{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shrimal S"],"funding":["NIGMS NIH HHS"],"pagination":["81-95"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3613688"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["201(1)"],"pubmed_abstract":["Metazoan organisms assemble two isoforms of the oligosaccharyltransferase (OST) that have different catalytic subunits (STT3A or STT3B) and partially nonoverlapping roles in asparagine-linked glycosylation. The STT3A isoform of the OST is primarily responsible for co-translational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum. The C-terminal 65-75 residues of a glycoprotein will not contact the translocation channel-associated STT3A isoform of the OST complex before chain termination. Biosynthetic pulse labeling of five human glycoproteins showed that extreme C-terminal glycosylation sites were modified by an STT3B-dependent posttranslocational mechanism. The boundary for STT3B-dependent glycosylation of C-terminal sites was determined to fall"],"journal":["The Journal of cell biology"],"pubmed_title":["Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST."],"pmcid":["PMC3613688"],"funding_grant_id":["GM43687","R01 GM043768"],"pubmed_authors":["Shrimal S","Gilmore R","Trueman SF"],"additional_accession":[]},"is_claimable":false,"name":"Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST.","description":"Metazoan organisms assemble two isoforms of the oligosaccharyltransferase (OST) that have different catalytic subunits (STT3A or STT3B) and partially nonoverlapping roles in asparagine-linked glycosylation. The STT3A isoform of the OST is primarily responsible for co-translational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum. The C-terminal 65-75 residues of a glycoprotein will not contact the translocation channel-associated STT3A isoform of the OST complex before chain termination. Biosynthetic pulse labeling of five human glycoproteins showed that extreme C-terminal glycosylation sites were modified by an STT3B-dependent posttranslocational mechanism. The boundary for STT3B-dependent glycosylation of C-terminal sites was determined to fall","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Apr","modification":"2026-05-04T04:07:20.71Z","creation":"2019-03-27T01:06:48Z"},"accession":"S-EPMC3613688","cross_references":{"pubmed":["23530066"],"doi":["10.1083/jcb.201301031"]}}