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Volumn 22, Issue 19, 2003, Pages 5015-5022

Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44

Author keywords

Disulfide bond formation; IgM polymerization; Protein secretion; Quality control; Redox regulation

Indexed keywords

CYSTEINE; OLIGOMER; PROTEIN ERO1 ALPHA; PROTEIN ERP44; SECRETORY PROTEIN; THIOL; UNCLASSIFIED DRUG;

EID: 0141753993     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg491     Document Type: Article
Times cited : (198)

References (34)
  • 1
    • 0025146994 scopus 로고
    • Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
    • Alberini, C.M., Bet, P., Milstein, C. and Sitia, R. (1990) Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature, 347, 485-487.
    • (1990) Nature , vol.347 , pp. 485-487
    • Alberini, C.M.1    Bet, P.2    Milstein, C.3    Sitia, R.4
  • 2
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli, T., Alessio, M., Mezghrani, A., Simmen, T., Talamo, F., Bachi, A. and Sitia, R. (2002) ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J., 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
  • 4
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M.R., Bulleid, N.J. and Sitia, R. (2000) ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem., 275, 4827-4833.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4827-4833
    • Cabibbo, A.1    Pagani, M.2    Fabbri, M.3    Rocchi, M.4    Farmery, M.R.5    Bulleid, N.J.6    Sitia, R.7
  • 5
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard, L. and Helenius, A. (2001) ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol., 13, 431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 6
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol., 3, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 7
    • 0035798550 scopus 로고    scopus 로고
    • Reduction of inter-chain disulfide bonds precedes the dislocation of Ig-μ chains from the endoplasmic reticulum to the cytosol for proteasomal degradation
    • Fagioli, C., Mezghrani, A. and Sitia, R. (2001) Reduction of inter-chain disulfide bonds precedes the dislocation of Ig-μ chains from the endoplasmic reticulum to the cytosol for proteasomal degradation. J. Biol. Chem., 276, 40962-40967.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40962-40967
    • Fagioli, C.1    Mezghrani, A.2    Sitia, R.3
  • 8
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • Fassio, A. and Sitia, R. (2002) Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum. Histochem. Cell Biol., 117, 151-157.
    • (2002) Histochem. Cell Biol. , vol.117 , pp. 151-157
    • Fassio, A.1    Sitia, R.2
  • 9
    • 0027440769 scopus 로고
    • Quality control of ER synthetized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra, A., Fagioli, C., Finazzi, D., Sitia, R. and Alberini, C. (1993) Quality control of ER synthetized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J., 12, 4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.5
  • 10
    • 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 Kaiser, C.A. (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
  • 11
    • 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 Kaiser, C.A. (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
  • 12
    • 0023096246 scopus 로고
    • Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein
    • Hendershot, L., Bole, D., Kohler, G. and Kearney, J.F. (1987) Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein. J. Cell Biol., 104, 761-767.
    • (1987) J. Cell Biol. , vol.104 , pp. 761-767
    • Hendershot, L.1    Bole, D.2    Kohler, G.3    Kearney, J.F.4
  • 14
    • 0029908325 scopus 로고    scopus 로고
    • Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval
    • Isidoro, C., Maggioni, C., Demoz, M., Pizzagalli, A., Fra, A.M. and Sitia, R. (1996) Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval. J. Biol. Chem., 271, 26138-26142.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26138-26142
    • Isidoro, C.1    Maggioni, C.2    Demoz, M.3    Pizzagalli, A.4    Fra, A.M.5    Sitia, R.6
  • 15
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens, A., van Duijn, E. and Braakman, I. (2002) Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science, 298, 2401-2403.
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1    Van Duijn, E.2    Braakman, I.3
  • 16
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dul, J.L. and Argon, Y. (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature, 370, 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 17
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier, L., Usherwood, Y.K., Chung, K.T. and Hendershot, L.M. (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell, 13, 4456-4469.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 18
