ArticleeLife2018
TAPBPR mediates peptide dissociation from MHC class I using a leucine lever.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
- Identification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR.Frontiers in immunology · 2026Article
- CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- TAPBPR promotes editing of the HLA-B44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan.Frontiers in immunology · 2025Article
- Review
- Reanalysis of Immunopeptidomics Datasets Provides Mechanistic Insight into TAPBPR-Mediated Peptide Editing on HLA-A, -B and -C Molecules.Wellcome open research · 2024Article
- Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes.Current opinion in immunology · 2023Review
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
- Partial peptide dissociation and binding groove plasticity in two major histocompatibility complex class I alleles - differences between allelesRSC advances · 2022Article
- Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.Nature communications · 2022Article
- TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules.Nature chemical biology · 2022Article
- Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity.Frontiers in immunology · 2022Review
- The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR.Molecular immunology · 2021Article
- Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules.Nature communications · 2021Article
- Partnering for the major histocompatibility complex class II and antigenic determinant requires flexibility and chaperons.Current opinion in immunology · 2021Review
- TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap.Nature communications · 2021Article
- Making Insulin and Staying Out of Autoimmune Trouble: The Beta-Cell Conundrum.Frontiers in immunology · 2021Review
- Peptide cargo tunes a network of correlated motions in human leucocyte antigens.The FEBS journal · 2020Article
- Atomistic structure and dynamics of the human MHC-I peptide-loading complex.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Approaching complexity: systems biology and ms-based techniques to address immune signaling.Expert review of proteomics · 2020Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Tapasin and TAPBPR are known to perform peptide editing on major histocompatibility complex class I (MHC I) molecules; however, the precise molecular mechanism(s) involved in this process remain largely enigmatic. Here, using immunopeptidomics in combination with novel cell-based assays that assess TAPBPR-mediated peptide exchange, we reveal a critical role for the K22-D35 loop of TAPBPR in mediating peptide exchange on MHC I. We identify a specific leucine within this loop that enables TAPBPR to facilitate peptide dissociation from MHC I. Moreover, we delineate the molecular features of the MHC I F pocket required for TAPBPR to promote peptide dissociation in a loop-dependent manner. These data reveal that chaperone-mediated peptide editing on MHC I can occur by different mechanisms dependent on the C-terminal residue that the MHC I accommodates in its F pocket and provide novel insights that may inform the therapeutic potential of TAPBPR manipulation to increase tumour immunogenicity.
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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.