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Volumn 141, Issue 4, 1998, Pages 917-927

Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN; CHOLERA TOXIN; ESCHERICHIA COLI ENTEROTOXIN; GANGLIOSIDE; GANGLIOSIDE GD 1A; GANGLIOSIDE GM1; RECEPTOR SUBUNIT;

EID: 0031802210     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.4.917     Document Type: Article
Times cited : (183)

References (75)
  • 1
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson, R.G. 1993a. Caveolae: where incoming and outgoing messengers meet. Proc. Natl. Acad. Sci. USA. 90:10909-10913.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10909-10913
    • Anderson, R.G.1
  • 2
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson, R.G. 1993b. Plasmalemmal caveolae and GPI-anchored membrane proteins. Curr. Opin. Cell Biol. 5:647-652.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 647-652
    • Anderson, R.G.1
  • 3
    • 0026545612 scopus 로고
    • Potocytosis: Sequestration and transport of small molecules by caveolae
    • Anderson, R.G., B.A. Kamen, K.G. Rothberg, and S.W. Lacey. 1992. Potocytosis: sequestration and transport of small molecules by caveolae. Science. 255: 410-411.
    • (1992) Science , vol.255 , pp. 410-411
    • Anderson, R.G.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 4
    • 0031019429 scopus 로고    scopus 로고
    • Understanding covalent modifications of proteins by lipids: Where cell biology and biophysics merge
    • Bhatnagar, R.S., and J.I. Gordon. 1997. Understanding covalent modifications of proteins by lipids: where cell biology and biophysics merge. Trends Cell Biol. 7:14-20.
    • (1997) Trends Cell Biol. , vol.7 , pp. 14-20
    • Bhatnagar, R.S.1    Gordon, J.I.2
  • 5
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M.S., and S. Munro. 1993. Cholesterol and the Golgi apparatus. Science. 261:1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 6
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and J.K. Rose. 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
  • 7
    • 0023388301 scopus 로고
    • Type II heat-labile enterotoxin of Escherichia coli activates adenylate cyclase in human fibroblasts by ADP ribosylation
    • Chang, P.P., J. Moss, E.M. Twiddy, and R.K. Holmes. 1987. Type II heat-labile enterotoxin of Escherichia coli activates adenylate cyclase in human fibroblasts by ADP ribosylation. Infect. Immun. 55:1854-1858.
    • (1987) Infect. Immun. , vol.55 , pp. 1854-1858
    • Chang, P.P.1    Moss, J.2    Twiddy, E.M.3    Holmes, R.K.4
  • 8
    • 0026576742 scopus 로고
    • Characterization of hybrid toxins produced in Escherichia coli by assembly of A and B polypeptides from Type I and Type II heat-labile enterotoxins
    • Connell, T.D., and R.K. Holmes. 1992. Characterization of hybrid toxins produced in Escherichia coli by assembly of A and B polypeptides from Type I and Type II heat-labile enterotoxins. Infect. Immun. 60:1653-1661.
    • (1992) Infect. Immun. , vol.60 , pp. 1653-1661
    • Connell, T.D.1    Holmes, R.K.2
  • 9
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • Conrad, P.A., E.J. Smart, Y.-S. Ying, R.G.W. Anderson, and G.S. Bloom. 1995. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J. Cell Biol. 131:1421-1433.
    • (1995) J. Cell Biol. , vol.131 , pp. 1421-1433
    • Conrad, P.A.1    Smart, E.J.2    Ying, Y.-S.3    Anderson, R.G.W.4    Bloom, G.S.5
  • 10
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert, M., M. Ticchioni, and A. Bernard. 1996. Endocytosis of GPI-anchored proteins in human lymphocytes: role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J. Cell Biol. 133:791-799.
    • (1996) J. Cell Biol. , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 12
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler, K., R.G. Parton, R. Kellner, T. Etzold, and K. Simons. 1994. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 13:1729-1740.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 13
    • 0020604944 scopus 로고
    • Uptake and metabolism of exogenous gangliosides by cultured cells: Effect of choleragen on the turnover of GM1
    • Fishman, P.H, R.M. Bradley, B.E. Hom, and J. Moss. 1983. Uptake and metabolism of exogenous gangliosides by cultured cells: effect of choleragen on the turnover of GM1. J. Lipid Res. 24:1002-1011.
