ArticleJournal of immunology (Baltimore, Md. : 1950)2011
Distinct functions for the glycans of tapasin and heavy chains in the assembly of MHC class I molecules.
Article in Journal of immunology (Baltimore, Md. : 1950), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR.Molecular immunology · 2021Article
- Article
- Protecting Tumors by Preventing Human Papilloma Virus Antigen Presentation: Insights from Emerging Bioinformatics Algorithms.Cancers · 2019Review
- Preferential interaction of MHC class I with TAPBPR in the absence of glycosylation.Molecular immunology · 2019Article
- Whole genome duplications have provided teleosts with many roads to peptide loaded MHC class I molecules.BMC evolutionary biology · 2018Article
- 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
- The key role of calreticulin in immunomodulation induced by chemotherapeutic agents.International journal of clinical oncology · 2015Article
- Distinct assembly profiles of HLA-B molecules.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- ERAAP and tapasin independently edit the amino and carboxyl termini of MHC class I peptides.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Calreticulin in the immune system: ins and outs.Trends in immunology · 2013Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Complexes of specific assembly factors and generic endoplasmic reticulum (ER) chaperones, collectively called the MHC class I peptide-loading complex (PLC), function in the folding and assembly of MHC class I molecules. The glycan-binding chaperone calreticulin (CRT) and partner oxidoreductase ERp57 are important in MHC class I assembly, but the sequence of assembly events and specific interactions involved remain incompletely understood. We show that the recruitments of CRT and ERp57 to the PLC are codependent and also dependent upon the ERp57 binding site and the glycan of the assembly factor tapasin. Furthermore, the ERp57 binding site and the glycan of tapasin enhance β(2)m and MHC class I heavy (H) chain recruitment to the PLC, with the ERp57 binding site having the dominant effect. In contrast, the conserved MHC class I H chain glycan played a minor role in CRT recruitment into the PLC, but impacted the recruitment of H chains into the PLC, and glycan-deficient H chains were impaired for tapasin-independent and tapasin-assisted assembly. The conserved MHC class I glycan and tapasin facilitated an early step in the assembly of H chain-β(2)m heterodimers, for which tapasin-ERp57 or tapasin-CRT complexes were not required. Together, these studies provide insights into how PLCs are constructed, demonstrate two distinct mechanisms by which PLCs can be stabilized, and suggest the presence of intermediate H chain-deficient PLCs.
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Registered trials
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