ArticleProceedings of the National Academy of Sciences of the United States of America2006
Direct peptide-regulatable interactions between MHC class I molecules and tapasin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Review
- Mass Spectrometric Profiling of HLA-B44 Peptidomes Provides Evidence for Tapasin-Mediated Tryptophan Editing.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Introducing Molecular Chaperones into the Causality and Prospective Management of Autoimmune Hepatitis.Digestive diseases and sciences · 2023Review
- Major histocompatibility complex class I assembly within endolysosomal pathways.Current opinion in immunology · 2023Review
- Mass spectrometric profiling of HLA-B44 peptidomes provides evidence for tapasin-mediated tryptophan editing.bioRxiv : the preprint server for biology · 2023Article
- Endo-lysosomal assembly variations among human leukocyte antigen class I (HLA class I) allotypes.eLife · 2023Article
- Chaperone function in antigen presentation by MHC class I molecules-tapasin in the PLC and TAPBPR beyond.Frontiers in immunology · 2023Review
- Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.Nature communications · 2022Article
- Designing a Recombinant Vaccine againstVaccines · 2022Article
- Know thy immune self and non-self: Proteomics informs on the expanse of self and non-self, and how and where they arise.Proteomics · 2021Review
- Conformational sensing of major histocompatibility complex (MHC) class I molecules by immune receptors and intracellular assembly factors.Current opinion in immunology · 2021Review
- HLA tapasin independence: broader peptide repertoire and HIV control.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Endoplasmic reticulum chaperones stabilize ligand-receptive MR1 molecules for efficient presentation of metabolite antigens.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Variations in MHC class I antigen presentation and immunopeptidome selection pathways.F1000Research · 2020Review
- Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Variations in HLA-B cell surface expression, half-life and extracellular antigen receptivity.eLife · 2018Article
- Article
- Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Distinct assembly profiles of HLA-B molecules.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- A mechanistic basis for the co-evolution of chicken tapasin and major histocompatibility complex class I (MHC I) proteins.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Tapasin (Tpn) has been implicated in multiple steps of the MHC class I assembly pathway, but the mechanisms of function remain incompletely understood. Using purified proteins, we could demonstrate direct binding of Tpn to peptide-deficient forms of MHC class I molecules at physiological temperatures. Tpn also bound to M10.5, a pheromone receptor-associated MHC molecule that has an open and empty groove and that shares significant sequence identity with class I sequences. Two types of MHC class I-Tpn complexes were detectable in vitro depending on the input proteins; those depleted in beta(2)m, and those containing beta(2)m. Both were competent for subsequent assembly with peptides, but the latter complexes assembled more rapidly. Thus, the assembly rate of Tpn-associated class I was determined by the conditions under which Tpn-MHC class I complexes were induced. Peptide loading of class I inhibited Tpn-class I-binding interactions, and peptide-depletion enhanced binding. In combination with beta(2)m, certain peptides induced efficient dissociation of preformed Tpn-class I complexes. Together, these studies demonstrate direct Tpn-MHC class I interactions and preferential binding of empty MHC class I by Tpn, and that the Tpn-class I interaction is regulated by both beta(2)m and peptide. In cells, Tpn is likely to be a direct mediator of peptide-regulated binding and release of MHC class I from the TAP complex.
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