{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T07:16:17Z","timestamp":1790752577401,"version":"4.1.0"},"reference-count":37,"publisher":"American Society for Cell Biology (ASCB)","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2005,11]]},"abstract":"<jats:p>Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by an unusually complex GPI-N-acetylglucosaminyltransferase (GPI-GnT) consisting of at least six proteins. Here, we report that human GPI-GnT requires another component, termed PIG-Y, a 71 amino acid protein with two transmembrane domains. The Burkitt lymphoma cell line Daudi, severely defective in the surface expression of GPI-anchored proteins, was a null mutant of PIG-Y. A complex of six components was formed without PIG-Y. PIG-Y appeared to be directly associated with PIG-A, implying that PIG-Y is the key molecule that regulates GPI-GnT activity by binding directly to the catalytic subunit PIG-A. PIG-Y is probably homologous to yeast Eri1p, a component of GPI-GnT. We did not obtain evidence for a functional linkage between GPI-GnT and ras GTPases in mammalian cells as has been reported for yeast cells. A single transcript encoded PIG-Y and, to its 5\u2032 side, another protein PreY that has homologues in a wide range of organisms and is characterized by a conserved domain termed DUF343. These two proteins are translated from one mRNA by leaky scanning of the PreY initiation site.<\/jats:p>","DOI":"10.1091\/mbc.e05-08-0743","type":"journal-article","created":{"date-parts":[[2005,9,15]],"date-time":"2005-09-15T00:33:27Z","timestamp":1126744407000},"page":"5236-5246","source":"Crossref","is-referenced-by-count":64,"title":["The Initial Enzyme for Glycosylphosphatidylinositol Biosynthesis Requires PIG-Y, a Seventh Component"],"prefix":"10.1091","volume":"16","author":[{"given":"Yoshiko","family":"Murakami","sequence":"first","affiliation":[{"name":"Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Uamporn","family":"Siripanyaphinyo","sequence":"additional","affiliation":[{"name":"Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yeongjin","family":"Hong","sequence":"additional","affiliation":[{"name":"Genomic Research Center for Enteropathogenic Bacteria and Department of Microbiology, Chonnam National University Medical School, Gwangju 501-746, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuko","family":"Tashima","sequence":"additional","affiliation":[{"name":"Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yusuke","family":"Maeda","sequence":"additional","affiliation":[{"name":"Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taroh","family":"Kinoshita","sequence":"additional","affiliation":[{"name":"Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1076","reference":[{"key":"REF1","doi-asserted-by":"crossref","unstructured":"Bateman, A.et al.(2004). 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Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels.J. Biol. Chem.279, 35313\u201335319.","DOI":"10.1074\/jbc.M404133200"},{"key":"REF21","doi-asserted-by":"crossref","unstructured":"McConville, M. J., and Menon, A. K. (2000). Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids.Mol. Membr. Biol.17, 1\u201316.","DOI":"10.1080\/096876800294443"},{"key":"REF22","doi-asserted-by":"crossref","unstructured":"Morelon, E., Dodelet, V., Lavery, P., Cashman, N. R., and Loertscher, R. (2001). The failure of Daudi cells to express the cellular prion protein is caused by a lack of glycosyl-phosphatidylinositol anchor formation.Immunology102, 242\u2013247.","DOI":"10.1046\/j.1365-2567.2001.01166.x"},{"key":"REF23","unstructured":"Nozaki, M., Ohishi, K., Yamada, N., Kinoshita, T., Nagy, A., and Takeda, J. (1999). Developmental abnormalities of glycosylphosphatidylinositol-anchor-deficient embryos revealed by Cre\/loxP system.Lab. Invest.79, 293\u2013299."