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http://purl.uniprot.org/citations/22158438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22158438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22158438http://www.w3.org/2000/01/rdf-schema#comment"The O-linked-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates basic cellular functions and is involved in the aetiology of diabetes and neurodegeneration. This intracellular O-GlcNAcylation is catalyzed by a single O-GlcNAc transferase, OGT. Here we report a novel OGT, EOGT, responsible for extracellular O-GlcNAcylation. Although both OGT and EOGT are regulated by hexosamine flux, EOGT localizes to the lumen of the endoplasmic reticulum and transfers GlcNAc to epidermal growth factor-like domains in an OGT-independent manner. Loss of Eogt gives phenotypes similar to those caused by defects in the apical extracellular matrix. Dumpy (Dp), a membrane-anchored extracellular protein, is O-GlcNAcylated, and EOGT is required for Dp-dependent epithelial cell-matrix interactions. Thus, O-GlcNAcylation of secreted and membrane glycoproteins is a novel mediator of cell-cell or cell-matrix interactions at the cell surface."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.org/dc/terms/identifier"doi:10.1038/ncomms1591"xsd:string
http://purl.uniprot.org/citations/22158438http://purl.org/dc/terms/identifier"doi:10.1038/ncomms1591"xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Ito M."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Ito M."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Murakami K."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Murakami K."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Furukawa K."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Furukawa K."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Nadano D."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Nadano D."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Nomura T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Nomura T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Suzuki E."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Suzuki E."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Okajima T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Okajima T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Matsuda T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Matsuda T."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Matsuura A."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Matsuura A."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Sakaidani Y."xsd:string
http://purl.uniprot.org/citations/22158438http://purl.uniprot.org/core/author"Sakaidani Y."xsd:string