{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ma M"],"funding":["NICHD NIH HHS","Medical Research Council","NIGMS NIH HHS"],"pagination":["667-672"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617332"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["386(6722)"],"pubmed_abstract":["One-fifth of human proteins are N-glycosylated in the endoplasmic reticulum (ER) by two oligosaccharyltransferases, OST-A and OST-B. Contrary to the prevailing view of N-glycosylation as a housekeeping function, we identified an ER pathway that modulates the activity of OST-A. Genetic analyses linked OST-A to HSP90B1, an ER chaperone for membrane receptors, and CCDC134, an ER luminal protein. During its translocation into the ER, an N-terminal peptide in HSP90B1 templates the assembly of a translocon complex containing CCDC134 and OST-A that protects HSP90B1 during folding, preventing its hyperglycosylation and degradation. Disruption of this pathway impairs WNT and IGF1R signaling and causes the bone developmental disorder osteogenesis imperfecta. Thus, N-glycosylation can be regulated by"],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Regulated N-glycosylation controls chaperone function and receptor trafficking."],"pmcid":["PMC7617332"],"funding_grant_id":["R35 GM118082","MC_UP_1201/32","P41 GM108538","R21 HD101980","R01 HD113790"],"pubmed_authors":["Overmyer KA","Singal B","Fedry J","Dubey R","Cormier-Daire V","Ma M","Jen A","Shishkova E","Aravind L","Pusapati GV","Rohatgi R","Coon JJ"],"additional_accession":[]},"is_claimable":false,"name":"Regulated N-glycosylation controls chaperone function and receptor trafficking.","description":"One-fifth of human proteins are N-glycosylated in the endoplasmic reticulum (ER) by two oligosaccharyltransferases, OST-A and OST-B. Contrary to the prevailing view of N-glycosylation as a housekeeping function, we identified an ER pathway that modulates the activity of OST-A. Genetic analyses linked OST-A to HSP90B1, an ER chaperone for membrane receptors, and CCDC134, an ER luminal protein. During its translocation into the ER, an N-terminal peptide in HSP90B1 templates the assembly of a translocon complex containing CCDC134 and OST-A that protects HSP90B1 during folding, preventing its hyperglycosylation and degradation. Disruption of this pathway impairs WNT and IGF1R signaling and causes the bone developmental disorder osteogenesis imperfecta. Thus, N-glycosylation can be regulated by","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2025-04-04T02:23:21.151Z","creation":"2025-04-04T02:23:21.151Z"},"accession":"S-EPMC7617332","cross_references":{"pubmed":["39509507"],"doi":["10.1126/science.adp7201"]}}