 [13].
  • ALG2, the Hansenula polymorpha isocitrate lyase gene [11].

Analytical, diagnostic and therapeutic context of ALG2


  1. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. O'Reilly, M.K., Zhang, G., Imperiali, B. Biochemistry (2006) [Pubmed]
  2. Yeast mutants deficient in protein glycosylation. Huffaker, T.C., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  3. Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Missotten, M., Nichols, A., Rieger, K., Sadoul, R. Cell Death Differ. (1999) [Pubmed]
  4. The Ca2+-binding Protein ALG-2 Is Recruited to Endoplasmic Reticulum Exit Sites by Sec31A and Stabilizes the Localization of Sec31A. Yamasaki, A., Tani, K., Yamamoto, A., Kitamura, N., Komada, M. Mol. Biol. Cell (2006) [Pubmed]
  5. The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum. Cipollo, J.F., Trimble, R.B., Chi, J.H., Yan, Q., Dean, N. J. Biol. Chem. (2001) [Pubmed]
  6. Characterization of alg2 encoding a mannosyltransferase in the zygomycete fungus Rhizomucor pusillus. Yamazaki, H., Shiraishi, N., Takeuchi, K., Ohnishi, Y., Horinouchi, S. Gene (1998) [Pubmed]
  7. Growth-related coordinate regulation of the early N-glycosylation genes in yeast. Kukuruzinska, M.A., Lennon, K. Glycobiology (1994) [Pubmed]
  8. Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces cerevisiae: the alg2 mutation. Jackson, B.J., Kukuruzinska, M.A., Robbins, P. Glycobiology (1993) [Pubmed]
  9. Overexpression of GDP-mannose pyrophosphorylase in Saccharomyces cerevisiae corrects defects in dolichol-linked saccharide formation and protein glycosylation. Janik, A., Sosnowska, M., Kruszewska, J., Krotkiewski, H., Lehle, L., Palamarczyk, G. Biochim. Biophys. Acta (2003) [Pubmed]
  10. Fatty acylation of yeast glycoproteins proceeds independently of N-linked glycosylation. Appukuttan, P.S., Wu, H.C. FEBS Lett. (1989) [Pubmed]
  11. ALG2, the Hansenula polymorpha isocitrate lyase gene. Berardi, E., Gambini, A., Bellu, A.R. Yeast (2003) [Pubmed]
  12. Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum. Gao, X.D., Nishikawa, A., Dean, N. Glycobiology (2004) [Pubmed]
  13. Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII. Rieger, M., Brückner, M., Schäfer, M., Müller-Auer, S. Yeast (1997) [Pubmed]
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