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Volumn 19, Issue 1, 2000, Pages 10-15

Intracellular transport of GPI-anchored proteins

Author keywords

Ceramide; GPI anchored protein; Intracellular transport; Microdomains; Sphingolipids; Sterols

Indexed keywords

CERAMIDE; CHOLESTEROL; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYPICAN; MEMBRANE PROTEIN; SPHINGOLIPID; STEROL;

EID: 0005946413     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.1.10     Document Type: Review
Times cited : (140)

References (58)
  • 1
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed, S.N., Brown, D.A. and London, E. (1997) On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry, 36, 10944-10953.
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 2
    • 0032489878 scopus 로고    scopus 로고
    • Cargo selection by the COPII budding machinery during export from the ER
    • Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C. and Balch, W.E. (1998) Cargo selection by the COPII budding machinery during export from the ER. J. Cell Biol., 141, 61-70.
    • (1998) J. Cell Biol. , vol.141 , pp. 61-70
    • Aridor, M.1    Weissman, J.2    Bannykh, S.3    Nuoffer, C.4    Balch, W.E.5
  • 3
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., McCaffery, J.M., Plutner, H. and Farquhar, M.G. (1994) Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell, 76, 841-852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plutner, H.3    Farquhar, M.G.4
  • 4
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport
    • Belden, W.J. and Barlowe, C. (1996) Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J. Biol. Chem., 271, 26939-26946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 5
    • 0033606823 scopus 로고    scopus 로고
    • N-glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells
    • Benting, J.H., Rietveld, A.G. and Simons, K. (1999) N-glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells. J. Cell Biol., 146, 313-320.
    • (1999) J. Cell Biol. , vol.146 , pp. 313-320
    • Benting, J.H.1    Rietveld, A.G.2    Simons, K.3
  • 6
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M.S. and Munro, S. (1993) Cholesterol and the Golgi apparatus. Science, 261, 1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 7
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A. and London, E. (1998) Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol., 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 8
    • 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
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R.E. (1998) Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci., 111, 1-9.
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 10
    • 0027468760 scopus 로고
    • Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol
    • Cerneus, D.P., Ueffing, E., Posthuma, G., Strous, G.J. and van der Ende, A. (1993) Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol. J. Biol. Chem., 268, 3150-3155.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3150-3155
    • Cerneus, D.P.1    Ueffing, E.2    Posthuma, G.3    Strous, G.J.4    Van Der Ende, A.5
  • 11
    • 0024503870 scopus 로고
    • Intrinsic molecules in lipid membranes change the lipid-domain interfacial area: Cholesterol at domain interfaces
    • Cruzeiro-Hansson, L., Ipsen, J.H. and Mouritsen, O.G. (1989) Intrinsic molecules in lipid membranes change the lipid-domain interfacial area: cholesterol at domain interfaces. Biochim. Biophys. Acta, 979, 166-176.
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 166-176
    • Cruzeiro-Hansson, L.1    Ipsen, J.H.2    Mouritsen, O.G.3
  • 12
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum, G., Lees, N.D., Bard, M. and Dickson, R. (1998) Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast, 14, 1471-1510.
    • (1998) Yeast , vol.14 , pp. 1471-1510
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickson, R.4
  • 13
    • 0032583117 scopus 로고    scopus 로고
    • Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast
    • David, D., Sundarababu, S. and Gerst, J.E. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J. Cell Biol., 143, 1167-1182.
    • (1998) J. Cell Biol. , vol.143 , pp. 1167-1182
    • David, D.1    Sundarababu, S.2    Gerst, J.E.3
  • 14
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson, R.C. (1998) Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. Annu. Rev. Biochem., 67, 27-48.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 15
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas Ip transport from the endoplasmic reticulum in COP II vesicles
    • Doering, T.L. and Schekman, R. (1996) GPI anchor attachment is required for Gas Ip transport from the endoplasmic reticulum in COP II vesicles. EMBO J., 15, 182-191.
    • (1996) EMBO J. , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 16
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund, P.T. (1993) The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem., 62, 121-138.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 17
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors and the contributions of trypanosome research
    • Ferguson, M.A.J. (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.J.1
  • 18
