메뉴 건너뛰기




Volumn 14, Issue 12, 2003, Pages 4783-4793

Gangliosides That Associate with Lipid Rafts Mediate Transport of Cholera and Related Toxins from the Plasma Membrane to Endoplasmic Reticulm

Author keywords

[No Author keywords available]

Indexed keywords

CHOLERA TOXIN; ESCHERICHIA COLI ENDOTOXIN; GANGLIOSIDE;

EID: 10744224620     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-06-0354     Document Type: Article
Times cited : (198)

References (45)
  • 1
    • 0034724182 scopus 로고    scopus 로고
    • Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
    • Bagnat, M., Keranen, S., Shevchenko, A., and Simons, K. (2000). Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc. Natl. Acad. Sci. USA 97, 3254-3259.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3254-3259
    • Bagnat, M.1    Keranen, S.2    Shevchenko, A.3    Simons, K.4
  • 2
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens, P.I.H., Majoul, I.V., Verveer, P.J., Söling, H.-D., and Jovin, T.M. (1996). Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J. 15, 4246-4253.
    • (1996) EMBO J. , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.H.1    Majoul, I.V.2    Verveer, P.J.3    Söling, H.-D.4    Jovin, T.M.5
  • 3
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D., and London, E. (2000). Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.1    London, E.2
  • 4
    • 0030820910 scopus 로고    scopus 로고
    • New consensus features for tyrosine O-sulfation determined by mutational analysis
    • Bundgaard, J.R., Vuust, J., and Rehfeld, J.F. (1997). New consensus features for tyrosine O-sulfation determined by mutational analysis. J. Biol. Chem. 272, 21700-21705.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21700-21705
    • Bundgaard, J.R.1    Vuust, J.2    Rehfeld, J.F.3
  • 5
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of shiga toxin b-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguieres, T., Mallard, F., Baron, C., Hanau, D., Lingwood, C., Goud, B., Salamero, J., and Johannes, L. (2001). Targeting of shiga toxin b-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 12, 2453-2468.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguieres, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5    Goud, B.6    Salamero, J.7    Johannes, L.8
  • 7
    • 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., Magnani, J.L., Twiddy, E.M., Holmes, R.K., and Ginsburg, V. (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
  • 8
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., and von Heijne, G. (1990). Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3, 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 9
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Gorlick, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Gorlick, D.1    Rapoport, T.A.2
  • 10
    • 0030886889 scopus 로고    scopus 로고
    • Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells
    • Hazes, B., and Read, R.J. (1997). Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells. Biochemistry 36, 11051-11054.
    • (1997) Biochemistry , vol.36 , pp. 11051-11054
    • Hazes, B.1    Read, R.J.2
  • 11
    • 0025783927 scopus 로고
    • Analysis of structure and function of the B subunit of cholera toxin by the use of site-directed mutagenesis
    • Jobling, M.G., and Holmes, R.K. (1991). Analysis of structure and function of the B subunit of cholera toxin by the use of site-directed mutagenesis. Mol. Microbiol. 5, 1755-1767.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1755-1767
    • Jobling, M.G.1    Holmes, R.K.2
  • 12
    • 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., Palmer, L.M., Erbe, J.L., and Holmes, R.K. (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
  • 13
    • 0030876616 scopus 로고    scopus 로고
    • Retrograde transport of KDEL-bearing B-fragment of shiga toxin
    • Johannes, L., Tenza, D., Antony, C., and Goud, B. (1997). Retrograde transport of KDEL-bearing B-fragment of shiga toxin. J. Biol. Chem. 272, 19554-19561.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19554-19561
    • Johannes, L.1    Tenza, D.2    Antony, C.3    Goud, B.4
  • 14
    • 0025909488 scopus 로고
    • Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins
    • Lee, C.-M., Chang, P.P., Tsai, S.-C., Adamik, R., Price, S.R., Kunz, B.C., Moss, J., Twiddy, E.M., and Holmes, R.K. (1991). Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins. J. Clin. Investig. 87, 1780-1786.
    • (1991) J. Clin. Investig. , 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
  • 15
    • 0028244642 scopus 로고
