{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brunnberg J"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","Deutsche Forschungsgemeinschaft","European Research Council"],"pagination":["e2321600121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11145271"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(22)"],"pubmed_abstract":["Antigen presentation via major histocompatibility complex class I (MHC-I) molecules is essential for surveillance by the adaptive immune system. Central to this process is the peptide-loading complex (PLC), which translocates peptides from the cytosol to the endoplasmic reticulum and catalyzes peptide loading and proofreading of peptide-MHC-I (pMHC-I) complexes. Despite its importance, the impact of individual PLC components on the presented pMHC-I complexes is still insufficiently understood. Here, we used stoichiometrically defined antibody-nanobody complexes and engineered soluble T cell receptors (sTCRs) to quantify different MHC-I allomorphs and defined pMHC-I complexes, respectively. Thereby, we uncovered distinct effects of individual PLC components on the pMHC-I surface pool. Knock"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Dual role of the peptide-loading complex as proofreader and limiter of MHC-I presentation."],"pmcid":["PMC11145271"],"funding_grant_id":["CRC 1507","TA 157/12-1","798121"],"pubmed_authors":["Tampe R","Winter C","de Wet B","Battin C","Brunnberg J","Fruhschulz S","Cole DK","Steinberger P","Barends M"],"additional_accession":[]},"is_claimable":false,"name":"Dual role of the peptide-loading complex as proofreader and limiter of MHC-I presentation.","description":"Antigen presentation via major histocompatibility complex class I (MHC-I) molecules is essential for surveillance by the adaptive immune system. Central to this process is the peptide-loading complex (PLC), which translocates peptides from the cytosol to the endoplasmic reticulum and catalyzes peptide loading and proofreading of peptide-MHC-I (pMHC-I) complexes. Despite its importance, the impact of individual PLC components on the presented pMHC-I complexes is still insufficiently understood. Here, we used stoichiometrically defined antibody-nanobody complexes and engineered soluble T cell receptors (sTCRs) to quantify different MHC-I allomorphs and defined pMHC-I complexes, respectively. Thereby, we uncovered distinct effects of individual PLC components on the pMHC-I surface pool. Knock","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-04-08T19:52:07.463Z","creation":"2026-04-08T14:33:48.608Z"},"accession":"S-EPMC11145271","cross_references":{"pubmed":["38771881"],"doi":["10.1073/pnas.2321600121"]}}