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Volumn 416, Issue , 2006, Pages 182-205

CHO Glycosylation Mutants: GPI Anchor

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; DOLICHOL PHOSPHATE; GLUCOSAMINE; GLYCOSYLPHOSPHATIDYLINOSITOL; MANNOSE; PHOSPHATIDYLINOSITOL; PHOSPHOETHANOLAMINE;

EID: 33750998494     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)16012-7     Document Type: Review
Times cited : (37)

References (55)
  • 2
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton L.M., Tseng L., Scadden D., and Cunningham J.M. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell 57 (1989) 659-666
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 3
    • 0035153789 scopus 로고    scopus 로고
    • Requirement of the Lec35 gene for all known classes of monosaccharide-P-dolichol-dependent glycosyltransferase reactions in mammals
    • Anand M., Rush J.S., Ray S., Doucey M.A., Weik J., Ware F.E., Hofsteenge J., Waechter C.J., and Lehrman M.A. Requirement of the Lec35 gene for all known classes of monosaccharide-P-dolichol-dependent glycosyltransferase reactions in mammals. Mol. Biol. Cell 12 (2001) 487-501
    • (2001) Mol. Biol. Cell , vol.12 , pp. 487-501
    • Anand, M.1    Rush, J.S.2    Ray, S.3    Doucey, M.A.4    Weik, J.5    Ware, F.E.6    Hofsteenge, J.7    Waechter, C.J.8    Lehrman, M.A.9
  • 4
    • 14844325758 scopus 로고    scopus 로고
    • Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I
    • Ashida H., Hong Y., Murakami Y., Shishioh N., Sugimoto N., Kim Y.U., Maeda Y., and Kinoshita T. Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I. Mol. Biol. Cell 16 (2005) 1439-1448
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1439-1448
    • Ashida, H.1    Hong, Y.2    Murakami, Y.3    Shishioh, N.4    Sugimoto, N.5    Kim, Y.U.6    Maeda, Y.7    Kinoshita, T.8
  • 5
    • 33644863493 scopus 로고    scopus 로고
    • DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3
    • Ashida H., Maeda Y., and Kinoshita T. DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3. J. Biol. Chem. 281 (2006) 896-904
    • (2006) J. Biol. Chem. , vol.281 , pp. 896-904
    • Ashida, H.1    Maeda, Y.2    Kinoshita, T.3
  • 6
    • 0025650995 scopus 로고
    • Complementing mutant alleles define three loci involved in mannosylation of Man5-GlcNAc2-P-P-dolichol in Chinese hamster ovary cells
    • Beck P.J., Gething M.J., Sambrook J., and Lehrman M.A. Complementing mutant alleles define three loci involved in mannosylation of Man5-GlcNAc2-P-P-dolichol in Chinese hamster ovary cells. Somat. Cell. Mol. Genet. 16 (1990) 539-548
    • (1990) Somat. Cell. Mol. Genet. , vol.16 , pp. 539-548
    • Beck, P.J.1    Gething, M.J.2    Sambrook, J.3    Lehrman, M.A.4
  • 7
    • 0029827249 scopus 로고    scopus 로고
    • Yeast Gpi8p is essential for GPI anchor attachment onto proteins
    • Benghezal M., Benachour A., Rusconi S., Aebi M., and Conzelmann A. Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J. 15 (1996) 6575-6583
    • (1996) EMBO J. , vol.15 , pp. 6575-6583
    • Benghezal, M.1    Benachour, A.2    Rusconi, S.3    Aebi, M.4    Conzelmann, A.5
  • 8
    • 0023846083 scopus 로고
    • No glycolipid anchors are added to Thy-1 glycoprotein in Thy-1 negative mutant thymoma cells of four different complementation classes
    • Conzelmann A., Spiazzi A., Bron C., and Hyman R. No glycolipid anchors are added to Thy-1 glycoprotein in Thy-1 negative mutant thymoma cells of four different complementation classes. Mol. Cell. Biol. 8 (1988) 674-678
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 674-678
    • Conzelmann, A.1    Spiazzi, A.2    Bron, C.3    Hyman, R.4
  • 9
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson M.A. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112 (1999) 2799-2809
    • (1999) J. Cell Sci. , vol.112 , pp. 2799-2809
    • Ferguson, M.A.1
  • 10
    • 0345344522 scopus 로고
    • Fusion of myeloma cells with immune spleen cells
    • Ausbel F.M., et al. (Ed), John Wiley & Sons, Inc.