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani, A., Fassio, A., Benham, A., Simmen, T., Braakman, I. and Sitia, R. (2001) Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J., 20, 6288-6296.
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 19
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-1β (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
    • Pagani, M., Fabbri, M., Benedetti, C., Fassio, A., Pilati, S., Bulleid, N.J., Cabibbo, A. and Sitia, R. (2000) Endoplasmic reticulum oxidoreductin 1-1β (ERO1-Lβ), 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
  • 20
    • 0035834372 scopus 로고    scopus 로고
    • The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function
    • Pagani, M., Pilati, S., Bertoli, G., Valsasina, B. and Sitia, R. (2001) The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. FEBS Lett., 508, 117-120.
    • (2001) FEBS Lett. , vol.508 , pp. 117-120
    • Pagani, M.1    Pilati, S.2    Bertoli, G.3    Valsasina, B.4    Sitia, R.5
  • 21
    • 0027489133 scopus 로고
    • Sorting of membrane proteins in the secretory pathway
    • Pelham, H.R. and Munro, S. (1993) Sorting of membrane proteins in the secretory pathway. Cell, 75, 603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.1    Munro, S.2
  • 22
    • 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., Travers, K.J. and Weissman, J.S. (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
  • 23
    • 0033485791 scopus 로고    scopus 로고
    • The contribution of ER quality control to the biologic functions of secretory IgM
    • Reddy, P.S. and Corley, R.B. (1999) The contribution of ER quality control to the biologic functions of secretory IgM. Immunol. Today, 20, 582-588.
    • (1999) Immunol. Today , vol.20 , pp. 582-588
    • Reddy, P.S.1    Corley, R.B.2
  • 24
    • 0029944851 scopus 로고    scopus 로고
    • Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains
    • Reddy, P., Sparvoli, A., Fagioli, C., Fassina, G. and Sitia, R. (1996) Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. EMBO J., 15, 2077-2085.
    • (1996) EMBO J. , vol.15 , pp. 2077-2085
    • Reddy, P.1    Sparvoli, A.2    Fagioli, C.3    Fassina, G.4    Sitia, R.5
  • 25
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem., 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 26
  • 27
    • 0032572582 scopus 로고    scopus 로고
    • Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential
    • Tortorella, D., Story, C.M., Huppa, J.B., Wiertz, E., Jones, T.R. and Ploegh, H.L. (1998) Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential. J. Cell Biol., 142, 365-376.
    • (1998) J. Cell Biol. , vol.142 , pp. 365-376
    • Tortorella, D.1    Story, C.M.2    Huppa, J.B.3    Wiertz, E.4    Jones, T.R.5    Ploegh, H.L.6
  • 28
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1
    • Tsai, B. and Rapoport, T.A. (2002) Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J. Cell Biol., 159, 207-216.
    • (2002) J. Cell Biol. , vol.159 , pp. 207-216
    • Tsai, B.1    Rapoport, T.A.2
  • 29
    • 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.A. (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
  • 30
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y. and Rapoport, TA. (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
  • 31
    • 0028588562 scopus 로고
    • The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi
    • Valetti, C. and Sitia, R. (1994) The differential effects of dithiothreitol and 2-mercaptoethanol on the secretion of partially and completely assembled immunoglobulins suggest that thiol-mediated retention does not take place in or beyond the Golgi. Mol. Biol. Cell, 5, 1311-1324.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1311-1324
    • Valetti, C.1    Sitia, R.2
  • 32
    • 0026347810 scopus 로고
    • Russell bodies: A general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum
    • Valetti, C., Grossi, C.E., Milstein, C. and Sitia, R. (1991) Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J. Cell Biol., 115, 983-994.
    • (1991) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Grossi, C.E.2    Milstein, C.3    Sitia, R.4
  • 33
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • vanAnken, E., Romijn, E.P., Maggioni, C., Mezgrhani, A., Sitia, R., Braakman, I. and Heck, A.J.R. (2003) Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity, 18, 243-253.
    • (2003) Immunity , vol.18 , pp. 243-253
    • VanAnken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezgrhani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.R.7
  • 34
    • 0034213595 scopus 로고    scopus 로고
    • ProFound: An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang, W. and Chait, B.T. (2000) ProFound: an expert system for protein identification using mass spectrometric peptide mapping information. Anal. Chem., 72, 2482-2489.
    • (2000) Anal. Chem. , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2


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