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Volumn 8, Issue 3, 2009, Pages 306-314

Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE; GLYCOSYLPHOSPHATIDYLINOSITOL; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 61949392673     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00257-08     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0016776835 scopus 로고
    • Substitution of cellular fatty acids in yeast cells by the antibiotic cerulenin and exogenous fatty acids
    • Awaya, J., T. Ohno, H. Ohno, and S. Omura. 1975. Substitution of cellular fatty acids in yeast cells by the antibiotic cerulenin and exogenous fatty acids. Biochim. Biophys. Acta 409:267-273.
    • (1975) Biochim. Biophys. Acta , vol.409 , pp. 267-273
    • Awaya, J.1    Ohno, T.2    Ohno, H.3    Omura, S.4
  • 2
    • 0345096560 scopus 로고    scopus 로고
    • Inositolphosphoceramide is not a substrate for the first steps in the biosynthesis of glycoinositolphospholipids in Trypanosoma cruzi
    • Bertello, L. E., M. J. Alves, W. Colli, and R. M. de Lederkremer. 2004. Inositolphosphoceramide is not a substrate for the first steps in the biosynthesis of glycoinositolphospholipids in Trypanosoma cruzi. Mol. Biochem. Parasitol. 133:71-80.
    • (2004) Mol. Biochem. Parasitol , vol.133 , pp. 71-80
    • Bertello, L.E.1    Alves, M.J.2    Colli, W.3    de Lederkremer, R.M.4
  • 3
    • 34547112529 scopus 로고    scopus 로고
    • Multiple functions of inositolphosphorylceramides in the formation and intracellular transport of glycosylphosphatidylinositol-anchored proteins in yeast
    • Bosson, R., and A. Conzelmann. 2007. Multiple functions of inositolphosphorylceramides in the formation and intracellular transport of glycosylphosphatidylinositol-anchored proteins in yeast. Biochem. Soc. Symp. 74:199-209.
    • (2007) Biochem. Soc. Symp , vol.74 , pp. 199-209
    • Bosson, R.1    Conzelmann, A.2
  • 4
    • 33744718462 scopus 로고    scopus 로고
    • GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor
    • Bosson, R., M. Jaquenoud, and A. Conzelmann. 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
  • 6
    • 0025174038 scopus 로고
    • Myoinositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53)
    • Conzelmann, A., C. Fankhauser, and C. Desponds. 1990. Myoinositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53). EMBO J. 9:653-661.
    • (1990) EMBO J , vol.9 , pp. 653-661
    • Conzelmann, A.1    Fankhauser, C.2    Desponds, C.3
  • 7
    • 0026592312 scopus 로고
    • Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae
    • Conzelmann, A., A. Puoti, R. L. Lester, and C. Desponds. 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
  • 10
    • 0023883979 scopus 로고
    • Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
    • Ferguson, M. A., S. W. Homans, R. A. Dwek, and T. W. Rademacher. 1988. Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane. Science 239:753-759.
    • (1988) Science , vol.239 , pp. 753-759
    • Ferguson, M.A.1    Homans, S.W.2    Dwek, R.A.3    Rademacher, T.W.4
  • 12
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • Fujita, M., and Y. Jigami. 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
  • 13
    • 31944447156 scopus 로고    scopus 로고
    • Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol- anchored proteins
    • Fujita, M., T. Yoko-O, and Y. Jigami. 2006. 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
  • 14
    • 34548348943 scopus 로고    scopus 로고
    • CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae
    • Ghugtyal, V., C. Vionnet, C. Roubaty, and A. Conzelmann. 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
  • 15
  • 16
    • 0033789168 scopus 로고    scopus 로고
    • Analysis of ceramides present in glycosylphosphatidylinositol anchored proteins of Saccharomyces cerevisiae
    • Guillas, I., M. Pfefferli, and A. Conzelmann. 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
  • 17
    • 0030701535 scopus 로고    scopus 로고
    • Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p
    • Haak, D., K. Gable, T. Beeler, and T. Dunn. 1997. Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J. Biol. Chem. 272:29704-29710.
    • (1997) J. Biol. Chem , vol.272 , pp. 29704-29710
    • Haak, D.1    Gable, K.2    Beeler, T.3    Dunn, T.4
  • 18
    • 0028142838 scopus 로고
    • Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast
    • Horvath, A., C. Sutterlin, U. Manning-Krieg, N. R. Movva, and H. Riezman. 1994. Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast. EMBO J. 13:3687-3695.
    • (1994) EMBO J , vol.13 , pp. 3687-3695
    • Horvath, A.1    Sutterlin, C.2    Manning-Krieg, U.3    Movva, N.R.4    Riezman, H.5
  • 20
    • 0027291426 scopus 로고
    • Regulation of fatty acid biosynthesis in Escherichia coli
    • Magnuson, K., S. Jackowski, C. O. Rock, and J. E. J. Cronan. 1993. Regulation of fatty acid biosynthesis in Escherichia coli. Microbiol. Rev. 57:522-542.
    • (1993) Microbiol. Rev , vol.57 , pp. 522-542
    • Magnuson, K.1    Jackowski, S.2    Rock, C.O.3    Cronan, J.E.J.4
  • 21
    • 0034935642 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae YCRO17c/CWH43 encodes a putative sensor/transporter protein upstream of the BCK2 branch of the PKC1-dependent cell wall integrity pathway
    • Martin-Yken, H., A. Dagkessamanskaia, P. De Groot, A. Ram, F. Klis, and J. Francois. 2001. Saccharomyces cerevisiae YCRO17c/CWH43 encodes a putative sensor/transporter protein upstream of the BCK2 branch of the PKC1-dependent cell wall integrity pathway. Yeast 18:827-840.