    • (1983) J. Lipid Res. , vol.24 , pp. 1002-1011
    • Fishman, P.H.1    Bradley, R.M.2    Hom, B.E.3    Moss, J.4
  • 14
    • 0030269967 scopus 로고    scopus 로고
    • Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm
    • French, C., E. Keshavarz-Moore, and J.M. Ward. 1996. Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm. Enzyme Microb. Technol. 19:332-338.
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 332-338
    • French, C.1    Keshavarz-Moore, E.2    Ward, J.M.3
  • 15
    • 0023916532 scopus 로고
    • Comparison of the carbohydrate-binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxins LTh-I, LT-IIa, and LT-IIb
    • Fukuta, S., J.L. Magnani, E.M. Twiddy, R.K. Holmes, and V. Ginsburg. 1988. Comparison of the carbohydrate-binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxins LTh-I, LT-IIa, and LT-IIb. Infect. Immun. 56:1748-1753.
    • (1988) Infect. Immun. , vol.56 , pp. 1748-1753
    • Fukuta, S.1    Magnani, J.L.2    Twiddy, E.M.3    Holmes, R.K.4    Ginsburg, V.5
  • 16
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • Gorodinsky, A., and D.A. Harris. 1995. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129:619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 17
    • 0022994808 scopus 로고
    • Variation in chemical properties and antigenic determinants among type II heat-labile enterotoxins of Escherichia coli
    • Guth, B.E.C., E.M. Twiddy, L.R. Trabulsi, and R.K. Holmes. 1986. Variation in chemical properties and antigenic determinants among type II heat-labile enterotoxins of Escherichia coli. Infect. Immun. 54:529-536.
    • (1986) Infect. Immun. , vol.54 , pp. 529-536
    • Guth, B.E.C.1    Twiddy, E.M.2    Trabulsi, L.R.3    Holmes, R.K.4
  • 18
    • 0001893070 scopus 로고
    • Chemistry of glycosphingolipids
    • J.N. Kanfer and S. Hakomori, editors. Plenum Press, New York
    • Hakomori, S. 1983. Chemistry of glycosphingolipids. In Sphingolipid Biochemistry. J.N. Kanfer and S. Hakomori, editors. Plenum Press, New York. 1-166.
    • (1983) Sphingolipid Biochemistry , pp. 1-166
    • Hakomori, S.1
  • 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., M. Nishijima, Y. Akamatsu, and R.E. Pagano. 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
    • 0027361965 scopus 로고
    • Molecules internalized by clathrin-independent endocytosis are delivered to endosomes containing transferrin receptors
    • Hansen, S.H., K. Sandvig, and B. van Deurs. 1993. Molecules internalized by clathrin-independent endocytosis are delivered to endosomes containing transferrin receptors. J. Cell Biol. 123:89-97.
    • (1993) J. Cell Biol. , vol.123 , pp. 89-97
    • Hansen, S.H.1    Sandvig, K.2    Van Deurs, B.3
  • 21
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeleton elements by sequestration of membrane cholesterol
    • Harder, T., R. Kellner, R.G. Parton, and J. Gruenberg. 1997. Specific release of membrane-bound annexin II and cortical cytoskeleton elements by sequestration of membrane cholesterol. Mol. Biol. Cell. 8:533-545.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 22
    • 0021088626 scopus 로고
    • Characterization of monoclonal antibodies that react with unique and cross-reacting determinants of cholera enterotoxin and its subunits
    • Holmes, R.K., and E.M. Twiddy. 1983. Characterization of monoclonal antibodies that react with unique and cross-reacting determinants of cholera enterotoxin and its subunits. Infect. Immun. 42:914-923.
    • (1983) Infect. Immun. , vol.42 , pp. 914-923
    • Holmes, R.K.1    Twiddy, E.M.2
  • 23
    • 0022443463 scopus 로고
    • Purification and characterization of type II heat-labile enterotoxin of Escherichia coli
    • Holmes, R. K., E.M. Twiddy, and C.L. Pickett. 1986. Purification and characterization of type II heat-labile enterotoxin of Escherichia coli. Infect. Immun. 53:464-473.
    • (1986) Infect. Immun. , vol.53 , pp. 464-473
    • Holmes, R.K.1    Twiddy, E.M.2    Pickett, C.L.3
  • 25
    • 0031280495 scopus 로고    scopus 로고
    • Construction and characterization of versatile cloning vectors for efficient delivery of native foreign proteins to the periplasm of Escherichia coli
    • Jobling, M.G., L.M. Palmer, J.L. Erbe, and R.K. Holmes. 1997. Construction and characterization of versatile cloning vectors for efficient delivery of native foreign proteins to the periplasm of Escherichia coli. Plasmid. 38:158-173.