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson, T. and Kurzchalia, T.V. (1998) Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature, 394, 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 19
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes
    • Hanada, K., Nishijima, M., Akamatsu, Y. and Pagano, R.E. (1995) Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J. Biol. Chem., 270, 6254-6260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 20
    • 0029894832 scopus 로고    scopus 로고
    • Traffic, polarity and detergent solubility of a glycosylphosphatidylinositol-anchored protein after LDL-deprivation of MDCK cells
    • Hannan, L.A. and Edidin, M. (1996) Traffic, polarity and detergent solubility of a glycosylphosphatidylinositol-anchored protein after LDL-deprivation of MDCK cells. J. Cell Biol., 133, 1265-1276.
    • (1996) J. Cell Biol. , vol.133 , pp. 1265-1276
    • Hannan, L.A.1    Edidin, M.2
  • 21
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P. and Simons, K. (1998) Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol., 141, 929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 23
    • 0028142838 scopus 로고
    • Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast
    • Horvath, A., Sütterlin, C., Manning-Krieg, U., Movva, N.R. and Riezman, H. (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    Sütterlin, C.2    Manning-Krieg, U.3    Movva, N.R.4    Riezman, H.5
  • 24
    • 0033169025 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana
    • Ilgoutz, S.C., Mullin, K.A., Southwell, B.R. and McConville, M.J. (1999) Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana. EMBO J., 18, 3643-3654.
    • (1999) EMBO J. , vol.18 , pp. 3643-3654
    • Ilgoutz, S.C.1    Mullin, K.A.2    Southwell, B.R.3    McConville, M.J.4
  • 25
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • Kirchhausen, T., Bonifacino, J.S. and Riezman, H. (1997) Linking cargo to vesicle formation: receptor tail interactions with coat proteins. Curr. Opin. Cell Biol., 9, 488-495.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 26
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors
    • Kornfeld, S. (1992) Structure and function of the mannose 6-phosphate/ insulin-like growth factor II receptors. Annu. Rev. Biochem., 61, 307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 27
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn, M.J., Herrmann, J.M. and Schekman, R. (1998) COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature, 391, 187-190.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 28
    • 0032584212 scopus 로고    scopus 로고
    • Neuronal polarity: Essential role of protein-lipid complexes in axonal sorting
    • Ledesma, M.D., Simons, K. and Dotti, C.G. (1998) Neuronal polarity: essential role of protein-lipid complexes in axonal sorting. Proc. Natl Acad. Sci. USA, 95, 3966-3971.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3966-3971
    • Ledesma, M.D.1    Simons, K.2    Dotti, C.G.3
  • 31
    • 0029881491 scopus 로고    scopus 로고
    • Interactions of N-stearoyl sphingomyelin with cholesterol and dipalmitoylphosphatidylcholine in bilayer membranes
    • Maulik, P.R. and Shipley, G.G. (1996) Interactions of N-stearoyl sphingomyelin with cholesterol and dipalmitoylphosphatidylcholine in bilayer membranes. Biophys. J., 70, 2256-2265.
    • (1996) Biophys. J. , vol.70 , pp. 2256-2265
    • Maulik, P.R.1    Shipley, G.G.2
  • 32
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays, R.W., Siemers, K.A., Fritz, B.A., Lowe, A.W., van Meer, G. and Nelson, W.J. (1995) Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol., 130, 1105-1115.
    • (1995) J. Cell Biol. , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 33
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville, M.J. and Ferguson, M.A. (1993) The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J., 294, 305-324.
    • (1993) Biochem. J. , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 34
    • 0032212917 scopus 로고    scopus 로고
    • Glycosyl-phosphatidylinositol-dependent secretory transport in Trypanosoma brucei
    • McDowell, M.A., Ransom, D.M. and Bangs, J.D. (1998) Glycosyl-phosphatidylinositol-dependent secretory transport in Trypanosoma brucei. Biochem. J., 335, 681-689.
    • (1998) Biochem. J. , vol.335 , pp. 681-689
    • McDowell, M.A.1    Ransom, D.M.2    Bangs, J.D.3
  • 35
    • 0027175236 scopus 로고
    • A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus
    • Mizuno, M. and Singer, S.J. (1993) A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc. Natl Acad. Sci. USA, 90, 5732-5736.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5732-5736
    • Mizuno, M.1    Singer, S.J.2
  • 36
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • Munro, S. (1998) Localization of proteins to the Golgi apparatus. Trends Cell Biol., 8, 11-15.
    • (1998) Trends Cell Biol. , vol.8 , pp. 11-15
    • Munro, S.1
  • 37
    • 0027438892 scopus 로고
    • A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase
    • Nagiec, M.M., Wells, G.B., Lester, R.L. and Dickson, R.C. (1993) A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase. J. Biol. Chem., 268, 22156-22163.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22156-22163
    • Nagiec, M.M.1    Wells, G.B.2    Lester, R.L.3    Dickson, R.C.4
  • 38
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes
    • Nezil, F.A. and Bloom, M. (1992) Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes. Biophys. J., 61, 1176-1183.
    • (1992) Biophys. J. , vol.61 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 39
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham, H.R. (1995) Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol., 7, 530-535.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 530-535
    • Pelham, H.R.1
  • 40
    • 0030928284 scopus 로고    scopus 로고
    • Lipid remodeling leads to the introduction and exchange of defined ceramides on GP1 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 GP1 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
  • 41
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld, A. and Simons, K. (1998) The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta, 1376, 467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 42
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E. and Wieland, F.T. (1996) Protein sorting by transport vesicles. Science, 272, 227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 43
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram, M.B. and Thompson, T.E. (1990) Interaction of cholesterol with various glycerophospholipids and sphingomyelin. Biochemistry, 29, 10670-10675.
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 44
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R. and Orci, L. (1996) Coat proteins and vesicle budding. Science, 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 45
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller, F., Singer-Kruger, B., Schroder, S., Kruger, U., Barlowe, C. and Riezman, H. (1995) The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J., 14, 1329-1339.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 46
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., London, E. and Brown, D. (1994) Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc. Natl Acad. Sci. USA, 91, 12130-12134.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 47
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder, R.J., Ahmed, S.N., Zhu, Y., London, E. and Brown, D.A. (1998) Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J. Biol. Chem., 213, 1150-1157.
    • (1998) J. Biol. Chem. , vol.213 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 48
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets, E.D., Lee, G.M., Simson, R. and Jacobson, K. (1997) Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry, 36, 12449-12458.
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 49
    • 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
  • 50
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K. and van Meer, G. (1988) Lipid sorting in epithelial cells. Biochemistry, 27, 6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 51
    • 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
  • 52
    • 0031038655 scopus 로고    scopus 로고
    • Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae
    • Skrzypek, M., Lester, R.L. and Dickson, R.C. (1997) Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae. J. Bacteriol., 179, 1513-1520.
    • (1997) J. Bacteriol. , vol.179 , pp. 1513-1520
    • Skrzypek, M.1    Lester, R.L.2    Dickson, R.C.3
  • 53
    • 0029945751 scopus 로고    scopus 로고
    • Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains
    • Smaby, J.M., Momsen, M., Kulkarni, V.S. and Brown, R.E. (1996) Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains. Biochemistry, 35, 5696-5704.
    • (1996) Biochemistry , vol.35 , pp. 5696-5704
    • Smaby, J.M.1    Momsen, M.2    Kulkarni, V.S.3    Brown, R.E.4
  • 54
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T.P. and Meyer, T. (1997) Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol., 139, 1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 55
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sütterlin, C., Doering, T.L., Schimmoller, F., Schroder, S. and Riezman, H. (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
    • Sütterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 56
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R. and Mayor, S. (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature, 394, 798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 57
    • 0033591358 scopus 로고    scopus 로고
    • Segregation of glycosylphosphatidylinositol biosynthetic reactions in a subcompartment of the endoplasmic reticulum
    • Vidugiriene, J., Sharma, D.K., Smith, T.K., Baumann, N.A. and Menon, A.K. (1999) Segregation of glycosylphosphatidylinositol biosynthetic reactions in a subcompartment of the endoplasmic reticulum. J. Biol. Chem., 274, 15203-15212.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15203-15212
    • Vidugiriene, J.1    Sharma, D.K.2    Smith, T.K.3    Baumann, N.A.4    Menon, A.K.5
  • 58
    • 0026317132 scopus 로고
    • Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme
    • Wang, E., Norred, W.P., Bacon, C.W., Riley, R.T. and Merrill, A.H., Jr (1991) Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme. J. Biol. Chem., 266, 14486-14490.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14486-14490
    • Wang, E.1    Norred, W.P.2    Bacon, C.W.3    Riley, R.T.4    Merrill, A.H.5


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