메뉴 건너뛰기




Volumn 16, Issue 11, 2005, Pages 5236-5246

The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCOSYLPHOSPHATIDYLINOSITOL; GPI ANCHORED PROTEIN; MESSENGER RNA; N ACETYLGLUCOSAMINYLTRANSFERASE; PROTEIN; PROTEIN PIG Y; UNCLASSIFIED DRUG;

EID: 27644514673     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-08-0743     Document Type: Article
Times cited : (54)

References (37)
  • 1
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman, A. et al (2004). The Pfam protein families database. Nucleic Acids Res. 32, D138-D141.
    • (2004) Nucleic Acids Res. , vol.32
    • Bateman, A.1
  • 2
    • 0035175540 scopus 로고    scopus 로고
    • Control of pseudohyphae formation in Saccharomyces cerevisiae
    • Gancedo, J. M. (2001). Control of pseudohyphae formation in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 25, 107-123.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 107-123
    • Gancedo, J.M.1
  • 3
    • 0033009538 scopus 로고    scopus 로고
    • The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae
    • Heinisch, J. J., Lorberg, A., Schmitz, H. P., and Jacoby, J. J. (1999). The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae. Mol. Microbiol. 32, 671-680.
    • (1999) Mol. Microbiol. , vol.32 , pp. 671-680
    • Heinisch, J.J.1    Lorberg, A.2    Schmitz, H.P.3    Jacoby, J.J.4
  • 4
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K., and Stoffel, W. (1993). TMbase-a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 347, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 5
    • 0024264015 scopus 로고
    • Biosynthesis and function of LFA-3 in human mutant cells deficient in phosphatidylinositol-anchored proteins
    • Hollander, N., Selvaraj, P., and Springer, T. A. (1988). Biosynthesis and function of LFA-3 in human mutant cells deficient in phosphatidylinositol- anchored proteins. J. Immunol. 141, 4283-4290.
    • (1988) J. Immunol. , vol.141 , pp. 4283-4290
    • Hollander, N.1    Selvaraj, P.2    Springer, T.A.3
  • 6
    • 0033603587 scopus 로고    scopus 로고
    • GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis
    • Hong, Y., Ohishi, K., Watanabe, R., Endo, Y., Maeda, Y., and Kinoshita, T. (1999). GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis. J. Biol. Chem. 274, 18582-18588.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18582-18588
    • Hong, Y.1    Ohishi, K.2    Watanabe, R.3    Endo, Y.4    Maeda, Y.5    Kinoshita, T.6
  • 7
    • 0036547672 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol (GPI)-anchored proteins
    • Ikezawa, H. (2002). Glycosylphosphatidylinositol (GPI)-anchored proteins. Biol. Pharm. Bull. 25, 409-417.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 409-417
    • Ikezawa, H.1
  • 9
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang, S. K., Krausslich, H. G., Nicklin, M. J., Duke, G. M., Palmenberg, A. C., and Wimmer, E. (1988). A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62, 2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 10
    • 0033637430 scopus 로고    scopus 로고
    • Dissecting and manipulating the pathway for glycosylphosphatidylinositol- anchor biosynthesis
    • Kinoshita, T., and Inoue, N. (2000). Dissecting and manipulating the pathway for glycosylphosphatidylinositol-anchor biosynthesis. Curr. Opin. Chem. Biol. 4, 632-638.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 632-638
    • Kinoshita, T.1    Inoue, N.2
  • 11
    • 0028802581 scopus 로고
    • Defectiveglycosylphosphatidylinositol anchor synthesis and paroxysmal nocturnal hemoglobinuria
    • Kinoshita, T., Inoue, N., and Takeda, J. (1995). Defectiveglycosylphosphatidylinositol anchor synthesis and paroxysmal nocturnal hemoglobinuria. Adv. Immunol. 60, 57-103.
    • (1995) Adv. Immunol. , vol.60 , pp. 57-103
    • Kinoshita, T.1    Inoue, N.2    Takeda, J.3
  • 12
    • 0030882053 scopus 로고    scopus 로고
    • GPI-anchor synthesis in mammalian cells: Genes, their products, and a deficiency
    • Kinoshita, T., Ohishi, K., and Takeda, J. (1997). GPI-anchor synthesis in mammalian cells: genes, their products, and a deficiency. J. Biochem. 122, 251-257.
