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Volumn 159, Issue 2, 2002, Pages 207-215

Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

Author keywords

Cholera toxin; Ero1; Oxidation; PDI; Retrotranslocation

Indexed keywords

CHOLERA TOXIN; ISOENZYME; PROTEIN DERIVATIVE; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERO1; UNCLASSIFIED DRUG;

EID: 0037191074     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200207120     Document Type: Article
Times cited : (128)

References (18)
  • 1
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli, T., M. Alessio, A. Mezghrani, T. Simmen, F. Talamo, A. Bachi, and R. Sitia. 2002. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBOJ. 21:835-844.
    • (2002) EMBO J. , vol.21 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 3
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A.R., and C.A. Kaiser. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1: 161-170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 4
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand, A.R., and C.A. Kaiser. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4:469-477.
    • (1999) Mol. Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 5
    • 0033611127 scopus 로고    scopus 로고
    • Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
    • Gillece, P., J.M. Luz, W.J. Lennarz, F.J. de La Cruz, and K. Romisch. 1999. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J. Cell Biol. 147:1443-1456.
    • (1999) J. Cell Biol. , vol.147 , pp. 1443-1456
    • Gillece, P.1    Luz, J.M.2    Lennarz, W.J.3    De La Cruz, F.J.4    Romisch, K.5
  • 6
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Gorlich, D., and T.A. Rapoport. 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
    • Gorlich, D.1    Rapoport, T.A.2
  • 7
    • 0030807389 scopus 로고    scopus 로고
    • Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum
    • Holst, B., C. Tachibana, and J.R. Winther. 1997. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J. Cell Biol. 138:1229-1238.
    • (1997) J. Cell Biol. , vol.138 , pp. 1229-1238
    • Holst, B.1    Tachibana, C.2    Winther, J.R.3
  • 8
    • 0033055636 scopus 로고    scopus 로고
    • Membrane traffic and the cellular uptake of cholera toxin
    • Lencer, W.I., T.R. Hirst, and R.K. Holmes. 1999. Membrane traffic and the cellular uptake of cholera toxin. Biochim. Biophys. Acta. 1450:177-190.
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 177-190
    • Lencer, W.I.1    Hirst, T.R.2    Holmes, R.K.3
  • 9
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K.E., W. Mothes, and T.A. Rapoport. 1998. Protein translocation: Tunnel vision. Cell. 92:381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.1    Mothes, W.2    Rapoport, T.A.3
  • 10
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani, M., M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N.J. Bulleid, A. Cabibbo, and R. Sitia. 2000. Endoplasmic reticulum oxidoreductin 1-1beta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275:23685-23692.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 11
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard, M.G., K.J. Travers, and J.S. Weissman. 1998. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 1:171-182.
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 12
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the Sec61p complex
    • Schmitz, A., H. Herrgen, A. Winkeler, and V. Herzog. 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
  • 13
    • 0029942531 scopus 로고    scopus 로고
    • Enteric bacterial toxins: Mechanisms of action and linkage to intestinal secretion
    • Sears, C.L., and J.B. Kaper. 1996. Enteric bacterial toxins: Mechanisms of action and linkage to intestinal secretion. Microbiol. Rev. 60:167-215.
    • (1996) Microbiol. Rev. , vol.60 , pp. 167-215
    • Sears, C.L.1    Kaper, J.B.2
  • 14
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., C. Rodighiero, W.I. Lencer, and T.A. Rapoport. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell. 104:937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 15
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Y. Ye, and T.A. Rapoport. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3:246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 16
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu, B.P., S.C. Ho-Schleyer, K.J. Travers, and J.S. Weissman. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 290: 1571-1574.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 17
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang, Q., and A. Chang. 1999. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18:5972-5982.
    • (1999) EMBO J. , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 18
    • 0033525472 scopus 로고    scopus 로고
    • Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo
    • Westphal, V., N.J. Darby, and J.R. Winther. 1999. Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo. J. Mol. Biol. 286:1229-1239.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1229-1239
    • Westphal, V.1    Darby, N.J.2    Winther, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.