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Volumn 88, Issue 1, 2013, Pages 140-155

Determination and physiological roles of the glycosylphosphatidylinositol lipid remodelling pathway in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CERAMIDE; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; MEMBRANE PROTEIN; PER1 PROTEIN; PHOSPHOLIPASE A2; PROTEIN CWH43; PROTEIN GUP1; PROTEIN TAT2; UNCLASSIFIED DRUG;

EID: 84875577098     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12175     Document Type: Article
Times cited : (27)

References (63)
  • 1
    • 0033591254 scopus 로고    scopus 로고
    • Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity
    • Benachour, A., Sipos, G., Flury, I., Reggiori, F., Canivenc-Gansel, E., Vionnet, C., etal. (1999) Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity. J Biol Chem 274: 15251-15261.
    • (1999) J Biol Chem , vol.274 , pp. 15251-15261
    • Benachour, A.1    Sipos, G.2    Flury, I.3    Reggiori, F.4    Canivenc-Gansel, E.5    Vionnet, C.6
  • 2
    • 0032739854 scopus 로고    scopus 로고
    • Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro
    • Benting, J., Rietveld, A., Ansorge, I., and Simons, K. (1999) Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro. FEBS Lett 462: 47-50.
    • (1999) FEBS Lett , vol.462 , pp. 47-50
    • Benting, J.1    Rietveld, A.2    Ansorge, I.3    Simons, K.4
  • 3
    • 33744718462 scopus 로고    scopus 로고
    • GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor
    • Bosson, R., Jaquenoud, M., and Conzelmann, A. (2006) GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor. Mol Biol Cell 17: 2636-2645.
    • (2006) Mol Biol Cell , vol.17 , pp. 2636-2645
    • Bosson, R.1    Jaquenoud, M.2    Conzelmann, A.3
  • 4
    • 61949392673 scopus 로고    scopus 로고
    • Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro
    • Bosson, R., Guillas, I., Vionnet, C., Roubaty, C., and Conzelmann, A. (2009) Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro. Eukaryot Cell 8: 306-314.
    • (2009) Eukaryot Cell , vol.8 , pp. 306-314
    • Bosson, R.1    Guillas, I.2    Vionnet, C.3    Roubaty, C.4    Conzelmann, A.5
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P., and Boeke, J.D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 0029090114 scopus 로고
    • Structures of the glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. Comprehensive structural studies on the porcine anchor and interspecies comparison of the glycan core structures
    • Brewis, I.A., Ferguson, M.A., Mehlert, A., Turner, A.J., and Hooper, N.M. (1995) Structures of the glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. Comprehensive structural studies on the porcine anchor and interspecies comparison of the glycan core structures. J Biol Chem 270: 22946-22956.
    • (1995) J Biol Chem , vol.270 , pp. 22946-22956
    • Brewis, I.A.1    Ferguson, M.A.2    Mehlert, A.3    Turner, A.J.4    Hooper, N.M.5
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and Rose, J.K. (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68: 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 9
    • 15444346372 scopus 로고    scopus 로고
    • In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae
    • Caro, L.H., Tettelin, H., Vossen, J.H., Ram, A.F., van den Ende, H., and Klis, F.M. (1997) In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae. Yeast 13: 1477-1489.
    • (1997) Yeast , vol.13 , pp. 1477-1489
    • Caro, L.H.1    Tettelin, H.2    Vossen, J.H.3    van den Ram, A.F.4    Ende, H.5    Klis, F.M.6
  • 10
  • 11
    • 80051686141 scopus 로고    scopus 로고
    • The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling
    • Castillon, G.A., Aguilera-Romero, A., Manzano-Lopez, J., Epstein, S., Kajiwara, K., Funato, K., etal. (2011) The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling. Mol Biol Cell 22: 2924-2936.
