메뉴 건너뛰기




Volumn 109, Issue 9, 1996, Pages 2383-2392

Quality control in protein biogenesis: Thiol-mediated retention monitors the redox state of proteins in the endoplasmic reticulum

Author keywords

Endoplasmic reticulum; IgM; Quality control; Secretion; Thiol mediated retention

Indexed keywords

CYSTEINE; IMMUNOGLOBULIN M; SECRETORY IMMUNOGLOBULIN;

EID: 0029843715     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (46)
  • 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
    • 0022379572 scopus 로고
    • Major carbohydrate structures at five glycosylation sites on murine IgM determined by high resolution 1H-NMR spectroscopy
    • Anderson, D. R., Atkinson, P. H. and Grimes, W. J. (1985). Major carbohydrate structures at five glycosylation sites on murine IgM determined by high resolution 1H-NMR spectroscopy. Arch. Biochem. Biophys. 243, 605-618.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 605-618
    • Anderson, D.R.1    Atkinson, P.H.2    Grimes, W.J.3
  • 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
  • 6
    • 0001321260 scopus 로고
    • Complement fixation on cell surfaces by 19S and 7S antibodies
    • Borsos, T. and Rapp, H. J. (1965). Complement fixation on cell surfaces by 19S and 7S antibodies. Science 150, 505-506.
    • (1965) Science , vol.150 , pp. 505-506
    • Borsos, T.1    Rapp, H.J.2
  • 8
    • 0028200169 scopus 로고
    • Mechanism and subcellular localization of secretory IgM polymer assembly
    • Brewer, J. W., Randall, T. D., Parkhouse, R. M. E. and Corley, R. B. (1994b). Mechanism and subcellular localization of secretory IgM polymer assembly. J. Biol. Chem. 269, 17338-17348.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17338-17348
    • Brewer, J.W.1    Randall, T.D.2    Parkhouse, R.M.E.3    Corley, R.B.4
  • 9
    • 0029986845 scopus 로고    scopus 로고
    • Igm polymerization inhibits the Golgi-mediated processing of the μ-chain carboxy-terminal glycans
    • Cals, M. M., Guenzi, S., Cavelli, S., Simmen, T., Sparvoli, A. and Sitia, R. (1996). Igm polymerization inhibits the Golgi-mediated processing of the μ-chain carboxy-terminal glycans. Mol. Immunol. 33, 15-24.
    • (1996) Mol. Immunol. , vol.33 , pp. 15-24
    • Cals, M.M.1    Guenzi, S.2    Cavelli, S.3    Simmen, T.4    Sparvoli, A.5    Sitia, R.6
  • 10
    • 0023403373 scopus 로고
    • Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain
    • Cattaneo, A. and Neuberger, M. S. (1987). Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain. EMRO J. 6, 2753-2758.
    • (1987) EMRO J. , vol.6 , pp. 2753-2758
    • Cattaneo, A.1    Neuberger, M.S.2
  • 11
    • 0027322942 scopus 로고
    • Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathway
    • Chanat, E., Weiss, U., Huttner, W. B. and Tooze, S. A. (1993). Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathway. EMBO J. 12, 2159-2168.
    • (1993) EMBO J. , vol.12 , pp. 2159-2168
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3    Tooze, S.A.4
  • 12
    • 0024792674 scopus 로고
    • Diversity in the available repertoire of murine antibodies reactive with bromelain-treated isologous erythrocytes
    • Conger, J. D., Sage, H. J. and Corley, R. B. (1989). Diversity in the available repertoire of murine antibodies reactive with bromelain-treated isologous erythrocytes. J. Immunol. 143, 4044-4052.
    • (1989) J. Immunol. , vol.143 , pp. 4044-4052
    • Conger, J.D.1    Sage, H.J.2    Corley, R.B.3
  • 14
    • 0024505096 scopus 로고
    • Differential glycosylation of polymeric and monomeric IgM
    • Davis, A. C., Collins, C. and Shulman, M. J. (1989). Differential glycosylation of polymeric and monomeric IgM. Mol. Immunol. 26, 147-152.
    • (1989) Mol. Immunol. , vol.26 , pp. 147-152
    • Davis, A.C.1    Collins, C.2    Shulman, M.J.3
  • 15
    • 0024591335 scopus 로고
    • IgM -Molecular requirements for its assembly and function
    • Davis, A. C. and Shulman, M. J. (1989). IgM -Molecular requirements for its assembly and function. Immunol. Today 10, 118-128.
    • (1989) Immunol. Today , vol.10 , pp. 118-128
    • Davis, A.C.1    Shulman, M.J.2
  • 16
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: An exposed thiol group is a three-way switch mediating assembly, retention and degradation
    • Fra, A. M., Fagioli, C., Finazzi, D., Sitia, R. and Alberini, C. M. (1993). Quality control of ER synthesized proteins: an exposed thiol group is a three-way switch mediating assembly, retention and degradation. EMBO J. 12, 4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.M.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.M.5