    • (1997) Plasmid , vol.38 , pp. 158-173
    • Jobling, M.G.1    Palmer, L.M.2    Erbe, J.L.3    Holmes, R.K.4
  • 26
    • 0028177422 scopus 로고
    • VIP21-Caveolin, a protein of the trans-Golgi network and caveolae
    • Kurzchalia, T.V., P. Dupree, and S. Monier. 1994. VIP21-Caveolin, a protein of the trans-Golgi network and caveolae. FEBS Lett. 346:88-91.
    • (1994) FEBS Lett. , vol.346 , pp. 88-91
    • Kurzchalia, T.V.1    Dupree, P.2    Monier, S.3
  • 27
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia, T.V., P. Dupree, R.G. Parton, R. Kellner, H. Virta, M. Lehnert, and K. Simons. 1992. VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol. 118: 1003-1014.
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 28
    • 0025909488 scopus 로고
    • Activation of Escherichia coli heatlabile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins
    • Lee, C.-M., P.P. Chang, S.-C. Tsai, R. Adamik, S.R. Price, B.C. Kunz, J. Moss, E.M. Twiddy, and R.K. Holmes. 1991. Activation of Escherichia coli heatlabile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins. J. Clin. Invest. 87:1780-1786.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1780-1786
    • Lee, C.-M.1    Chang, P.P.2    Tsai, S.-C.3    Adamik, R.4    Price, S.R.5    Kunz, B.C.6    Moss, J.7    Twiddy, E.M.8    Holmes, R.K.9
  • 29
    • 0026681578 scopus 로고
    • Mechanism of cholera toxin action on a polarized human epithelial cell line: Role of vesicular traffic
    • Lencer, W.I., C. Delp, M.R. Neutra, and J.L. Madara. 1992. Mechanism of cholera toxin action on a polarized human epithelial cell line: role of vesicular traffic. J. Cell Biol. 117:1197-1209.
    • (1992) J. Cell Biol. , vol.117 , pp. 1197-1209
    • Lencer, W.I.1    Delp, C.2    Neutra, M.R.3    Madara, J.L.4
  • 30
    • 0027142025 scopus 로고
    • Entry of cholera toxin into polarized human intestinal epithelial cells: Identification of an early brefeldin a sensitive event required for A1-peptide generation
    • Lencer, W.I., J.B. de Almeida, S. Moe, J.L. Stow, D.A. Ausiello, and J.L. Madara. 1993. Entry of cholera toxin into polarized human intestinal epithelial cells: identification of an early brefeldin A sensitive event required for A1-peptide generation. J. Clin. Invest. 92:2941-2951.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2941-2951
    • Lencer, W.I.1    De Almeida, J.B.2    Moe, S.3    Stow, J.L.4    Ausiello, D.A.5    Madara, J.L.6
  • 32
    • 0028853907 scopus 로고
    • Transcytosis of cholera toxin subunits across model human intestinal epithelia
    • Lencer, W.I., S. Moe, P.A. Rufo, and J.L. Madara. 1995b. Transcytosis of cholera toxin subunits across model human intestinal epithelia. Proc. Natl. Acad. Sci. USA. 92:10094-10098.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10094-10098
    • Lencer, W.I.1    Moe, S.2    Rufo, P.A.3    Madara, J.L.4
  • 33
    • 0028787861 scopus 로고
    • Signal transduction by cholera toxin: Processing in vesicular compartments does not require acidification
    • Lencer, W.I., G. Strohmeier, S. Moe, S.L. Carlson, C.T. Constable, and J.L. Madara. 1995c. Signal transduction by cholera toxin: processing in vesicular compartments does not require acidification. Am. J. Physiol. 269:G548-G557.