    • Fuller S.A., Takahashi M., and Hurrell G.R. Fusion of myeloma cells with immune spleen cells. In: Ausbel F.M., et al. (Ed). "Current Protocols in Molecular Biology" (1987), John Wiley & Sons, Inc. 11.7.1-11.7.4
    • (1987) "Current Protocols in Molecular Biology"
    • Fuller, S.A.1    Takahashi, M.2    Hurrell, G.R.3
  • 11
    • 0032536091 scopus 로고    scopus 로고
    • Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycosylphosphatidylinositols to proteins
    • Hiroi Y., Komuro I., Chen R., Hosoda T., Mizuno T., Kudoh S., Georgescu S.P., Medof M.E., and Yazaki Y. Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycosylphosphatidylinositols to proteins. FEBS Lett. 421 (1998) 252-258
    • (1998) FEBS Lett. , vol.421 , pp. 252-258
    • Hiroi, Y.1    Komuro, I.2    Chen, R.3    Hosoda, T.4    Mizuno, T.5    Kudoh, S.6    Georgescu, S.P.7    Medof, M.E.8    Yazaki, Y.9
  • 12
    • 0026801201 scopus 로고
    • Characterization of putative glycoinositol phospholipid anchor precursors in mammalian cells. Localization of phosphoethanolamine
    • Hirose S., Prince G.M., Sevlever D., Ravi L., Rosenberry T.L., Ueda E., and Medof M.E. Characterization of putative glycoinositol phospholipid anchor precursors in mammalian cells. Localization of phosphoethanolamine. J. Biol. Chem. 267 (1992) 16968-16974
    • (1992) J. Biol. Chem. , vol.267 , pp. 16968-16974
    • Hirose, S.1    Prince, G.M.2    Sevlever, D.3    Ravi, L.4    Rosenberry, T.L.5    Ueda, E.6    Medof, M.E.7
  • 13
    • 0014202537 scopus 로고
    • Selective extraction of Polyoma DNA from infected mouse cell cultures
    • Hirt B. Selective extraction of Polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 26 (1967) 365-369
    • (1967) J. Mol. Biol. , vol.26 , pp. 365-369
    • Hirt, B.1
  • 14
    • 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. Biosynthesis and function of LFA-3 in human mutant cells deficient in phosphatidylinositol-anchored proteins. J. Immunol. 141 (1988) 4283-4290
    • (1988) J. Immunol. , vol.141 , pp. 4283-4290
    • Hollander, N.1    Selvaraj, P.2    Springer, T.A.3
  • 15
    • 0034617298 scopus 로고    scopus 로고
    • Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the third mannose in glycosylphosphatidylinositol
    • Hong Y., Maeda Y., Watanabe R., Inoue N., Ohishi K., and Kinoshita T. Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the third mannose in glycosylphosphatidylinositol. J. Biol. Chem. 275 (2000) 20911-20919
    • (2000) J. Biol. Chem. , vol.275 , pp. 20911-20919
    • Hong, Y.1    Maeda, Y.2    Watanabe, R.3    Inoue, N.4    Ohishi, K.5    Kinoshita, T.6
  • 16
    • 0033521023 scopus 로고    scopus 로고
    • Pig-N, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol
    • Hong Y., Maeda Y., Watanabe R., Ohishi K., Mishkind M., Riezman H., and Kinoshita T. Pig-N, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol. J. Biol. Chem. 274 (1999) 35099-35106
    • (1999) J. Biol. Chem. , vol.274 , pp. 35099-35106
    • Hong, Y.1    Maeda, Y.2    Watanabe, R.3    Ohishi, K.4    Mishkind, M.5    Riezman, H.6    Kinoshita, T.7
  • 17
    • 0036792614 scopus 로고    scopus 로고
    • Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin
    • Hong Y., Ohishi K., Inoue N., Kang J.Y., Shime H., Horiguchi Y., van der Goot F.G., Sugimoto N., and Kinoshita T. Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin. EMBO J. 21 (2002) 5047-5056
    • (2002) EMBO J. , vol.21 , pp. 5047-5056
