ArticleThe Biochemical journal2003
Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 55 citations in OpenAlex.
- Reactive oxygen species promotion drives auranofin's antiviral activity against hepatitis E virus.Journal of virology · 2026Article
- EDEM1 Drives Misfolded Protein Degradation via ERAD and Exploits ER-Phagy as Back-Up Mechanism When ERAD Is Impaired.International journal of molecular sciences · 2020Article
- Role for a Zinc Finger Protein (Zfp111) in Transformation of 208F Rat Fibroblasts by Jaagsiekte Sheep Retrovirus Envelope Protein.Journal of virology · 2015Article
- The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Molecules (Basel, Switzerland) · 2015Review
- Sorting things out through endoplasmic reticulum quality control.Molecular membrane biology · 2010Review
- The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER.Molecular cell · 2009Article
- A luminal flavoprotein in endoplasmic reticulum-associated degradation.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum.The Journal of cell biology · 2009Article
- Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.Molecular cell · 2008Article
- SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation.Molecular biology of the cell · 2008Article
- SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.The Journal of cell biology · 2006Article
- Free N-linked oligosaccharide chains: formation and degradation.Glycoconjugate journal · 2006Review
- The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum.Molecular biology of the cell · 2005Article
- A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, the role of N-linked glycans in the process of ERAD (endoplasmic reticulum-associated degradation) of proteins has been widely recognized. In the present study, we attempted to delineate further the sequence of events leading from a fully glycosylated soluble protein to its deglycosylated form. Degradation intermediates of a truncated form of ribophorin I, namely RI(332), which contains a single N-linked oligosaccharide and is a substrate for the ERAD/ubiquitin-proteasome pathway, were characterized in HeLa cells under conditions blocking proteasomal degradation. The action of a deoxymannojirimycin- and kifunensine-sensitive alpha1,2-mannosidase was shown here to be required for both further glycan processing and progression of RI(332) in the ERAD pathway. In a first step, the Man(8) isomer B, generated by ER mannosidase I, appears to be the major oligomannoside structure associated with RI(332) intermediates. Some other trimmed N-glycan species, in particular Glc(1)Man(7)GlcNAc(2), were also found on the protein, indicating that several mannosidases might be implicated in the initial trimming of the oligomannoside. Secondly, another intermediate of degradation of RI(332) accumulated after proteasome inhibition. We demonstrated that this completely deglycosylated form arose from the action of an N-glycanase closely linked to the ER membrane. Indeed, the deglycosylated form of the protein remained membrane-associated, while being accessible from the cytoplasm to ubiquitinating enzymes and to added protease. Our results indicate that deglycosylation of a soluble ERAD substrate glycoprotein occurs in at least two distinct steps and is coupled with the retro-translocation of the protein preceding its proteasomal degradation.
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