{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McWilliam HEG"],"funding":["NIAID NIH HHS","Department of Health | National Health and Medical Research Council","Australian Research Council"],"pagination":["24974-24985"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7547156"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(40)"],"pubmed_abstract":["The antigen-presenting molecule MR1 (MHC class I-related protein 1) presents metabolite antigens derived from microbial vitamin B<sub>2</sub> synthesis to activate mucosal-associated invariant T (MAIT) cells. Key aspects of this evolutionarily conserved pathway remain uncharacterized, including where MR1 acquires ligands and what accessory proteins assist ligand binding. We answer these questions by using a fluorophore-labeled stable MR1 antigen analog, a conformation-specific MR1 mAb, proteomic analysis, and a genome-wide CRISPR/Cas9 library screen. We show that the endoplasmic reticulum (ER) contains a pool of two unliganded MR1 conformers stabilized via interactions with chaperones tapasin and tapasin-related protein. This pool is the primary source of MR1 molecules for the presentation"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Endoplasmic reticulum chaperones stabilize ligand-receptive MR1 molecules for efficient presentation of metabolite antigens."],"pmcid":["PMC7547156"],"funding_grant_id":["1113293","DE170100575","1058193","R01 AI148407","FT160100083","CE140100011","170102471","DE170100407","1117017"],"pubmed_authors":["Liu H","Villadangos JA","McWilliam HEG","Reddiex SJJ","Liu L","Mak JYW","Rossjohn J","Yan Y","Wormald S","McCluskey J","Fairlie DP","Li S","Mintern JD","Awad W","Eckle SBG","Dagley LF","Zorkau M","Cruz-Gomez S","Lim HJ","Corbett AJ"],"additional_accession":[]},"is_claimable":false,"name":"Endoplasmic reticulum chaperones stabilize ligand-receptive MR1 molecules for efficient presentation of metabolite antigens.","description":"The antigen-presenting molecule MR1 (MHC class I-related protein 1) presents metabolite antigens derived from microbial vitamin B<sub>2</sub> synthesis to activate mucosal-associated invariant T (MAIT) cells. Key aspects of this evolutionarily conserved pathway remain uncharacterized, including where MR1 acquires ligands and what accessory proteins assist ligand binding. We answer these questions by using a fluorophore-labeled stable MR1 antigen analog, a conformation-specific MR1 mAb, proteomic analysis, and a genome-wide CRISPR/Cas9 library screen. We show that the endoplasmic reticulum (ER) contains a pool of two unliganded MR1 conformers stabilized via interactions with chaperones tapasin and tapasin-related protein. This pool is the primary source of MR1 molecules for the presentation","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-05-01T17:34:40.631Z","creation":"2025-04-06T07:58:49.28Z"},"accession":"S-EPMC7547156","cross_references":{"pubmed":["32958637"],"doi":["10.1073/pnas.2011260117"]}}