    • Hong, Y.1    Ohishi, K.2    Inoue, N.3    Kang, J.Y.4    Shime, H.5    Horiguchi, Y.6    van der Goot, F.G.7    Sugimoto, N.8    Kinoshita, T.9
  • 18
    • 0038247909 scopus 로고    scopus 로고
    • Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins
    • Hong Y., Ohishi K., Kang J.Y., Tanaka S., Inoue N., Nishimura J., Maeda Y., and Kinoshita T. Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol. Biol. Cell 14 (2003) 1780-1789
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1780-1789
    • Hong, Y.1    Ohishi, K.2    Kang, J.Y.3    Tanaka, S.4    Inoue, N.5    Nishimura, J.6    Maeda, Y.7    Kinoshita, T.8
  • 19
    • 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. GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis. J. Biol. Chem. 274 (1999) 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
  • 20
    • 0023860483 scopus 로고
    • Somatic genetic analysis of the expression of cell surface molecules
    • Hyman R. Somatic genetic analysis of the expression of cell surface molecules. Trends Genet. 4 (1988) 5-8
    • (1988) Trends Genet. , vol.4 , pp. 5-8
    • Hyman, R.1
  • 21
    • 2442611903 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol (GPI) proteins of Saccharomyces cerevisiae contain ethanolamine phosphate groups on the α1,4-linked mannose of the GPI anchor
    • Imhof I., Flury I., Vionnet C., Roubaty C., Egger D., and Conzelmann A. Glycosylphosphatidylinositol (GPI) proteins of Saccharomyces cerevisiae contain ethanolamine phosphate groups on the α1,4-linked mannose of the GPI anchor. J. Biol. Chem. 279 (2004) 19614-19627
    • (2004) J. Biol. Chem. , vol.279 , pp. 19614-19627
    • Imhof, I.1    Flury, I.2    Vionnet, C.3    Roubaty, C.4    Egger, D.5    Conzelmann, A.6
  • 22
    • 0027409423 scopus 로고
    • Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy
    • Inoue N., Kinoshita T., Orii T., and Takeda J. Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J. Biol. Chem. 268 (1993) 6882-6885
    • (1993) J. Biol. Chem. , vol.268 , pp. 6882-6885
    • Inoue, N.1    Kinoshita, T.2    Orii, T.3    Takeda, J.4
  • 23
    • 0030568835 scopus 로고    scopus 로고
    • PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2
    • Inoue N., Watanabe R., Takeda J., and Kinoshita T. PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem. Biophys. Res. Comm. 226 (1996) 193-199
    • (1996) Biochem. Biophys. Res. Comm. , vol.226 , pp. 193-199
    • Inoue, N.1    Watanabe, R.2    Takeda, J.3    Kinoshita, T.4
  • 24
    • 0027371092 scopus 로고
    • Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk-cells by a human cDNA clone
    • Kamitani T., Chang H.M., Rollins C., Waneck G.L., and Yeh E.T.H. Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk-cells by a human cDNA clone. J. Biol. Chem. 268 (1993) 20733-20736
    • (1993) J. Biol. Chem. , vol.268 , pp. 20733-20736
    • Kamitani, T.1    Chang, H.M.2    Rollins, C.3    Waneck, G.L.4    Yeh, E.T.H.5
  • 26
    • 0029069154 scopus 로고
    • Expression cloning strategies for glycosylphosphatidylinositol-anchor biosynthesis enzymes and regulators
    • Kinoshita T., Miyata T., Inoue N., and Takeda J. Expression cloning strategies for glycosylphosphatidylinositol-anchor biosynthesis enzymes and regulators. Methods Enzymol. 250 (1995) 547-560
    • (1995) Methods Enzymol. , vol.250 , pp. 547-560
    • Kinoshita, T.1    Miyata, T.2    Inoue, N.3    Takeda, J.4
  • 27
    • 0033637430 scopus 로고    scopus 로고
