ArticleJournal of immunology (Baltimore, Md. : 1950)2009
N-glycosylation enhances presentation of a MHC class I-restricted epitope from tyrosinase.
Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- A new strategy to separate peptide methionine sulfoxides stereoisomers for potential immunotherapy application.Analytical and bioanalytical chemistry · 2026Article
- The immunology of vitiligo.Nature reviews. Immunology · 2026Review
- Engineered Proteins and Chemical Tools to Probe the Cell Surface Proteome.Chemical reviews · 2025Review
- Antigen presentation of post-translationally modified peptides in major histocompatibility complexes.Immunology and cell biology · 2025Review
- The Role of Glycosylation in Inflammatory Diseases.Advances in experimental medicine and biology · 2021Article
- Recent progress on MHC-I epitope prediction in tumor immunotherapy.American journal of cancer research · 2021Review
- Immunopeptidomic Analysis Reveals That Deamidated HLA-bound Peptides Arise Predominantly from Deglycosylated Precursors.Molecular & cellular proteomics : MCP · 2020Article
- Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Human molecular genetics · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Surface display of glycosylated Tyrosinase related protein-2 (TRP-2) tumour antigen on Lactococcus lactis.BMC biotechnology · 2015Article
- An antigenic peptide produced by reverse splicing and double asparagine deamidation.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Insights into the processing of MHC class I ligands gained from the study of human tumor epitopes.Cellular and molecular life sciences : CMLS · 2011Review
- Variant of TYR and autoimmunity susceptibility loci in generalized vitiligo.The New England journal of medicine · 2010Article
- Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2010Article
- Purification and N-glycosylation analysis of melanoma antigen dopachrome tautomerase.The protein journal · 2010Article
- Defective ribosomal products are the major source of antigenic peptides endogenously generated from influenza A virus neuraminidase.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity.The Journal of biological chemistry · 2010Article
- Post-translationally modified T cell epitopes: immune recognition and immunotherapy.Journal of molecular medicine (Berlin, Germany) · 2009Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We recently demonstrated that the mechanism of processing of an HLA-A*0201-restricted peptide epitope, Tyr(369)(D), derived from the membrane protein tyrosinase, involves retrotranslocation of glycosylated molecules from the endoplasmic reticulum to the cytosol, removal of an N-linked carbohydrate from Asn(371) by peptide N-glycanase, proteolysis by the proteasome and other proteases, and retransport of the resulting peptides into the endoplasmic reticulum for association with HLA-A*0201. Carbohydrate removal results in deamidation of Asn(371) to aspartic acid. The asparagine-containing homolog of this peptide, Tyr(369)(N), is not presented by tyrosinase-expressing cells, and this has been presumed to be due to quantitative glycosylation of Asn(371). Although examining cytosolic intermediates that accumulated in human melanoma cells treated with proteasome inhibitors, we were surprised to find both molecules that had been deglycosylated by peptide N-glycanase and a large number of molecules that had not been previously glycosylated. The failure of Tyr(369)(N) to be processed and presented from these latter molecules may be partially due to a process of deamidation independent of glycosylation. However, we also established that proteasomes degrade tyrosinase molecules that are still glycosylated, giving rise to a set of discrete intermediates that are not observed when unglycosylated molecules are degraded. We propose that Tyr(369)(N) fails to be presented because unglycosylated tyrosinase is degraded rapidly and relatively nonselectively. In contrast, glycosylation alters the selectivity of tyrosinase processing by the proteasome, enhancing the production or survival of Tyr(369)(D).
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Registered trials
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