ArticleGlycobiology2009
A novel role for Gtb1p in glucose trimming of N-linked glycans.
Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.Protein science : a publication of the Protein Society · 2016Article
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- Expression of α-subunit of α-glucosidase II in adult mouse brain regions and selected organs.Journal of neuroscience research · 2015Article
- Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.The Journal of biological chemistry · 2013Article
- Review
- Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins.Plant molecular biology · 2012Article
- Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core.PloS one · 2012Article
- Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.Molecular biology of the cell · 2011Article
- UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control.Seminars in cell & developmental biology · 2010Review
- Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.Biochimica et biophysica acta · 2010Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Glucosidase II (GluII) is a glycan-trimming enzyme active on nascent glycoproteins in the endoplasmic reticulum (ER). It trims the middle and innermost glucose residues (Glc2 and Glc1) from N-linked glycans. The monoglucosylated glycan produced by the first GluII trimming reaction is recognized by calnexin/calreticulin and serves as the signal for entry into this folding pathway. GluII is a heterodimer of alpha and beta subunits corresponding to yeast Gls2p and Gtb1p, respectively. While Gls2p contains the glucosyl hydrolase active site, the Gtb1p subunit has previously been shown to be essential for the Glc1 trimming event. Here we demonstrate that Gtb1p also determines the rate of Glc2 trimming. In order to further dissect these activities we mutagenized a number of conserved residues across the protein. Our data demonstrate that both the MRH and G2B domains of Gtb1p contribute to the Glc2 trimming event but that the MRH domain is essential for Glc1 trimming.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.