    • (2001) Yeast , vol.18 , pp. 827-840
    • Martin-Yken, H.1    Dagkessamanskaia, A.2    De Groot, P.3    Ram, A.4    Klis, F.5    Francois, J.6
  • 22
    • 0030724890 scopus 로고    scopus 로고
    • Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids
    • Mitchell, A. G., and C. E. Martin. 1997. Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. J. Biol. Chem. 272:28281-28288.
    • (1997) J. Biol. Chem , vol.272 , pp. 28281-28288
    • Mitchell, A.G.1    Martin, C.E.2
  • 23
    • 0029075192 scopus 로고
    • Serine palmitoyltransferase is the primary target of a sphingosine-like immunosuppressant, ISP-1/myriocin
    • Miyake, Y., Y. Kozutsumi, S. Nakamura, T. Fujita, and T. Kawasaki. 1995. Serine palmitoyltransferase is the primary target of a sphingosine-like immunosuppressant, ISP-1/myriocin. Biochem. Biophys. Res. Commun. 211:396-403.
    • (1995) Biochem. Biophys. Res. Commun , vol.211 , pp. 396-403
    • Miyake, Y.1    Kozutsumi, Y.2    Nakamura, S.3    Fujita, T.4    Kawasaki, T.5
  • 24
    • 0030970048 scopus 로고    scopus 로고
    • Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene
    • Nagiec, M. M., E. E. Nagiec, J. A. Baltisberger, G. B. Wells, R. L. Lester, and R. C. Dickson. 1997. Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J. Biol. Chem. 272:9809-9817.
    • (1997) J. Biol. Chem , vol.272 , pp. 9809-9817
    • Nagiec, M.M.1    Nagiec, E.E.2    Baltisberger, J.A.3    Wells, G.B.4    Lester, R.L.5    Dickson, R.C.6
  • 25
    • 18944406929 scopus 로고    scopus 로고
    • The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy
    • Natter, K., P. Leitner, A. Faschinger, H. Wolinski, S. McCraith, S. Fields, and S. D. Kohlwein. 2005. The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy. Mol. Cell Proteomics 4:662-672.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 662-672
    • Natter, K.1    Leitner, P.2    Faschinger, A.3    Wolinski, H.4    McCraith, S.5    Fields, S.6    Kohlwein, S.D.7
  • 26
    • 33947232747 scopus 로고    scopus 로고
    • Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae
    • Pittet, M., and A. Conzelmann. 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
  • 27
    • 31144478612 scopus 로고    scopus 로고
    • The N-glycosylation defect of cwh8Delta yeast cells causes a distinct defect in sphingolipid biosynthesis
    • Pittet, M., D. Uldry, M. Aebi, and A. Conzelmann. 2006. The N-glycosylation defect of cwh8Delta yeast cells causes a distinct defect in sphingolipid biosynthesis. Glycobiology 16:155-164.
    • (2006) Glycobiology , vol.16 , pp. 155-164
    • Pittet, M.1    Uldry, D.2    Aebi, M.3    Conzelmann, A.4
  • 28
    • 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., E. Canivenc-Gansel, and A. Conzelmann. 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
  • 29
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter, R., B. Brugger, R. Sandhoff, G. Zellnig, A. Leber, M. Lampl, K. Athenstaedt, C. Hrastnik, S. Eder, G. Daum, F. Paltauf, F. T. Wieland, and S. D. Kohlwein. 1999. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146:741-754.
    • (1999) J. Cell Biol , vol.146 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12    Kohlwein, S.D.13
  • 30
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. 2002. Getting started with yeast. Methods Enzymol. 350:3-41.
    • (2002) Methods Enzymol , vol.350 , pp. 3-41
    • Sherman, F.1
  • 31
    • 0030978758 scopus 로고    scopus 로고
    • Alternative lipid remodelling pathways for glycosylphosphatidylinositol membrane anchors in Saccharomyces cerevisiae
    • Sipos, G., F. Reggiori, C. Vionnet, and A. Conzelmann. 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
  • 32
    • 0016221254 scopus 로고
    • Inositol phosphorylceramide, a novel substance and the chief member of a major group of yeast sphingolipids containing a single inositol phosphate
    • Smith, S. W., and R. L. Lester. 1974. Inositol phosphorylceramide, a novel substance and the chief member of a major group of yeast sphingolipids containing a single inositol phosphate. J. Biol. Chem. 249:3395-3405.
    • (1974) J. Biol. Chem , vol.249 , pp. 3395-3405
    • Smith, S.W.1    Lester, R.L.2
  • 33
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sutterlin, C., T. L. Doering, F. Schimmoller, S. Schroder, and H. Riezman. 1997. Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J. Cell Sci. 110:2703-2714.
    • (1997) J. Cell Sci , vol.110 , pp. 2703-2714
    • Sutterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 34
    • 35848950226 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides
    • Umemura, M., M. Fujita, T. Yoko-O, A. Fukamizu, and Y. Jigami. 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
  • 35
    • 0037147230 scopus 로고    scopus 로고
    • Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast
    • Watanabe, R., K. Funato, K. Venkataraman, A. H. Futerman, and H. Riezman. 2002. Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast. J. Biol. Chem. 277:49538-49544.
    • (2002) J. Biol. Chem , vol.277 , pp. 49538-49544
    • Watanabe, R.1    Funato, K.2    Venkataraman, K.3    Futerman, A.H.4    Riezman, H.5
  • 36
    • 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., C. Vionnet, and A. Conzelmann. 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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