ArticleNature communications2022
Structure of an MHC I-tapasin-ERp57 editing complex defines chaperone promiscuity.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 38 citations in OpenAlex.
- Reconstitution of glycan-driven MHC-I recycling reveals calreticulin as mediator between TAPBPR and tapasin.The EMBO journal · 2026Article
- Dynamic states of an MHC class I molecule during peptide exchange.Nature communications · 2026Article
- Quantitative nanoscale imaging shows peptide-MHC I complexes are monomeric and spatially regulated in human dendritic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genetic characterization of the TAPBP and its allelic association with BF2 in the chicken major histocompatibility complex.Immunogenetics · 2026Article
- Article
- Messing with Signal 1: How Perturbed MHC Class I Antigen Presentation Contributes to Cancer.Cells · 2026Review
- HLA-Shuttle: A system for enhancing antigen presentation in immunologically cold tumors.Science advances · 2026Article
- Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.Science advances · 2026Article
- The race between viral immune evasion and the MHC class I antigen processing pathway.FEMS microbiology reviews · 2026Review
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
- Review
- Loss of Tapasin in Tumors Potentiates T-Cell Recognition and Anti-Tumor Effects of Immune Checkpoint Blockade.Cancer science · 2025Article
- 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
- Evidence of focusing the MHC class I immunopeptidome by tapasin.Frontiers in immunology · 2025Article
- TAPBPR promotes editing of the HLA-B44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan.Frontiers in immunology · 2025Article
- Viral manipulation of the HLA class I antigen processing and presentation pathway.Frontiers in immunology · 2025Review
- How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading.Frontiers in immunology · 2025Article
- Tapasin assembly surveillance by the RNF185/Membralin ubiquitin ligase complex regulates MHC-I surface expression.Nature communications · 2024Article
- Dual role of the peptide-loading complex as proofreader and limiter of MHC-I presentation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adaptive immunity depends on cell surface presentation of antigenic peptides by major histocompatibility complex class I (MHC I) molecules and on stringent ER quality control in the secretory pathway. The chaperone tapasin in conjunction with the oxidoreductase ERp57 is crucial for MHC I assembly and for shaping the epitope repertoire for high immunogenicity. However, how the tapasin-ERp57 complex engages MHC I clients has not yet been determined at atomic detail. Here, we present the 2.7-Å crystal structure of a tapasin-ERp57 heterodimer in complex with peptide-receptive MHC I. Our study unveils molecular details of client recognition by the multichaperone complex and highlights elements indispensable for peptide proofreading. The structure of this transient ER quality control complex provides the mechanistic basis for the selector function of tapasin and showcases how the numerous MHC I allomorphs are chaperoned during peptide loading and editing.
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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.