    • (1995) Am. J. Physiol. , vol.269
    • Lencer, W.I.1    Strohmeier, G.2    Moe, S.3    Carlson, S.L.4    Constable, C.T.5    Madara, J.L.6
  • 34
    • 0031006074 scopus 로고    scopus 로고
    • Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells: Signal transduction by a protease-resistant toxin variant
    • Lencer, W.I., C. Constable, S. Moe, P.A. Rufo, A. Wolf, M.G. Jobling, S.P. Ruston, J.L. Madara, R.K. Holmes, and T.R. Hirst. 1997. Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells: signal transduction by a protease-resistant toxin variant. J. Biol. Chem. 272:15562-15568.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15562-15568
    • Lencer, W.I.1    Constable, C.2    Moe, S.3    Rufo, P.A.4    Wolf, A.5    Jobling, M.G.6    Ruston, S.P.7    Madara, J.L.8    Holmes, R.K.9    Hirst, T.R.10
  • 35
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M.P., P.E. Scherer, Z. Tang, and M. Sargiacomo. 1994. Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis. Trends Cell Biol. 4:231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.3    Sargiacomo, M.4
  • 36
    • 0030936016 scopus 로고    scopus 로고
    • Organized endothelial cell surface signal transduction in caveolae distinct from glycosylphosphatidylinositol-anchored protein microdomains
    • Liu, J., P. Oh, T. Horner, R.A. Rodgers, and J.E. Schnitzer. 1997. Organized endothelial cell surface signal transduction in caveolae distinct from glycosylphosphatidylinositol-anchored protein microdomains. J. Biol. Chem. 272: 7211-7222.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7211-7222
    • Liu, J.1    Oh, P.2    Horner, T.3    Rodgers, R.A.4    Schnitzer, J.E.5
  • 37
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vero cells
    • Majoul, I.V., P.I.H. Bastiaens, and H.-D. Soling. 1996. Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells. J. Cell Biol. 133: 777-789.
    • (1996) J. Cell Biol. , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.H.2    Soling, H.-D.3
  • 38
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor, S., and F.R. Maxfield. 1995. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell. 6:929-944.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 39
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
    • Montesanto, R., J. Roth, and L. Orci. 1982. Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins. Nature. 296:651-653.
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesanto, R.1    Roth, J.2    Orci, L.3
  • 40
    • 0031048978 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of the a subunit of cholera toxin in a human intestinal cell line
    • Orlandi, P.A. 1997. Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line. J. Biol. Chem. 272: 4591-4599.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4591-4599
    • Orlandi, P.A.1
  • 41
    • 0027314536 scopus 로고
    • Brefeldin a blocks the response of cultured cells to cholera toxin: Implications for intracellular trafficking in toxin action
    • Orlandi, P.A., P.K. Curran, and P.H. Fishman. 1993. Brefeldin A blocks the response of cultured cells to cholera toxin: implications for intracellular trafficking in toxin action. J. Biol. Chem. 268:12010-12016.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12010-12016
    • Orlandi, P.A.1    Curran, P.K.2    Fishman, P.H.3
  • 43
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides: GM1 is concentrated in caveolae
    • Parton, R.G. 1994. Ultrastructural localization of gangliosides: GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42:155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 44
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton, R.G., B. Joggerst, and K. Simons. 1994. Regulated internalization of caveolae. J. Cell Biol. 127:1199-1215.
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 45
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R.G., and K. Simons. 1995. Digging into caveolae. Science. 269:1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 46
    • 0030890789 scopus 로고    scopus 로고
    • Assembly and intracellular targeting of the βγ subunits of heterotrimeric G proteins
    • Rehm, A., and H.L. Ploegh. 1997. Assembly and intracellular targeting of the βγ subunits of heterotrimeric G proteins. J. Cell Biol. 137:305-317.
    • (1997) J. Cell Biol. , vol.137 , pp. 305-317
    • Rehm, A.1    Ploegh, H.L.2
  • 47
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p561ck associated with glycolipid-enriched membrane domains
    • Rodgers, W., and J.K. Rose. 1996. Exclusion of CD45 inhibits activity of p561ck associated with glycolipid-enriched membrane domains. J. Cell Biol. 135: 1515-1523.
    • (1996) J. Cell Biol. , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 48
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K.G., Y.-S. Ying, B.A. Kamen, and R.G.W. Anderson. 1990. Cholesterol controls the clustering of the glycospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol. 111:2931-2938.
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.-S.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 49
    • 0028352977 scopus 로고
    • Retrograde transport from the Golgi complex to the ER of both shiga toxin and the nontoxic shiga B-fragment is regulated by buteric acid and cAMP
    • Sandvig, K., M. Ryd, Ø. Garred, E. Schweda, P.K. Holm, and B. van Deurs. 1994. Retrograde transport from the Golgi complex to the ER of both shiga toxin and the nontoxic shiga B-fragment is regulated by buteric acid and cAMP. J. Cell Biol. 126:53-64.