    • (1997) J. Biochem. , vol.122 , pp. 251-257
    • Kinoshita, T.1    Ohishi, K.2    Takeda, J.3
  • 13
    • 0034664959 scopus 로고    scopus 로고
    • 3-(4-azidoanilido)uridine 5′-triphosphate identifies Gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis
    • 3-(4-azidoanilido)uridine 5′-triphosphate identifies Gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis. Biochem. J. 350, 815-822.
    • (2000) Biochem. J. , vol.350 , pp. 815-822
    • Kostova, Z.1    Rancour, D.M.2    Menon, A.K.3    Orlean, P.4
  • 14
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M. (1987). An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15, 8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 15
    • 0037121050 scopus 로고    scopus 로고
    • Pushing the limits of the scanning mechanism for initiation of translation
    • Kozak, M. (2002). Pushing the limits of the scanning mechanism for initiation of translation. Gene 299, 1-34.
    • (2002) Gene , vol.299 , pp. 1-34
    • Kozak, M.1
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0028361106 scopus 로고
    • A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis
    • Leidich, S. D., Drapp, D. A., and Orlean, P. (1994). A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis. J. Biol. Chem. 269, 10193-10196.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10193-10196
    • Leidich, S.D.1    Drapp, D.A.2    Orlean, P.3
  • 18
    • 0032168288 scopus 로고    scopus 로고
    • DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: Correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate
    • Maeda, Y., Tomita, S., Watanabe, R., Ohishi, K., and Kinoshita, T. (1998). DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate. EMBO J. 17, 4920-4929.
    • (1998) EMBO J. , vol.17 , pp. 4920-4929
    • Maeda, Y.1    Tomita, S.2    Watanabe, R.3    Ohishi, K.4    Kinoshita, T.5
  • 19
    • 0035863209 scopus 로고    scopus 로고
    • PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER
    • Maeda, Y., Watanabe, R., Harris, C. L., Hong, Y., Ohishi, K., Kinoshita, K., and Kinoshita, T. (2001). PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 20, 250-261.
    • (2001) EMBO J. , vol.20 , pp. 250-261
    • Maeda, Y.1    Watanabe, R.2    Harris, C.L.3    Hong, Y.4    Ohishi, K.5    Kinoshita, K.6    Kinoshita, T.7
  • 20
    • 4143074732 scopus 로고    scopus 로고
    • Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: Differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels
    • Marshall, S., Nadeau, O., and Yamasaki, K. (2004). 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, 35313-35319.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35313-35319
    • Marshall, S.1    Nadeau, O.2    Yamasaki, K.3
  • 21
    • 0034091742 scopus 로고    scopus 로고
    • Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids
    • McConville, M. J., and Menon, A. K. (2000). Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids. Mol. Membr. Biol. 17, 1-16.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 1-16
    • McConville, M.J.1    Menon, A.K.2
  • 22
    • 0035099785 scopus 로고    scopus 로고
    • The failure of Daudi cells to express the cellular prion protein is caused by a lack of glycosyl-phosphatidylinositol anchor formation
    • 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. Immunology 102, 242-247.
    • (2001) Immunology , vol.102 , pp. 242-247
    • Morelon, E.1    Dodelet, V.2    Lavery, P.3    Cashman, N.R.4    Loertscher, R.5
  • 23
    • 0032918610 scopus 로고    scopus 로고
    • Developmental abnormalities of glycosylphosphatidylinositol-anchor- deficient embryos revealed by Cre/loxP system
    • 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, 293-299.
    • (1999) Lab. Invest. , vol.79 , pp. 293-299
    • Nozaki, M.1    Ohishi, K.2    Yamada, N.3    Kinoshita, T.4    Nagy, A.5    Takeda, J.6
  • 26
    • 0038111847 scopus 로고    scopus 로고
    • A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum
    • 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. Biol. 23, 4983-4990.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4983-4990
    • Sobering, A.K.1    Romeo, M.J.2    Vay, H.A.3    Levin, D.E.4
  • 27
    • 2542423740 scopus 로고    scopus 로고
    • Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER
    • Sobering, A. K., Watanabe, R., Romeo, M. J., Yan, B. C., Specht, C. A., Orlean, P., Riezman, H., and Levin, D. E. (2004). Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Cell 117, 637-648.