    • Tagging secretory and membrane proteins with a tyrosine sulfation site. Tyrosine sulfation precedes galactosylation and sialylation in COS-7 cells
    • Leitinger, B., Brown, J.L., and Spiess, M. (1994). Tagging secretory and membrane proteins with a tyrosine sulfation site. Tyrosine sulfation precedes galactosylation and sialylation in COS-7 cells. J. Biol. Chem. 269, 8115-8121.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8115-8121
    • Leitinger, B.1    Brown, J.L.2    Spiess, M.3
  • 16
    • 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., de Almeida, J.B., Moe, S., Stow, J.L., Ausiello, D.A., and Madara, J.L. (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. Investig. 92, 2941-2951.
    • (1993) J. Clin. Investig. , 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
  • 18
    • 0032476577 scopus 로고    scopus 로고
    • KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from Golgi involves COPI, p23, and the COOH terminus of Erd2p
    • Majoul, I., Sohn, K., Wieland, F.T., Pepperkok, R., Pizza, M., Hillemann, J., and Söling, H.-D. (1998). KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from Golgi involves COPI, p23, and the COOH terminus of Erd2p. J. Cell Biol. 143, 601-612.
    • (1998) J. Cell Biol. , vol.143 , pp. 601-612
    • Majoul, I.1    Sohn, K.2    Wieland, F.T.3    Pepperkok, R.4    Pizza, M.5    Hillemann, J.6    Söling, H.-D.7
  • 19
    • 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., Bastiaens, P.I.H., and Söling, H.-D. (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    Söling, H.-D.3
  • 20
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols, B.J. (2002). A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat. Cell Biol 4, 374-378.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 21
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • Nichols, B.J. (2003). GM1-containing lipid rafts are depleted within clathrin-coated pits. Curr. Biol. 13, 686-690.
    • (2003) Curr. Biol. , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 23
    • 0027314536 scopus 로고
    • Brefeldin A blocks the response of cultured cells to cholera toxin: Implications for intracellular trafficking in toxin action
    • Orlandi, P.A., Curran, P.K., and Fishman, P.H. (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
  • 24
    • 0031750101 scopus 로고    scopus 로고
    • Fihpin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi, P.A., and Fishman, P.H. (1998). Fihpin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 141, 905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 25
    • 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
  • 26
    • 0031964547 scopus 로고    scopus 로고
    • Cell surface glycoproteins undergo postbiosynthetic modification of their N-glycans by stepwise demannosylation
    • Porwoll, S., Loch, N., Kannicht, C., Nuck, R., Grunow, D., Reutter, W., and Tauber, R. (1998). Cell surface glycoproteins undergo postbiosynthetic modification of their N-glycans by stepwise demannosylation. J. Biol. Chem. 273, 1075-1085.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1075-1085
    • Porwoll, S.1    Loch, N.2    Kannicht, C.3    Nuck, R.4    Grunow, D.5    Reutter, W.6    Tauber, R.7
  • 27
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to the cytosol
    • Rapak, A., Falnes, P.Ø., and Olsnes, S. (1997). Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to the cytosol. Proc. Natl. Acad. Sci. USA 94, 3783-3788.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.Ø.2    Olsnes, S.3
  • 28
    • 0036000023 scopus 로고    scopus 로고
    • Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection
    • Richards, A.A., Stang, E., Pepperkok, R., and Parton, R.G. (2002). Inhibitors of COP-mediated transport and cholera toxin action inhibit simian virus 40 infection. Mol. Biol. Cell 13, 1750-1764.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1750-1764
    • Richards, A.A.1    Stang, E.2    Pepperkok, R.3    Parton, R.G.4
  • 29
    • 12244305596 scopus 로고    scopus 로고
    • Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation
    • Rodighiero, C., Tsai, B., Rapoport, T.A., and Lencer, W.I. (2002). Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation. EMBO Rep. 3, 1222-1227.
    • (2002) EMBO Rep. , vol.3 , pp. 1222-1227
    • Rodighiero, C.1    Tsai, B.2    Rapoport, T.A.3    Lencer, W.I.4
  • 30
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • Sabharanjak, S., Sharma, P., Parton, R.G., and Mayor, S. (2002). GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell 2, 411-423.
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 31
    • 0029909329 scopus 로고    scopus 로고
    • Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin
    • Sandvig, K., and van Deurs, B. (1996). Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin. Physiol. Rev. 76, 949-966.
    • (1996) Physiol. Rev. , vol.76 , pp. 949-966
    • Sandvig, K.1    Van Deurs, B.2
  • 32
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the sec61p complex
    • Schmitz, A., Herrgen, H., Winkeler, A., and Herzog, V. (2000). Cholera toxin is exported from microsomes by the sec61p complex. J. Cell Biol. 148, 1203-1212.
    • (2000) J. Cell Biol. , vol.148 , pp. 1203-1212
    • Schmitz, A.1    Herrgen, H.2    Winkeler, A.3    Herzog, V.4
  • 33
    • 0035937752 scopus 로고    scopus 로고
    • Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism
    • Shogomori, H., and Futerman, A.H. (2001a). Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism. J. Biol. Chem. 276, 9182-9188.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9182-9188
    • Shogomori, H.1    Futerman, A.H.2
  • 34
    • 0034851545 scopus 로고    scopus 로고
    • Cholesterol depletion by methyl-beta-cyclodextrin blocks cholera toxin transport from endosomes to the Golgi apparatus in hippocampal neurons
    • Shogomori, H., and Futerman, A.H. (2001b). Cholesterol depletion by methyl-beta-cyclodextrin blocks cholera toxin transport from endosomes to the Golgi apparatus in hippocampal neurons. J. Neurochem. 78, 991-999.
    • (2001) J. Neurochem. , vol.78 , pp. 991-999
    • Shogomori, H.1    Futerman, A.H.2
  • 35
    • 0027174854 scopus 로고
    • Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin
    • Sixma, T.K., Kalk, K.H., van Zanten, B.A., Dauter, Z., Kingma, J., Witholt, B., and Hol, W.G. (1993). Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. J. Mol. Biol. 230, 890-918.
    • (1993) J. Mol. Biol. , vol.230 , pp. 890-918
    • Sixma, T.K.1    Kalk, K.H.2    Van Zanten, B.A.3    Dauter, Z.4    Kingma, J.5    Witholt, B.6    Hol, W.G.7
  • 36
    • 0036839684 scopus 로고    scopus 로고
    • Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway
    • Teter, K., Allyn, R.L., Jobling, M.G., and Holmes, R.K. (2002). Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway. Infect. Immun. 70, 6166-6171.
    • (2002) Infect. Immun. , vol.70 , pp. 6166-6171
    • Teter, K.1    Allyn, R.L.2    Jobling, M.G.3    Holmes, R.K.4
  • 37
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Erol
    • Tsai, B., and Rapoport, T. (2002). Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Erol. J. Cell Biol. 159, 207-215.
    • (2002) J. Cell Biol. , vol.159 , pp. 207-215
    • Tsai, B.1    Rapoport, T.2
  • 38
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W.I., and Rapoport, T. (2001). Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 304, 937-948.
    • (2001) Cell , vol.304 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.4
  • 40
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: Rafts and translocators
    • van Meer, G., and Lisman, Q. (2002). Sphingolipid transport: rafts and translocators. J. Biol. Chem. 277, 25855-25858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25855-25858
    • Van Meer, G.1    Lisman, Q.2
  • 41
    • 0029129121 scopus 로고
    • Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells
    • Volz, B., Orberger, G., Porwoll, S., Hauri, H.P., and Tauber, R. (1995). Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells. J. Cell Biol. 330, 537-551.
    • (1995) J. Cell Biol. , vol.330 , pp. 537-551
    • Volz, B.1    Orberger, G.2    Porwoll, S.3    Hauri, H.P.4    Tauber, R.5
  • 42
    • 0037013269 scopus 로고    scopus 로고
    • Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol
    • Wolf, A.A., Fujinaga, Y., and Lencer, W.I. (2002). Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol. J. Biol. Chem. 277, 16249-16256.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16249-16256
    • Wolf, A.A.1    Fujinaga, Y.2    Lencer, W.I.3
  • 43
    • 0031802210 scopus 로고    scopus 로고
    • Ganglioside structure dictates signal transduction by cholera toxin in polarized epithelia and association with caveolae-like membrane domains
    • Wolf, A.A., Jobling, M.G., Wimer-Mackin, S., Madara, J.L., Holmes, R.K., and Lencer, W.I. (1998). Ganglioside structure dictates signal transduction by cholera toxin in polarized epithelia and association with caveolae-like membrane domains. J. Cell Biol. 141, 917-927.
    • (1998) J. Cell Biol. , vol.141 , pp. 917-927
    • Wolf, A.A.1    Jobling, M.G.2    Wimer-Mackin, S.3    Madara, J.L.4    Holmes, R.K.5    Lencer, W.I.6
  • 44
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.