    • Dissecting and manipulating the pathway for glycosylphosphatidylinositol-anchor biosynthesis
    • Kinoshita T., and Inoue N. Dissecting and manipulating the pathway for glycosylphosphatidylinositol-anchor biosynthesis. Curr. Opin. Chem. Biol. 4 (2000) 632-638
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 632-638
    • Kinoshita, T.1    Inoue, N.2
  • 28
    • 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 (2000) 815-822
    • (2000) Biochem. J. , vol.350 , pp. 815-822
    • Kostova, Z.1    Rancour, D.M.2    Menon, A.K.3    Orlean, P.4
  • 29
    • 0034213178 scopus 로고    scopus 로고
    • Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3
    • Maeda Y., Tanaka S., Hino J., Kangawa K., and Kinoshita T. Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3. EMBO J. 19 (2000) 2475-2482
    • (2000) EMBO J. , vol.19 , pp. 2475-2482
    • Maeda, Y.1    Tanaka, S.2    Hino, J.3    Kangawa, K.4    Kinoshita, T.5
  • 30
    • 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. 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 (1998) 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
  • 31
    • 0035863209 scopus 로고    scopus 로고
    • PIG-M transfers the first mannose to glycosylphosphatidylinositol on the luminal side of the ER
    • Maeda Y., Watanabe R., Harris C.L., Hong Y., Ohishi K., Kinoshita K., and Kinoshita T. PIG-M transfers the first mannose to glycosylphosphatidylinositol on the luminal side of the ER. EMBO J. 20 (2001) 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
  • 32
    • 0032836137 scopus 로고    scopus 로고
    • Immobilization of glycosylphosphatidylinositol-anchored proteins inhibits T cell growth but not function
    • Marmor M.D., Bachmann M.F., Ohashi P.S., Malek T.R., and Julius M. Immobilization of glycosylphosphatidylinositol-anchored proteins inhibits T cell growth but not function. Int. Immunol. 11 (1999) 1381-1393
    • (1999) Int. Immunol. , vol.11 , pp. 1381-1393
    • Marmor, M.D.1    Bachmann, M.F.2    Ohashi, P.S.3    Malek, T.R.4    Julius, M.5
  • 34
    • 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. The failure of Daudi cells to express the cellular prion protein is caused by a lack of glycosyl-phosphatidylinositol anchor formation. Immunology 102 (2001) 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
  • 35
    • 27644514673 scopus 로고    scopus 로고
    • The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component
    • Murakami Y., Siripanyaphinyo U., Hong Y., Tashima Y., Maeda Y., and Kinoshita T. The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol. Biol. Cell 16 (2005) 5236-5246
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5236-5246
    • Murakami, Y.1    Siripanyaphinyo, U.2    Hong, Y.3    Tashima, Y.4    Maeda, Y.5    Kinoshita, T.6
  • 38
    • 0035421238 scopus 로고    scopus 로고
    • PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
    • Ohishi K., Inoue N., and Kinoshita T. PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 20 (2001) 4088-4098
    • (2001) EMBO J. , vol.20 , pp. 4088-4098
    • Ohishi, K.1    Inoue, N.2    Kinoshita, T.3
  • 39
    • 0034108088 scopus 로고    scopus 로고
    • Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins
    • Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., and Kinoshita T. Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. Mol. Biol. Cell 11 (2000) 1523-1533
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1523-1533