    • (2011) Mol Biol Cell , vol.22 , pp. 2924-2936
    • Castillon, G.A.1    Aguilera-Romero, A.2    Manzano-Lopez, J.3    Epstein, S.4    Kajiwara, K.5    Funato, K.6
  • 12
    • 0024043540 scopus 로고
    • A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae is attached to the lipid bilayer through an inositol-containing phospholipid
    • Conzelmann, A., Riezman, H., Desponds, C., and Bron, C. (1988) A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae is attached to the lipid bilayer through an inositol-containing phospholipid. EMBO J 7: 2233-2240.
    • (1988) EMBO J , vol.7 , pp. 2233-2240
    • Conzelmann, A.1    Riezman, H.2    Desponds, C.3    Bron, C.4
  • 13
    • 0026592312 scopus 로고
    • Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae
    • Conzelmann, A., Puoti, A., Lester, R.L., and Desponds, C. (1992) Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae. EMBO J 11: 457-466.
    • (1992) EMBO J , vol.11 , pp. 457-466
    • Conzelmann, A.1    Puoti, A.2    Lester, R.L.3    Desponds, C.4
  • 14
    • 20544439767 scopus 로고    scopus 로고
    • Features and functions of covalently linked proteins in fungal cell walls
    • De Groot, P.W., Ram, A.F., and Klis, F.M. (2005) Features and functions of covalently linked proteins in fungal cell walls. Fungal Genet Biol 42: 657-675.
    • (2005) Fungal Genet Biol , vol.42 , pp. 657-675
    • De Groot, P.W.1    Ram, A.F.2    Klis, F.M.3
  • 16
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson, M.A. (1999) The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J Cell Sci 112: 2799-2809.
    • (1999) J Cell Sci , vol.112 , pp. 2799-2809
    • Ferguson, M.A.1
  • 17
    • 33749993571 scopus 로고    scopus 로고
    • Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology
    • Ferreira, C., Silva, S., van Voorst, F., Aguiar, C., Kielland-Brandt, M.C., Brandt, A., and Lucas, C. (2006) Absence of Gup1p in Saccharomyces cerevisiae results in defective cell wall composition, assembly, stability and morphology. FEMS Yeast Res 6: 1027-1038.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1027-1038
    • Ferreira, C.1    van Silva, S.2    Voorst, F.3    Aguiar, C.4    Kielland-Brandt, M.C.5    Brandt, A.6    Lucas, C.7
  • 18
    • 0037367735 scopus 로고    scopus 로고
    • Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins
    • Fontaine, T., Magnin, T., Melhert, A., Lamont, D., Latge, J.P., and Ferguson, M.A. (2003) Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins. Glycobiology 13: 169-177.
    • (2003) Glycobiology , vol.13 , pp. 169-177
    • Fontaine, T.1    Magnin, T.2    Melhert, A.3    Lamont, D.4    Latge, J.P.5    Ferguson, M.A.6
  • 19
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • Fujita, M., and Jigami, Y. (2008) Lipid remodeling of GPI-anchored proteins and its function. Biochim Biophys Acta 1780: 410-420.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 410-420
    • Fujita, M.1    Jigami, Y.2
  • 20
    • 77951895530 scopus 로고    scopus 로고
    • Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins
    • Fujita, M., and Kinoshita, T. (2010) Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins. FEBS Lett 584: 1670-1677.
    • (2010) FEBS Lett , vol.584 , pp. 1670-1677
    • Fujita, M.1    Kinoshita, T.2
  • 21
    • 84862189303 scopus 로고    scopus 로고
    • GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics
    • Fujita, M., and Kinoshita, T. (2012) GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics. Biochim Biophys Acta 1821: 1050-1058.
    • (2012) Biochim Biophys Acta , vol.1821 , pp. 1050-1058
    • Fujita, M.1    Kinoshita, T.2
  • 22
    • 31944447156 scopus 로고    scopus 로고
    • Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins
    • Fujita, M., Yoko-o, T., and Jigami, Y. (2006a) Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins. Mol Biol Cell 17: 834-850.
