ArticleThe Journal of biological chemistry2014
Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- 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
- Mining Potential Drug Targets and Constructing Diagnostic Models for Heart Failure Based on miRNA-mRNA Networks.Mediators of inflammation · 2022Article
- Relationship between HLA-DPA1 genetic polymorphism and anembryonic pregnancy.Molecular genetics & genomic medicine · 2020Article
- Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018Review
- Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the transporter associated with antigen processing trapped by herpes simplex virus.eLife · 2016Article
- A dual inhibition mechanism of herpesviral ICP47 arresting a conformationally thermostable TAP complex.Scientific reports · 2016Article
- Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.Scientific reports · 2015Article
- Genome-wide SNP identification for the construction of a high-resolution genetic map of Japanese flounder (Paralichthys olivaceus): applications to QTL mapping of Vibrio anguillarum disease resistance and comparative genomic analysis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antigen presentation to cytotoxic T lymphocytes via major histocompatibility complex class I (MHC I) molecules depends on the heterodimeric transporter associated with antigen processing (TAP). For efficient antigen supply to MHC I molecules in the ER, TAP assembles a macromolecular peptide-loading complex (PLC) by recruiting tapasin. In evolution, TAP appeared together with effector cells of adaptive immunity at the transition from jawless to jawed vertebrates and diversified further within the jawed vertebrates. Here, we compared TAP function and interaction with tapasin of a range of species within two classes of jawed vertebrates. We found that avian and mammalian TAP1 and TAP2 form heterodimeric complexes across taxa. Moreover, the extra N-terminal domain TMD0 of mammalian TAP1 and TAP2 as well as avian TAP2 recruits tapasin. Strikingly, however, only TAP1 and TAP2 from the same taxon can form a functional heterodimeric translocation complex. These data demonstrate that the dimerization interface between TAP1 and TAP2 and the tapasin docking sites for PLC assembly are conserved in evolution, whereas elements of antigen translocation diverged later in evolution and are thus taxon specific.
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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.