    • Ohishi, K.1    Inoue, N.2    Maeda, Y.3    Takeda, J.4    Riezman, H.5    Kinoshita, T.6
  • 40
    • 15744391942 scopus 로고    scopus 로고
    • GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol
    • Shishioh N., Hong Y., Ohishi K., Ashida H., Maeda Y., and Kinoshita T. GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J. Biol. Chem. 280 (2005) 9728-9734
    • (2005) J. Biol. Chem. , vol.280 , pp. 9728-9734
    • Shishioh, N.1    Hong, Y.2    Ohishi, K.3    Ashida, H.4    Maeda, Y.5    Kinoshita, T.6
  • 41
    • 0030038437 scopus 로고    scopus 로고
    • Isolation and characterization of a CHO mutant defective in the second step in glycosylphosphatidylinositol biosynthesis
    • Stevens V.L., Zhang H., and Harreman M. Isolation and characterization of a CHO mutant defective in the second step in glycosylphosphatidylinositol biosynthesis. Biochem. J. 313 (1996) 253-258
    • (1996) Biochem. J. , vol.313 , pp. 253-258
    • Stevens, V.L.1    Zhang, H.2    Harreman, M.3
  • 42
    • 0020319033 scopus 로고
    • Mutant of Chinese hamster ovary cells with altered mannose 6-phosphate receptor activity is unable to synthesize mannosylphosphoryldolichol
    • Stoll J., Robbins A.R., and Krag S.S. Mutant of Chinese hamster ovary cells with altered mannose 6-phosphate receptor activity is unable to synthesize mannosylphosphoryldolichol. Proc. Natl. Acad. Sci. USA 79 (1982) 2296-2300
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2296-2300
    • Stoll, J.1    Robbins, A.R.2    Krag, S.S.3
  • 43
    • 0032524569 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B, is required for glycosylphosphatidylinositol-anchor synthesis
    • Sutterlin C., Escribano M.V., Gerold P., Maeda Y., Mazon M.J., Kinoshita T., Schwarz R.T., and Riezman H. Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B, is required for glycosylphosphatidylinositol-anchor synthesis. Biochem. J. 332 (1998) 153-159
    • (1998) Biochem. J. , vol.332 , pp. 153-159
    • Sutterlin, C.1    Escribano, M.V.2    Gerold, P.3    Maeda, Y.4    Mazon, M.J.5    Kinoshita, T.6    Schwarz, R.T.7    Riezman, H.8
  • 44
    • 1642583948 scopus 로고    scopus 로고
    • Identification of a species-specific inhibitor of glycosylphosphatidylinositol synthesis
    • Sutterlin C., Horvath A., Gerold P., Schwarz R.T., Wang Y., Dreyfuss M., and Riezman H. Identification of a species-specific inhibitor of glycosylphosphatidylinositol synthesis. EMBO J. 16 (1997) 6374-6383
    • (1997) EMBO J. , vol.16 , pp. 6374-6383
    • Sutterlin, C.1    Horvath, A.2    Gerold, P.3    Schwarz, R.T.4    Wang, Y.5    Dreyfuss, M.6    Riezman, H.7
  • 45
    • 0029782178 scopus 로고    scopus 로고
    • PIG-B, a membrane protein of the endoplasmic reticulum with a large luminal domain, is involved in transferring the third mannose of the GPI anchor
    • Takahashi M., Inoue N., Ohishi K., Maeda Y., Nakamura N., Endo Y., Fujita T., Takeda J., and Kinoshita T. PIG-B, a membrane protein of the endoplasmic reticulum with a large luminal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J. 15 (1996) 4254-4261
    • (1996) EMBO J. , vol.15 , pp. 4254-4261
    • Takahashi, M.1    Inoue, N.2    Ohishi, K.3    Maeda, Y.4    Nakamura, N.5    Endo, Y.6    Fujita, T.7    Takeda, J.8    Kinoshita, T.9
  • 46
    • 1842790673 scopus 로고    scopus 로고
    • Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p
    • Tanaka S., Maeda Y., Tashima Y., and Kinoshita T. Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. J. Biol. Chem. 279 (2004) 14256-14263
