{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Takeuchi H"],"funding":["HHS | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["E8395-E8402"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6130362"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["115(36)"],"pubmed_abstract":["The Notch-signaling pathway is normally activated by Notch-ligand interactions. A recent structural analysis suggested that a novel <i>O</i>-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands. This serine occurs between conserved cysteines 3 and 4 of Epidermal Growth Factor-like (EGF) repeat 11 of NOTCH1, a site distinct from those modified by protein <i>O</i>-glucosyltransferase 1 (POGLUT1), suggesting that a different enzyme is responsible. Here, we identify two novel protein <i>O</i>-glucosyltransferases, POGLUT2 and POGLUT3 (formerly KDELC1 and KDELC2, respectively), which transfer <i>O</i>-glucose (<i>O</i>-Glc) from UDP-Glc to serine 435. Mass spectrometric analysis of NOTCH1 produced in HEK293T cells lac"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Two novel protein <i>O</i>-glucosyltransferases that modify sites distinct from POGLUT1 and affect Notch trafficking and signaling."],"pmcid":["PMC6130362"],"funding_grant_id":["T32 GM107004","GM061126","R01 GM061126"],"pubmed_authors":["Takeuchi M","Haltiwanger RS","Schneider M","Handford PA","Takeuchi H","Williamson DB","Ito A"],"additional_accession":[]},"is_claimable":false,"name":"Two novel protein <i>O</i>-glucosyltransferases that modify sites distinct from POGLUT1 and affect Notch trafficking and signaling.","description":"The Notch-signaling pathway is normally activated by Notch-ligand interactions. A recent structural analysis suggested that a novel <i>O</i>-linked hexose modification on serine 435 of the mammalian NOTCH1 core ligand-binding domain lies at the interface with its ligands. This serine occurs between conserved cysteines 3 and 4 of Epidermal Growth Factor-like (EGF) repeat 11 of NOTCH1, a site distinct from those modified by protein <i>O</i>-glucosyltransferase 1 (POGLUT1), suggesting that a different enzyme is responsible. Here, we identify two novel protein <i>O</i>-glucosyltransferases, POGLUT2 and POGLUT3 (formerly KDELC1 and KDELC2, respectively), which transfer <i>O</i>-glucose (<i>O</i>-Glc) from UDP-Glc to serine 435. Mass spectrometric analysis of NOTCH1 produced in HEK293T cells lac","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Sep","modification":"2026-06-10T05:41:06.262Z","creation":"2019-08-04T08:13:26Z"},"accession":"S-EPMC6130362","cross_references":{"pubmed":["30127001"],"doi":["10.1073/pnas.1804005115"]}}