ArticleCellular and molecular life sciences : CMLS2012
Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complex.
Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.Science advances · 2026Article
- The potential applications of peptide-loading complex in cancer treatment.Frontiers in immunology · 2025Review
- Structure of an MHC I-tapasin-ERp57 editing complex defines chaperone promiscuity.Nature communications · 2022Article
- Offense and Defense in Granulomatous Inflammation Disease.Frontiers in cellular and infection microbiology · 2022Review
- Current Insights in Genetics of Sarcoidosis: Functional and Clinical Impacts.Journal of clinical medicine · 2020Review
- Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018Review
- Structure of the transporter associated with antigen processing trapped by herpes simplex virus.eLife · 2016Article
- Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.Scientific reports · 2015Article
- Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver?Cellular & molecular immunology · 2015Review
- A negative feedback modulator of antigen processing evolved from a frameshift in the cowpox virus genome.PLoS pathogens · 2014Article
- Assembly and function of the major histocompatibility complex (MHC) I peptide-loading complex are conserved across higher vertebrates.The Journal of biological chemistry · 2014Article
- An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing).The Journal of biological chemistry · 2014Article
- Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter.Nature communications · 2014Article
- Three tapasin docking sites in TAP cooperate to facilitate transporter stabilization and heterodimerization.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The loading of antigenic peptides onto major histocompatibility complex class I (MHC I) molecules is an essential step in the adaptive immune response against virally or malignantly transformed cells. The ER-resident peptide-loading complex (PLC) consists of the transporter associated with antigen processing (TAP1 and TAP2), assembled with the auxiliary factors tapasin and MHC I. Here, we demonstrated that the N-terminal extension of each TAP subunit represents an autonomous domain, named TMD(0), which is correctly targeted to and inserted into the ER membrane. In the absence of coreTAP, each TMD(0) recruits tapasin in a 1:1 stoichiometry. Although the TMD(0)s lack known ER retention/retrieval signals, they are localized to the ER membrane even in tapasin-deficient cells. We conclude that the TMD(0)s of TAP form autonomous interaction hubs linking antigen translocation into the ER with peptide loading onto MHC I, hence ensuring a major function in the integrity of the antigen-processing machinery.
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