    • (2006) Mol Biol Cell , vol.17 , pp. 834-850
    • Fujita, M.1    Yoko-o, T.2    Jigami, Y.3
  • 23
  • 24
    • 79960238560 scopus 로고    scopus 로고
    • Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI
    • Fujita, M., Watanabe, R., Jaensch, N., Romanova-Michaelides, M., Satoh, T., Kato, M., etal. (2011) Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI. J Cell Biol 194: 61-75.
    • (2011) J Cell Biol , vol.194 , pp. 61-75
    • Fujita, M.1    Watanabe, R.2    Jaensch, N.3    Romanova-Michaelides, M.4    Satoh, T.5    Kato, M.6
  • 25
    • 34548348943 scopus 로고    scopus 로고
    • CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae
    • Ghugtyal, V., Vionnet, C., Roubaty, C., and Conzelmann, A. (2007) CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae. Mol Microbiol 65: 1493-1502.
    • (2007) Mol Microbiol , vol.65 , pp. 1493-1502
    • Ghugtyal, V.1    Vionnet, C.2    Roubaty, C.3    Conzelmann, A.4
  • 26
    • 0033789168 scopus 로고    scopus 로고
    • Analysis of ceramides present in glycosylphosphatidylinositol anchored proteins of Saccharomyces cerevisiae
    • Guillas, I., Pfefferli, M., and Conzelmann, A. (2000) Analysis of ceramides present in glycosylphosphatidylinositol anchored proteins of Saccharomyces cerevisiae. Methods Enzymol 312: 506-515.
    • (2000) Methods Enzymol , vol.312 , pp. 506-515
    • Guillas, I.1    Pfefferli, M.2    Conzelmann, A.3
  • 27
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo, S., Stolz, L.E., Lemrow, S.M., and York, J.D. (1999) SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J Biol Chem 274: 12990-12995.
    • (1999) J Biol Chem , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 28
    • 0033024416 scopus 로고    scopus 로고
    • Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins
    • Hamada, K., Terashima, H., Arisawa, M., Yabuki, N., and Kitada, K. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181: 3886-3889.
    • (1999) J Bacteriol , vol.181 , pp. 3886-3889
    • Hamada, K.1    Terashima, H.2    Arisawa, M.3    Yabuki, N.4    Kitada, K.5
  • 29
    • 0033909398 scopus 로고    scopus 로고
    • GUP1 and its close homologue GUP2, encoding multimembrane-spanning proteins involved in active glycerol uptake in Saccharomyces cerevisiae
    • Holst, B., Lunde, C., Lages, F., Oliveira, R., Lucas, C., and Kielland-Brandt, M.C. (2000) GUP1 and its close homologue GUP2, encoding multimembrane-spanning proteins involved in active glycerol uptake in Saccharomyces cerevisiae. Mol Microbiol 37: 108-124.
    • (2000) Mol Microbiol , vol.37 , pp. 108-124
    • Holst, B.1    Lunde, C.2    Lages, F.3    Oliveira, R.4    Lucas, C.5    Kielland-Brandt, M.C.6
  • 30
    • 79956290239 scopus 로고    scopus 로고
    • Triacylglycerol/phospholipid molecular species profiling of fatty livers and regenerated non-fatty livers in cystathionine beta-synthase-deficient mice, an animal model for homocysteinemia/homocystinuria
    • Ikeda, K., Kubo, A., Akahoshi, N., Yamada, H., Miura, N., Hishiki, T., etal. (2011) Triacylglycerol/phospholipid molecular species profiling of fatty livers and regenerated non-fatty livers in cystathionine beta-synthase-deficient mice, an animal model for homocysteinemia/homocystinuria. Anal Bioanal Chem 400: 1853-1863.