    • (1994) J. Cell Biol. , vol.126 , pp. 53-64
    • Sandvig, K.1    Ryd, M.2    Garred, Ø.3    Schweda, E.4    Holm, P.K.5    Van Deurs, B.6
  • 50
    • 0028313982 scopus 로고
    • Thin-layer chromatography of glycosphingolipids
    • Schnaar, R.L., and L.K. Necdham. 1994. Thin-layer chromatography of glycosphingolipids. Methods Enzymol. 230:371-389.
    • (1994) Methods Enzymol. , vol.230 , pp. 371-389
    • Schnaar, R.L.1    Necdham, L.K.2
  • 51
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolaemediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer, J.E., P. Oh, E. Pinney, and J. Allard. 1994. Filipin-sensitive caveolaemediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127: 1217-1232.
    • (1994) J. Cell Biol. , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 52
    • 0029014820 scopus 로고
    • Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases
    • Schnitzer, J.E., J. Liu, and P. Oh. 1995a. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J. Biol. Chem. 270:14399-14404.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14399-14404
    • Schnitzer, J.E.1    Liu, J.2    Oh, P.3
  • 53
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer, J.E., D.P. McIntosh, A.M. Dvorak, J. Liu, and P. Oh. 1995b. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science. 269:1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 55
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer, J.E., P. Oh, and D.P. McIntosh. 1996. Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science. 274:239-242.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 56
    • 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., E. London, and D. Brown. 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
  • 57
    • 0017878781 scopus 로고
    • A model for ganglioside behavior in cell membranes
    • Sharom, F.J., and C.W.M. Grant. 1978. A model for ganglioside behavior in cell membranes. Biochim. Biophys. Acta. 507:280-293.
    • (1978) Biochim. Biophys. Acta , vol.507 , pp. 280-293
    • Sharom, F.J.1    Grant, C.W.M.2
  • 58
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 59
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 60
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K., and G. van Meer. 1988. Lipid sorting in epithelial cells. Biochemistry. 27:6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 61
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K, and A. Wandinger-Ness. 1990. Polarized sorting in epithelia. Cell. 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 63
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart, E.J., Y.-S. Ying, P.A. Conrad, and R.G. Anderson. 1994. Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation. J. Cell Biol. 127:1185-1197.
    • (1994) J. Cell Biol. , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.-S.2    Conrad, P.A.3    Anderson, R.G.4
  • 64
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
    • Spangler, B.D. 1992. Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol. Rev. 56:622-647.
    • (1992) Microbiol. Rev. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 66
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolac
    • Stang, E., J. Kartenbeck, and R.G. Parton. 1997. Major histocompatibility complex class I molecules mediate association of SV40 with caveolac. Mol. Biol. Cell. 8:47-57.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 68
    • 0028352175 scopus 로고
    • Large-scale coaggregation of fluorescent lipid probes with cell surface proteins
    • Thomas, J.L., D. Holowka, B. Baird, and W.W. Webb. 1994. Large-scale coaggregation of fluorescent lipid probes with cell surface proteins. J. Cell Biol. 125:795-802.
    • (1994) J. Cell Biol. , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 69
    • 0021979912 scopus 로고
    • Organization of glycosphingolipids in bilayers and plasma membranes of mammalian cells
    • Thompson, T.E., and T.W. Tillack. 1985. Organization of glycosphingolipids in bilayers and plasma membranes of mammalian cells. Annu. Rev. Biophys. Bioeng. 14:361-386.
    • (1985) Annu. Rev. Biophys. Bioeng. , vol.14 , pp. 361-386
    • Thompson, T.E.1    Tillack, T.W.2
  • 70
    • 0023449563 scopus 로고
    • Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway
    • Tran, D., J.-L. Carpentier, F. Sawano, P. Gorden, and L. Orci. 1987. Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway. Proc. Natl. Acad. Sci. USA. 84:7956-7961.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7956-7961
    • Tran, D.1    Carpentier, J.-L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 72
    • 0027316267 scopus 로고
    • Lipid sorting - Measurement and interpretation
    • van Genderen, I.L., and G. van Meer. 1993. Lipid sorting - measurement and interpretation. Biochem. Soc. Trans. 21:235-239.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 235-239
    • Van Genderen, I.L.1    Van Meer, G.2
  • 73
    • 0027640552 scopus 로고
    • Transport and sorting of membrane lipids
    • van Meer, G. 1993. Transport and sorting of membrane lipids. Curr. Opin. Cell Biol. 5:661-673.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 661-673
    • Van Meer, G.1


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