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http://purl.uniprot.org/citations/10944123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10944123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10944123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/10944123http://www.w3.org/2000/01/rdf-schema#comment"Glycosylphosphatidylinositols (GPIs) are attached to the C-termini of many proteins, thereby acting as membrane anchors. Biosynthesis of GPI is initiated by GPI-N-acetylglucosaminyltransferase (GPI-GnT), which transfers N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol. GPI-GnT is a uniquely complex glycosyltransferase, consisting of at least four proteins, PIG-A, PIG-H, PIG-C and GPI1. Here, we report that GPI-GnT requires another component, termed PIG-P, and that DPM2, which regulates dolichol-phosphate-mannose synthase, also regulates GPI-GnT. PIG-P, a 134-amino acid protein having two hydrophobic domains, associates with PIG-A and GPI1. PIG-P is essential for GPI-GnT since a cell lacking PIG-P is GPI-anchor negative. DPM2, but not two other components of dolichol-phosphate-mannose synthase, associates with GPI-GnT through interactions with PIG-A, PIG-C and GPI1. Lec15 cell, a null mutant of DPM2, synthesizes early GPI intermediates, indicating that DPM2 is not essential for GPI-GnT; however, the enzyme activity is enhanced 3-fold in the presence of DPM2. These results reveal new essential and regulatory components of GPI-GnT and imply co-regulation of GPI-GnT and the dolichol-phosphate-mannose synthase that generates a mannosyl donor for GPI."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.16.4402"xsd:string
http://purl.uniprot.org/citations/10944123http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.16.4402"xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Inoue N."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Inoue N."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Watanabe R."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Watanabe R."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Kangawa K."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Kangawa K."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Hino J."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Hino J."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Julius M."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Julius M."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Marmor M.D."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/author"Marmor M.D."xsd:string
http://purl.uniprot.org/citations/10944123http://purl.uniprot.org/core/date"2000"xsd:gYear