    • (2004) J. Biol. Chem. , vol.279 , pp. 14256-14263
    • Tanaka, S.1    Maeda, Y.2    Tashima, Y.3    Kinoshita, T.4
  • 47
    • 4143059365 scopus 로고    scopus 로고
    • Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo
    • Taron B.W., Colussi P.A., Grimme J.M., Orlean P., and Taron C.H. Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo. J. Biol. Chem. 279 (2004) 36083-36092
    • (2004) J. Biol. Chem. , vol.279 , pp. 36083-36092
    • Taron, B.W.1    Colussi, P.A.2    Grimme, J.M.3    Orlean, P.4    Taron, C.H.5
  • 48
    • 33644853935 scopus 로고    scopus 로고
    • PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
    • Tashima Y., Taguchi R., Murata C., Ashida H., Kinoshita T., and Maeda Y. PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins. Mol. Biol. Cell 17 (2006) 1410-1420
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1410-1420
    • Tashima, Y.1    Taguchi, R.2    Murata, C.3    Ashida, H.4    Kinoshita, T.5    Maeda, Y.6
  • 49
    • 0032502759 scopus 로고    scopus 로고
    • A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells
    • Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., and Kinoshita T. A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells. J. Biol. Chem. 273 (1998) 9249-9254
    • (1998) J. Biol. Chem. , vol.273 , pp. 9249-9254
    • Tomita, S.1    Inoue, N.2    Maeda, Y.3    Ohishi, K.4    Takeda, J.5    Kinoshita, T.6
  • 50
    • 0018192860 scopus 로고
    • The synthesis and properties of T25 glycoprotein in Thy-1-negative mutant lymphoma cells
    • Trowbridge I.S., Hyman R., and Mazauskas C. The synthesis and properties of T25 glycoprotein in Thy-1-negative mutant lymphoma cells. Cell 14 (1978) 21-32
    • (1978) Cell , vol.14 , pp. 21-32
    • Trowbridge, I.S.1    Hyman, R.2    Mazauskas, C.3
  • 51
    • 17544365076 scopus 로고    scopus 로고
    • Expression cloning of a novel suppressor of the Lec15 and Lec35 glycosylation mutations of chinese hamster ovary cells
    • Ware F.E., and Lehrman M.A. Expression cloning of a novel suppressor of the Lec15 and Lec35 glycosylation mutations of chinese hamster ovary cells. J. Biol. Chem. 271 (1996) 13935-13938
    • (1996) J. Biol. Chem. , vol.271 , pp. 13935-13938
    • Ware, F.E.1    Lehrman, M.A.2
  • 52
    • 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. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 17 (1998) 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
  • 54
    • 0030778207 scopus 로고    scopus 로고
    • The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase
    • Yu J., Nagarajan S., Knez J.J., Udenfriend S., Chen R., and Medof M.E. The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase. Proc. Natl. Acad. Sci. USA 94 (1997) 12580-12585
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12580-12585
    • Yu, J.1    Nagarajan, S.2    Knez, J.J.3    Udenfriend, S.4    Chen, R.5    Medof, M.E.6
  • 55
    • 3042575122 scopus 로고    scopus 로고
    • Genome-wide phenotype analysis in ES cells by regulated disruption of Bloom's syndrome gene
    • Yusa K., Horie K., Kondoh G., Kouno M., Maeda Y., Kinoshita T., and Takeda J. Genome-wide phenotype analysis in ES cells by regulated disruption of Bloom's syndrome gene. Nature 429 (2004) 896-899
    • (2004) Nature , vol.429 , pp. 896-899
    • Yusa, K.1    Horie, K.2    Kondoh, G.3    Kouno, M.4    Maeda, Y.5    Kinoshita, T.6    Takeda, J.7


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