{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Ms. Mizuki Ishida"],"funding":["MEXT | Japan Society for the Promotion of Science (JSPS)","Ministry of Health, Labour and Welfare (MHLW)","Mizutani Foundation for Glycoscience (MFG)","KOSE Cosmetology Research Foundation","Japan Agency for Medical Research and Development (AMED)"],"journal":["EMBO Reports"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-SCDT-EMBOR-2021-54352V1"],"abstract":["Glycosylphosphatidylinositols (GPIs) are glycolipids that anchor many proteins (GPI-APs) on the cell surface. The core glycan of GPI precursor has three mannoses, which in mammals, are all modified by ethanolamine-phosphate (EthN-P). It is postulated that EthN-P on the third mannose (EthN-P-Man3) is the bridge between GPI and the protein and the second (EthN-P-Man2) is removed after GPI-protein attachment. However, EthN-P-Man2 may not be always transient, as mutations of PIGG, the enzyme that transfers EthN-P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN-P on Man2 is the preferential bridge in some GPI-APs, among them, the Ect-5'-nucleotidase and Netrin G2. We find that CD59, a GPI-AP, is attached via EthN-P-Man2 both "],"repository":["biostudies-other"],"funding_grant_id":["JP21H02415","21ek0109418h0003","JP17H06422"],"pubmed_authors":["Ms. Yoko Takada","Dr. Yoshiko Murakami","Dr. Philippe, M Campeau","Ms. Mizuki Ishida","Mr. Akinori Ninomiya","Dr. Yuta Maki","Dr. Taroh Kinoshita"],"additional_accession":[]},"is_claimable":false,"name":"Ethanolamine-phosphate on the second mannose is a preferential bridge for some GPI-anchored proteins","description":"Glycosylphosphatidylinositols (GPIs) are glycolipids that anchor many proteins (GPI-APs) on the cell surface. The core glycan of GPI precursor has three mannoses, which in mammals, are all modified by ethanolamine-phosphate (EthN-P). It is postulated that EthN-P on the third mannose (EthN-P-Man3) is the bridge between GPI and the protein and the second (EthN-P-Man2) is removed after GPI-protein attachment. However, EthN-P-Man2 may not be always transient, as mutations of PIGG, the enzyme that transfers EthN-P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN-P on Man2 is the preferential bridge in some GPI-APs, among them, the Ect-5'-nucleotidase and Netrin G2. We find that CD59, a GPI-AP, is attached via EthN-P-Man2 both ","dates":{"release":"2022-07-18T00:00:00Z","modification":"2022-07-18T15:53:17.951Z","creation":"2022-07-18T15:53:17.951Z"},"accession":"S-SCDT-EMBOR-2021-54352V1","cross_references":{"doi":["10.15252/embr.202154352"]}}