ArticleThe Journal of experimental medicine1998
The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol.
Article in The Journal of experimental medicine, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 120 citations in OpenAlex.
- Melanoma-specific tumor-infiltrating lymphocytes but not circulating melanoma-specific T cells may predict survival in resected advanced-stage melanoma patients.Cancer immunology, immunotherapy : CII · 2006Trial
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- NGLY1 as an Emerging Critical Modulator for Neurodevelopment and Pathogenesis in the Brain.International journal of molecular sciences · 2025Review
- Kinetically distinct processing pathways diversify the CD8Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Immunopeptidomic Analysis Reveals That Deamidated HLA-bound Peptides Arise Predominantly from Deglycosylated Precursors.Molecular & cellular proteomics : MCP · 2020Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- DRiPs solidify: progress in understanding endogenous MHC class I antigen processing.Trends in immunology · 2011Review
- 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
- Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2010Article
- N-glycosylation enhances presentation of a MHC class I-restricted epitope from tyrosinase.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- MHC class II presentation of gp100 epitopes in melanoma cells requires the function of conventional endosomes and is influenced by melanosomes.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.EMBO reports · 2007Article
- Rethinking peptide supply to MHC class I molecules.Nature reviews. Immunology · 2007Review
- The contributions of mass spectrometry to understanding of immune recognition by T lymphocytes.International journal of mass spectrometry · 2007Article
- Intracellular composition of fatty acid affects the processing and function of tyrosinase through the ubiquitin-proteasome pathway.The Biochemical journal · 2006Article
- A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.The EMBO journal · 2004Article
- A role for N-glycanase in the cytosolic turnover of glycoproteins.The EMBO journal · 2003Article
- Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway.The Journal of experimental medicine · 2001Article
- Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Formation of major histocompatibility complex class I-associated peptides from membrane proteins has not been thoroughly investigated. We examined the processing of an HLA-A*0201-associated epitope, YMDGTMSQV, that is derived from the membrane protein tyrosinase by posttranslational conversion of the sequence YMNGTMSQV. Only YMDGTMSQV and not YMNGTMSQV was presented by HLA-A*0201 on cells expressing full-length tyrosinase, although both peptides have similar affinities for HLA-A*0201 and are transported by TAP. In contrast, translation of YMNGTMSQV in the cytosol, as a minigene or a larger fragment of tyrosinase, led to the presentation of the unconverted YMNGTMSQV. This was not due to overexpression leading to saturation of the processing/conversion machinery, since presentation of the converted peptide, YMDGTMSQV, was low or undetectable. Thus, presentation of unconverted peptide was associated with translation in the cytosol, suggesting that processing of the full-length tyrosinase occurs after translation in the endoplasmic reticulum. Nevertheless, presentation of YMDGTMSQV in cells expressing full-length tyrosinase was TAP (transporter associated with antigen processing) and proteasome dependent. After inhibition of proteasome activity, tyrosinase species could be detected in the cytosol. We propose that processing of tyrosinase involves translation in the endoplasmic reticulum, export of full-length tyrosinase to the cytosol, and retransport of converted peptides by TAP for association with HLA-A*0201.
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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.