{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Williams RV"],"funding":["HHS | National Institutes of Health","ODCDC CDC HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["e2202992119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9618145"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(43)"],"pubmed_abstract":["<i>N</i>-glycosylation is a common posttranslational modification of secreted proteins in eukaryotes. This modification targets asparagine residues within the consensus sequence, N-X-S/T. While this sequence is required for glycosylation, the initial transfer of a high-mannose glycan by oligosaccharyl transferases A or B (OST-A or OST-B) can lead to incomplete occupancy at a given site. Factors that determine the extent of transfer are not well understood, and understanding them may provide insight into the function of these important enzymes. Here, we use mass spectrometry (MS) to simultaneously measure relative occupancies for three <i>N</i>-glycosylation sites on the N-terminal IgV domain of the recombinant glycoprotein, hCEACAM1. We demonstrate that addition is primarily by the OST-B e"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV."],"pmcid":["PMC9618145"],"funding_grant_id":["S10 OD025118","R35 GM131829","R01 GM033225"],"pubmed_authors":["Huang C","Ahmed T","Amster IJ","Prestegard JH","Williams RV","Moremen KW","Columbus L","McDermott C"],"additional_accession":[]},"is_claimable":false,"name":"Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV.","description":"<i>N</i>-glycosylation is a common posttranslational modification of secreted proteins in eukaryotes. This modification targets asparagine residues within the consensus sequence, N-X-S/T. While this sequence is required for glycosylation, the initial transfer of a high-mannose glycan by oligosaccharyl transferases A or B (OST-A or OST-B) can lead to incomplete occupancy at a given site. Factors that determine the extent of transfer are not well understood, and understanding them may provide insight into the function of these important enzymes. Here, we use mass spectrometry (MS) to simultaneously measure relative occupancies for three <i>N</i>-glycosylation sites on the N-terminal IgV domain of the recombinant glycoprotein, hCEACAM1. We demonstrate that addition is primarily by the OST-B e","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-27T21:06:17.615Z","creation":"2025-04-25T17:11:29.451Z"},"accession":"S-EPMC9618145","cross_references":{"pubmed":["36251991"],"doi":["10.1073/pnas.2202992119"]}}