    • (2004) Cell , vol.117 , pp. 637-648
    • Sobering, A.K.1    Watanabe, R.2    Romeo, M.J.3    Yan, B.C.4    Specht, C.A.5    Orlean, P.6    Riezman, H.7    Levin, D.E.8
  • 28
    • 0031037987 scopus 로고    scopus 로고
    • Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins
    • Spotts, G. D., Patel, S. V., Xiao, Q., and Harm, S. R. (1997). Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins. Mol. Cell. Biol. 17, 1459-1468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1459-1468
    • Spotts, G.D.1    Patel, S.V.2    Xiao, Q.3    Harm, S.R.4
  • 29
    • 2342633872 scopus 로고    scopus 로고
    • Cellular internal ribosome entry segments: Structures, trans-acting factors and regulation of gene expression
    • Stoneley, M., and Willis, A. E. (2004). Cellular internal ribosome entry segments: structures, trans-acting factors and regulation of gene expression. Oncogene 23, 3200-3207.
    • (2004) Oncogene , vol.23 , pp. 3200-3207
    • Stoneley, M.1    Willis, A.E.2
  • 30
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • 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. Cell 73, 703-711.
    • (1993) Cell , vol.73 , pp. 703-711
    • Takeda, J.1    Miyata, T.2    Kawagoe, K.3    Iida, Y.4    Endo, Y.5    Fujita, T.6    Takahashi, M.7    Kitani, T.8    Kinoshita, T.9
  • 31
    • 0030825272 scopus 로고    scopus 로고
    • Tissue specific knock-out of the mouse Pig-a gene reveals important roles for GPI-anchored proteins in skin development
    • 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. USA 94, 7400-7405.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7400-7405
    • Tarutani, M.1    Itami, S.2    Okabe, M.3    Ikawa, M.4    Tezuka, T.5    Yoshikawa, K.6    Kinoshita, T.7    Takeda, J.8
  • 32
    • 0032996466 scopus 로고    scopus 로고
    • Biosynthesis of glycosylphosphatidylinositols in mammalian and unicellular microbes
    • Tiede, A., Bastisch, I., Schubert, J., Orlean, P., and Schmidt, R. E. (1999). Biosynthesis of glycosylphosphatidylinositols in mammalian and unicellular microbes. Biol. Chem. 380, 503-523.
    • (1999) Biol. Chem. , vol.380 , pp. 503-523
    • Tiede, A.1    Bastisch, I.2    Schubert, J.3    Orlean, P.4    Schmidt, R.E.5
  • 34
    • 0035721915 scopus 로고    scopus 로고
    • Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance in Saccharomyces cerevisiae
    • Toh-e, A., and Oguchi, T. (2001). Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance in Saccharomyces cerevisiae. Genes Genet. Syst. 76, 393-410.
    • (2001) Genes Genet. Syst. , vol.76 , pp. 393-410
    • Toh-E, A.1    Oguchi, T.2
  • 35
    • 0034764497 scopus 로고    scopus 로고
    • Irresistible IRES. Attracting the translation machinery to internal ribosome entry sites
    • Vagner, S., Galy, B., and Pyronnet, S. (2001). Irresistible IRES. Attracting the translation machinery to internal ribosome entry sites. EMBO Rep. 2, 893-898.
    • (2001) EMBO Rep. , vol.2 , pp. 893-898
    • Vagner, S.1    Galy, B.2    Pyronnet, S.3
  • 36
    • 0032481318 scopus 로고    scopus 로고
    • The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
    • 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, 877-885.
    • (1998) EMBO J. , vol.17 , pp. 877-885
    • Watanabe, R.1    Inoue, N.2    Westfall, B.3    Taron, C.H.4    Orlean, P.5    Takeda, J.6    Kinoshita, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.