    • (2011) Anal Bioanal Chem , vol.400 , pp. 1853-1863
    • Ikeda, K.1    Kubo, A.2    Akahoshi, N.3    Yamada, H.4    Miura, N.5    Hishiki, T.6
  • 32
    • 0032962171 scopus 로고    scopus 로고
    • The contribution of cell wall proteins to the organization of the yeast cell wall
    • Kapteyn, J.C., Van Den Ende, H., and Klis, F.M. (1999) The contribution of cell wall proteins to the organization of the yeast cell wall. Biochim Biophys Acta 1426: 373-383.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 373-383
    • Kapteyn, J.C.1    Van Den Ende, H.2    Klis, F.M.3
  • 33
    • 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
  • 34
    • 33645121842 scopus 로고    scopus 로고
    • Cell wall construction in Saccharomyces cerevisiae
    • Klis, F.M., Boorsma, A., and De Groot, P.W. (2006) Cell wall construction in Saccharomyces cerevisiae. Yeast 23: 185-202.
    • (2006) Yeast , vol.23 , pp. 185-202
    • Klis, F.M.1    Boorsma, A.2    De Groot, P.W.3
  • 35
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., McKenzie, A., 3rd, Demarini, D.J., Shah, N.G., Wach, A., Brachat, A., etal. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14: 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6
  • 36
    • 0027268692 scopus 로고
    • The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis
    • McConville, M.J., Collidge, T.A., Ferguson, M.A., and Schneider, P. (1993) The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis. J Biol Chem 268: 15595-15604.
    • (1993) J Biol Chem , vol.268 , pp. 15595-15604
    • McConville, M.J.1    Collidge, T.A.2    Ferguson, M.A.3    Schneider, P.4
  • 37
    • 34247228098 scopus 로고    scopus 로고
    • Fatty acid remodeling of GPI-anchored proteins is required for their raft association
    • Maeda, Y., Tashima, Y., Houjou, T., Fujita, M., Yoko-o, T., Jigami, Y., etal. (2007) Fatty acid remodeling of GPI-anchored proteins is required for their raft association. Mol Biol Cell 18: 1497-1506.
    • (2007) Mol Biol Cell , vol.18 , pp. 1497-1506
    • Maeda, Y.1    Tashima, Y.2    Houjou, T.3    Fujita, M.4    Yoko-o, T.5    Jigami, Y.6
  • 38
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • Malinska, K., Malinsky, J., Opekarova, M., and Tanner, W. (2003) Visualization of protein compartmentation within the plasma membrane of living yeast cells. Mol Biol Cell 14: 4427-4436.
    • (2003) Mol Biol Cell , vol.14 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 39
    • 0031553842 scopus 로고    scopus 로고
    • 14C]ceramide synthesis by sphingolipid ceramide N-deacylase: new assay for ceramidase activity detection
    • 14C]ceramide synthesis by sphingolipid ceramide N-deacylase: new assay for ceramidase activity detection. Anal Biochem 247: 52-57.
    • (1997) Anal Biochem , vol.247 , pp. 52-57
    • Mitsutake, S.1    Kita, K.2    Okino, N.3    Ito, M.4
  • 40
    • 79851485648 scopus 로고    scopus 로고
    • Isolation of nano-meso scale detergent resistant membrane that has properties expected of lipid 'rafts'
    • Morris, R.J., Jen, A., and Warley, A. (2011) Isolation of nano-meso scale detergent resistant membrane that has properties expected of lipid 'rafts'. J Neurochem 116: 671-677.
    • (2011) J Neurochem , vol.116 , pp. 671-677
    • Morris, R.J.1    Jen, A.2    Warley, A.3
  • 41
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muñiz, M., Morsomme, P., and Riezman, H. (2001) Protein sorting upon exit from the endoplasmic reticulum. Cell 104: 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muñiz, M.1    Morsomme, P.2    Riezman, H.3
  • 42
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro, S. (2003) Lipid rafts: elusive or illusive? Cell 115: 377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 43
    • 33645216185 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins are required for the transport of detergent-resistant microdomain-associated membrane proteins Tat2p and Fur4p
    • Okamoto, M., Yoko-o, T., Umemura, M., Nakayama, K., and Jigami, Y. (2006) Glycosylphosphatidylinositol-anchored proteins are required for the transport of detergent-resistant microdomain-associated membrane proteins Tat2p and Fur4p. J Biol Chem 281: 4013-4023.
