ArticleScientific reports2015
Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- 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
- Structurally diverse viral inhibitors converge on a shared mechanism to stall the antigen transporter TAP.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing.Immunity · 2025Article
- A Structural Atlas of TAP Inhibition by Herpesviruses and Poxviruses.bioRxiv : the preprint server for biology · 2025Article
- Tapasin assembly surveillance by the RNF185/Membralin ubiquitin ligase complex regulates MHC-I surface expression.Nature communications · 2024Article
- Harnessing antibody-mediated recognition of the intracellular proteome with T cell receptor-like specificity.Frontiers in immunology · 2024Review
- The Intracellular Proteome as a Source for Novel Targets in CAR-T and T-Cell Engagers-Based Immunotherapy.Cells · 2022Review
- Proteomics research of SARS-CoV-2 and COVID-19 disease.Medical review (2021) · 2022Review
- TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap.Nature communications · 2021Article
- Light control of the peptide-loading complex synchronizes antigen translocation and MHC I trafficking.Communications biology · 2021Article
- Atomistic structure and dynamics of the human MHC-I peptide-loading complex.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lysosomal targeting of the ABC transporter TAPL is determined by membrane-localized charged residues.The Journal of biological chemistry · 2019Article
- Structural and functional insights into the interaction and targeting hub TMD0 of the polypeptide transporter TAPL.Scientific reports · 2018Article
- Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018Review
- ABCB6, an ABC Transporter Impacting Drug Response and Disease.The AAPS journal · 2017Review
- 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
- Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.Frontiers in immunology · 2017Review
- Structure and Dynamics of Antigenic Peptides in Complex with TAP.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Salt bridges in lipid bilayers play a decisive role in the dynamic assembly and downstream signaling of the natural killer and T-cell receptors. Here, we describe the identification of an inter-subunit salt bridge in the membrane within yet another key component of the immune system, the peptide-loading complex (PLC). The PLC regulates cell surface presentation of self-antigens and antigenic peptides via molecules of the major histocompatibility complex class I. We demonstrate that a single salt bridge in the membrane between the transporter associated with antigen processing TAP and the MHC I-specific chaperone tapasin is essential for the assembly of the PLC and for efficient MHC I antigen presentation. Molecular modeling and all-atom molecular dynamics simulations suggest an ionic lock-switch mechanism for the binding of TAP to tapasin, in which an unfavorable uncompensated charge in the ER-membrane is prevented through complex formation. Our findings not only deepen the understanding of the interaction network within the PLC, but also provide evidence for a general interaction principle of dynamic multiprotein membrane complexes in immunity.
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