},{"key":"REF24","doi-asserted-by":"crossref","unstructured":"Ohba, Y., Mochizuki, N., Matsuo, K., Yamashita, S., Nakaya, M., Hashimoto, Y., Hamaguchi, M., Kurata, T., Nagashima, K., and Matsuda, M. (2000). Rap2 as a slowly responding molecular switch in the Rap1 signaling cascade.Mol. Cell. Biol.20, 6074\u20136083.","DOI":"10.1128\/MCB.20.16.6074-6083.2000"},{"key":"REF25","doi-asserted-by":"crossref","unstructured":"Simons, K., and Toomre, D. (2000). Lipid rafts and signal transduction.Nat. Rev. Mol. Cell. Biol.1, 31\u201339.","DOI":"10.1038\/35036052"},{"key":"REF26","doi-asserted-by":"crossref","unstructured":"Sobering, A. K., Romeo, M. J., Vay, H. A., and Levin, D. E. (2003). A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum.Mol. Cell. 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Cellular internal ribosome entry segments: structures, trans-acting factors and regulation of gene expression.Oncogene23, 3200\u20133207.","DOI":"10.1038\/sj.onc.1207551"},{"key":"REF30","doi-asserted-by":"crossref","unstructured":"Takeda, J., Miyata, T., Kawagoe, K., Iida, Y., Endo, Y., Fujita, T., Takahashi, M., Kitani, T., and Kinoshita, T. (1993). Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria.Cell73, 703\u2013711.","DOI":"10.1016\/0092-8674(93)90250-T"},{"key":"REF31","doi-asserted-by":"crossref","unstructured":"Tarutani, M., Itami, S., Okabe, M., Ikawa, M., Tezuka, T., Yoshikawa, K., Kinoshita, T., and Takeda, J. (1997). Tissue specific knock-out of the mouse Pig-a gene reveals important roles for GPI-anchored proteins in skin development.Proc. Natl. Acad. Sci. USA94, 7400\u20137405.","DOI":"10.1073\/pnas.94.14.7400"},{"key":"REF32","doi-asserted-by":"crossref","unstructured":"Tiede, A., Bastisch, I., Schubert, J., Orlean, P., and Schmidt, R. E. (1999). Biosynthesis of glycosylphosphatidylinositols in mammalian and unicellular microbes.Biol. Chem.380, 503\u2013523.","DOI":"10.1515\/BC.1999.066"},{"key":"REF33","doi-asserted-by":"crossref","unstructured":"Toda, T., Uno, I., Ishikawa, T., Powers, S., Kataoka, T., Broek, D., Cameron, S., Broach, J., Matsumoto, K., and Wigler, M. (1985). In yeast, RAS proteins are controlling elements of adenylate cyclase.Cell40, 27\u201336.","DOI":"10.1016\/0092-8674(85)90305-8"},{"key":"REF34","doi-asserted-by":"crossref","unstructured":"Toh-e, A., and Oguchi, T. (2001). Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance inSaccharomyces cerevisiae.Genes Genet. Syst.76, 393\u2013410.","DOI":"10.1266\/ggs.76.393"},{"key":"REF35","doi-asserted-by":"crossref","unstructured":"Vagner, S., Galy, B., and Pyronnet, S. (2001). Irresistible IRES. Attracting the translation machinery to internal ribosome entry sites.EMBO Rep.2, 893\u2013898.","DOI":"10.1093\/embo-reports\/kve208"},{"key":"REF36","doi-asserted-by":"crossref","unstructured":"Watanabe, R., Inoue, N., Westfall, B., Taron, C. H., Orlean, P., Takeda, J., and Kinoshita, T. (1998). The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.EMBO J.17, 877\u2013885.","DOI":"10.1093\/emboj\/17.4.877"},{"key":"REF37","doi-asserted-by":"crossref","unstructured":"Watanabe, R., Murakami, Y., Marmor, M. D., Inoue, N., Maeda, Y., Hino, J., Kangawa, K., Julius, M., and Kinoshita, T. (2000). Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2.EMBO J.19, 4402\u20134411.","DOI":"10.1093\/emboj\/19.16.4402"}],"container-title":["Molecular Biology of the Cell"],"original-title":[],"language":"en","deposited":{"date-parts":[[2023,5,4]],"date-time":"2023-05-04T13:56:11Z","timestamp":1683208571000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.molbiolcell.org\/doi\/10.1091\/mbc.e05-08-0743"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,11]]},"references-count":37,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2005,11]]}},"alternative-id":["10.1091\/mbc.e05-08-0743"],"URL":"https:\/\/doi.org\/10.1091\/mbc.e05-08-0743","relation":{},"ISSN":["1059-1524","1939-4586"],"issn-type":[{"value":"1059-1524","type":"print"},{"value":"1939-4586","type":"electronic"}],"subject":[],"published":{"date-parts":[[2005,11]]}}}