    • (2006) J Biol Chem , vol.281 , pp. 4013-4023
    • Okamoto, M.1    Yoko-o, T.2    Umemura, M.3    Nakayama, K.4    Jigami, Y.5
  • 44
    • 34248227584 scopus 로고    scopus 로고
    • Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids
    • Orlean, P., and Menon, A.K. (2007) Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J Lipid Res 48: 993-1011.
    • (2007) J Lipid Res , vol.48 , pp. 993-1011
    • Orlean, P.1    Menon, A.K.2
  • 45
    • 33947232747 scopus 로고    scopus 로고
    • Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae
    • Pittet, M., and Conzelmann, A. (2007) Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1771: 405-420.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 405-420
    • Pittet, M.1    Conzelmann, A.2
  • 46
    • 0032903637 scopus 로고    scopus 로고
    • The Gas1 glycoprotein, a putative wall polymer cross-linker
    • Popolo, L., and Vai, M. (1999) The Gas1 glycoprotein, a putative wall polymer cross-linker. Biochim Biophys Acta 1426: 385-400.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 385-400
    • Popolo, L.1    Vai, M.2
  • 47
    • 0030928284 scopus 로고    scopus 로고
    • Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae
    • Reggiori, F., Canivenc-Gansel, E., and Conzelmann, A. (1997) Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae. EMBO J 16: 3506-3518.
    • (1997) EMBO J , vol.16 , pp. 3506-3518
    • Reggiori, F.1    Canivenc-Gansel, E.2    Conzelmann, A.3
  • 48
    • 0032827469 scopus 로고    scopus 로고
    • A constitutive role for GPI anchors in Saccharomyces cerevisiae: cell wall targeting
    • de Sampaïo, G., Bourdineaud, J.P., and Lauquin, G.J. (1999) A constitutive role for GPI anchors in Saccharomyces cerevisiae: cell wall targeting. Mol Microbiol 34: 247-256.
    • (1999) Mol Microbiol , vol.34 , pp. 247-256
    • de Sampaïo, G.1    Bourdineaud, J.P.2    Lauquin, G.J.3
  • 49
    • 0034670379 scopus 로고    scopus 로고
    • Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae
    • Sawai, H., Okamoto, Y., Luberto, C., Mao, C., Bielawska, A., Domae, N., and Hannun, Y.A. (2000) Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae. J Biol Chem 275: 39793-39798.
    • (2000) J Biol Chem , vol.275 , pp. 39793-39798
    • Sawai, H.1    Okamoto, Y.2    Luberto, C.3    Mao, C.4    Bielawska, A.5    Domae, N.6    Hannun, Y.A.7
  • 50
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol 194: 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 51
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 52
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387: 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 53
    • 0028300734 scopus 로고
    • Glycosylphosphatidylinositol membrane anchors in Saccharomyces cerevisiae: absence of ceramides from complete precursor glycolipids
    • Sipos, G., Puoti, A., and Conzelmann, A. (1994) Glycosylphosphatidylinositol membrane anchors in Saccharomyces cerevisiae: absence of ceramides from complete precursor glycolipids. EMBO J 13: 2789-2796.
    • (1994) EMBO J , vol.13 , pp. 2789-2796
    • Sipos, G.1    Puoti, A.2    Conzelmann, A.3
  • 54
    • 0030978758 scopus 로고    scopus 로고
    • Alternative lipid remodelling pathways for glycosylphosphatidylinositol membrane anchors in Saccharomyces cerevisiae
    • Sipos, G., Reggiori, F., Vionnet, C., and Conzelmann, A. (1997) Alternative lipid remodelling pathways for glycosylphosphatidylinositol membrane anchors in Saccharomyces cerevisiae. EMBO J 16: 3494-3505.
