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ALG5 Alg5p

alg5, dolichylphosphate glucosyltransferase, Alg5p
This gene encodes a member of the glycosyltransferase 2 family. The encoded protein participates in glucosylation of the oligomannose core in N-linked glycosylation of proteins. The addition of glucose residues to the oligomannose core is necessary to ensure substrate recognition, and therefore, effectual transfer of the oligomannose core to the nascent glycoproteins. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2008] (from NCBI)
Top mentioned proteins: ALG6, CAN, ACID, CD45, ALG8
Papers on alg5
Genes involved in protein glycosylation determine the activity and cell internalization of the antifungal peptide PAF26 in Saccharomyces cerevisiae.
Marcos et al., Paterna, Spain. In Fungal Genet Biol, 2013
Increased tolerance to PAF26 was observed in mutants with the following disrupted genes: PMT1-6, EOS1, ALG5, MNN1, MNN4 and MNN5.
The Alg5 ortholog Wollknäuel is essential for correct epidermal differentiation during Drosophila late embryogenesis.
Moussian et al., Tübingen, Germany. In Glycobiology, 2011
Mutations in the Drosophila alg5 gene wollknäuel (wol) that codes for an enzyme initiating the glucosylation of the dolichol-linked oligosaccharide decrease, as expected, glucosylation and the amounts of N-glycosylated proteins such as the cuticle-organizing factor Knickkopf, without affecting their correct localization.
Dolichyl-phosphate-glucose is used to make O-glycans on glycoproteins of Trichomonas vaginalis.
Samuelson et al., Boston, United States. In Eukaryot Cell, 2008
Recently we found that Trichomonas has numerous genes encoding putative dolichyl-phosphate-glucose (Dol-P-Glc) synthases (encoded by ALG5 genes) despite the fact that Trichomonas lacks the glycosyltransferases (encoded by ALG6, ALG8, and ALG10 genes) that use Dol-P-Glc to glucosylate dolichyl-PP-linked glycans.
Wollknauel is required for embryo patterning and encodes the Drosophila ALG5 UDP-glucose:dolichyl-phosphate glucosyltransferase.
Mannervik et al., Stockholm, Sweden. In Development, 2008
In a screen for maternal factors involved in embryo patterning, we isolated mutations in Drosophila ALG5, a UDP-glucose:dolichyl-phosphate glucosyltransferase.
Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation.
Eichler et al., Israel. In Mol Microbiol, 2006
Gene deletions point to certain genes, like alg11, as being essential yet revealed that others, such as the two versions of alg5, are not.
Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system.
Herscovics et al., Montréal, Canada. In J Cell Sci, 2001
A weak interaction was observed between Alg5p and Rer1p.
[Internal symmetry in nucleotide sequences of genes encoding the dolichol cycle enzymes].
Shpakov, Saint Petersburg, Russia. In Tsitologiia, 2000
In genes alg5, alg8 and swp1 of Saccharomyces cerevisiae, gpt of Schizosaccharomyces pombe and human gene alg6, encoding the dolichol cycle enzymes, a mirror type internal symmetry was found.
A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic.
Hennet et al., Zürich, Switzerland. In Proc Natl Acad Sci U S A, 1999
Elaborating on the analogy of this finding with the phenotype of alg5 and alg6 Saccharomyces cerevisiae strains, we have cloned and analyzed the human orthologs to the ALG5 dolichyl phosphate glucosyltransferase and ALG6 dolichyl pyrophosphate Man9GlcNAc2 alpha1,3-glucosyltransferase in four novel CDGS patients.
Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence.
Abeijón et al., Buenos Aires, Argentina. In Mol Biol Cell, 1999
Monoglucosylated protein-linked oligosaccharides were detected in alg6 or alg5 mutant cells, which transfer Man9GlcNAc2 to protein; glucosylation was dependent on the inhibition of glucosidase II or the disruption of the gene encoding this enzyme.
A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo.
te Heesen et al., Zürich, Switzerland. In Proc Natl Acad Sci U S A, 1998
The Alg5 protein also localizes to the membrane of the endoplasmic reticulum, but does not interact with the oligosaccharyltransferase. Specific interactions are detected between Wbp1p and Ost1p, but not between Wbp1p and Alg5p.
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.
Larriba et al., Badajoz, Spain. In Biochim Biophys Acta, 1995
These mutants synthesize and transfer to nascent proteins truncated oligosaccharides lacking two (alg8) or three (alg5 and alg6) glucoses.
Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae.
Aebi et al., Zürich, Switzerland. In Eur J Biochem, 1994
Overexpression of Alg5p in both yeast and Escherichia coli results in an increase of UDP-glucose:dolichyl-phosphate glucosyltransferase activity, whereas a deletion of the yeast gene leads to a loss of this activity and a concomitant underglycosylation of carboxypeptidase Y.
The submicrosomal localization of uridine 5'-diphosphate-glucose dolichyl-phosphate glucosyltransferase and bile acid glucosyltransferase in the human liver.
Matern et al., Aachen, Germany. In J Hepatol, 1994
Uridine 5'-diphosphate-glucose dolichyl-phosphate glucosyltransferase and bile acid glucosyltransferase were quantitatively determined in subcellular fractions obtained by differential centrifugation of human liver homogenate.
Photoaffinity labelling of glycosyltransferases.
Review
Elbein et al., Little Rock, United States. In Glycobiology, 1992
A summary of the past and current uses of these analogues is presented, as well as photoaffinity data for the enzyme UDP-glucose: dolichylphosphate glucosyltransferase (Glc-P-Dol synthase).
Partial Purification, Photoaffinity Labeling, and Properties of Mung Bean UDP-Glucose:Dolicholphosphate Glucosyltransferase.
Elbein et al., San Antonio, United States. In Plant Physiol, 1991
UDP-glucose:dolichylphosphate glucosyltransferase has been purified 734-fold from Triton X-100 solubilized mung bean (Phaseolus aureus) microsomes.
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