    • (1997) EMBO J , vol.16 , pp. 3494-3505
    • Sipos, G.1    Reggiori, F.2    Vionnet, C.3    Conzelmann, A.4
  • 55
    • 0031893414 scopus 로고    scopus 로고
    • Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae
    • Stolz, L.E., Huynh, C.V., Thorner, J., and York, J.D. (1998a) Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae. Genetics 148: 1715-1729.
    • (1998) Genetics , vol.148 , pp. 1715-1729
    • Stolz, L.E.1    Huynh, C.V.2    Thorner, J.3    York, J.D.4
  • 56
    • 0032496156 scopus 로고    scopus 로고
    • INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype
    • Stolz, L.E., Kuo, W.J., Longchamps, J., Sekhon, M.K., and York, J.D. (1998b) INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4, 5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype. J Biol Chem 273: 11852-11861.
    • (1998) J Biol Chem , vol.273 , pp. 11852-11861
    • Stolz, L.E.1    Kuo, W.J.2    Longchamps, J.3    Sekhon, M.K.4    York, J.D.5
  • 58
    • 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. (2004) Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. J Biol Chem 279: 14256-14263.
    • (2004) J Biol Chem , vol.279 , pp. 14256-14263
    • Tanaka, S.1    Maeda, Y.2    Tashima, Y.3    Kinoshita, T.4
  • 59
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B.J., and Rothstein, R. (1989) Elevated recombination rates in transcriptionally active DNA. Cell 56: 619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 60
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
    • Umebayashi, K., and Nakano, A. (2003) Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J Cell Biol 161: 1117-1131.
    • (2003) J Cell Biol , vol.161 , pp. 1117-1131
    • Umebayashi, K.1    Nakano, A.2
  • 61
    • 35848950226 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides
    • Umemura, M., Fujita, M., Yoko-o, T., Fukamizu, A., and Jigami, Y. (2007) Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides. Mol Biol Cell 18: 4304-4316.
    • (2007) Mol Biol Cell , vol.18 , pp. 4304-4316
    • Umemura, M.1    Fujita, M.2    Yoko-o, T.3    Fukamizu, A.4    Jigami, Y.5
  • 62
    • 0035831447 scopus 로고    scopus 로고
    • The yeast inositol polyphosphate 5-phosphatase Inp54p localizes to the endoplasmic reticulum via a C-terminal hydrophobic anchoring tail: regulation of secretion from the endoplasmic reticulum
    • Wiradjaja, F., Ooms, L.M., Whisstock, J.C., McColl, B., Helfenbaum, L., Sambrook, J.F., etal. (2001) The yeast inositol polyphosphate 5-phosphatase Inp54p localizes to the endoplasmic reticulum via a C-terminal hydrophobic anchoring tail: regulation of secretion from the endoplasmic reticulum. J Biol Chem 276: 7643-7653.
    • (2001) J Biol Chem , vol.276 , pp. 7643-7653
    • Wiradjaja, F.1    Ooms, L.M.2    Whisstock, J.C.3    McColl, B.4    Helfenbaum, L.5    Sambrook, J.F.6
  • 63
    • 33745970481 scopus 로고    scopus 로고
    • Ethanolaminephosphate side chain added to glycosylphosphatidylinositol (GPI) anchor by Mcd4p is required for ceramide remodeling and forward transport of GPI proteins from endoplasmic reticulum to Golgi
    • Zhu, Y., Vionnet, C., and Conzelmann, A. (2006) Ethanolaminephosphate side chain added to glycosylphosphatidylinositol (GPI) anchor by Mcd4p is required for ceramide remodeling and forward transport of GPI proteins from endoplasmic reticulum to Golgi. J Biol Chem 281: 19830-19839.
    • (2006) J Biol Chem , vol.281 , pp. 19830-19839
    • Zhu, Y.1    Vionnet, C.2    Conzelmann, A.3


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