  • 17
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M. J., McCammon, K. and Sambrook, J. (1986). Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46, 939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 18
    • 0028168233 scopus 로고
    • The efficiency of cysteine-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells
    • Guenzi, S., Fra, A. M., Sparvoli, A., Bet, P., Rocco, M. and Sitia, R. (1994). The efficiency of cysteine-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells. Eur. J. Immmunol. 24, 2477-2482.
    • (1994) Eur. J. Immmunol. , vol.24 , pp. 2477-2482
    • Guenzi, S.1    Fra, A.M.2    Sparvoli, A.3    Bet, P.4    Rocco, M.5    Sitia, R.6
  • 19
    • 0028110180 scopus 로고
    • BiP (GRP78), an essential Hsp70 resident protein in the endoplasmic reticulum
    • Haas, I. G. (1994). BiP (GRP78), an essential Hsp70 resident protein in the endoplasmic reticulum. Experentia 50, 1012-1020.
    • (1994) Experentia , vol.50 , pp. 1012-1020
    • Haas, I.G.1
  • 20
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C. and Helenius, A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 21
    • 0025007007 scopus 로고
    • Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition
    • Hendershot, L. M. (1990). Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition. J. Cell Biol. 111, 829-837.
    • (1990) J. Cell Biol. , vol.111 , pp. 829-837
    • Hendershot, L.M.1
  • 22
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M. and Helenius, A. (1989). Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 23
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A. J. and Lodish, H. F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 24
    • 0016322151 scopus 로고
    • Intracellular J chain in mouse plasmacytomas secreting IgA, IgM and IgG
    • Kaji, H. and Parkhouse, R. M. E. (1974). Intracellular J chain in mouse plasmacytomas secreting IgA, IgM and IgG. Nature 249, 45-47.
    • (1974) Nature , vol.249 , pp. 45-47
    • Kaji, H.1    Parkhouse, R.M.E.2
  • 25
    • 0027530614 scopus 로고
    • Interrelations between assembly and secretion of recombinant human acetylcholinesterase
    • Kerem, A., Kronman, C., Bar-Nun, S., Shafferman, A. and Velan, B. (1993). Interrelations between assembly and secretion of recombinant human acetylcholinesterase. J. Biol. Chem. 268, 180-184.
    • (1993) J. Biol. Chem. , vol.268 , pp. 180-184
    • Kerem, A.1    Kronman, C.2    Bar-Nun, S.3    Shafferman, A.4    Velan, B.5
  • 27
    • 0022327488 scopus 로고
    • The coming of age of the immunoglobulin J chain
    • Koshland, M. E. (1985). The coming of age of the immunoglobulin J chain. Annu. Rev. Immunol. 3, 425-453.
    • (1985) Annu. Rev. Immunol. , vol.3 , pp. 425-453
    • Koshland, M.E.1
  • 28
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface
    • Kreis, T. E. and Lodish, H. F. (1986). Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46, 929-937.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodish, H.F.2
  • 29
    • 0022395244 scopus 로고
    • Antigen-nonspecific T cell derived factors in B cell activation; differences in the requirements for interleukin 2 in responses of unprimed and primed B cells
    • Kuhara, T., Haughton, G. and Corley, R. B. (1985). Antigen-nonspecific T cell derived factors in B cell activation; differences in the requirements for interleukin 2 in responses of unprimed and primed B cells. Eur. J. Immunol. 15, 787-793.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 787-793
    • Kuhara, T.1    Haughton, G.2    Corley, R.B.3
  • 30
    • 0022272544 scopus 로고
    • Immunoglobulin A (IgA)
    • Mestecky, J. and Kilian, M. (1985). Immunoglobulin A (IgA). Meth. Enzymol. 116, 37-75.
    • (1985) Meth. Enzymol. , vol.116 , pp. 37-75
    • Mestecky, J.1    Kilian, M.2
  • 31
    • 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. Nat. Acad. Sci. USA 90, 5732-5736.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 5732-5736
    • Mizuno, M.1    Singer, S.J.2
  • 32
    • 0020973560 scopus 로고
    • Biosynthesis, processing, and function of secretory component
    • Mostov, K. E. and Blobel, G. (1983). Biosynthesis, processing, and function of secretory component. Meth. Enzymol. 98, 458-466.
    • (1983) Meth. Enzymol. , vol.98 , pp. 458-466
    • Mostov, K.E.1    Blobel, G.2
  • 33
    • 0023176828 scopus 로고
    • Quantitation of cell surface molecules on a differentiating Ly-1+ B cell lymphoma
    • Ovnic, M. and Corley, R. B. (1987). Quantitation of cell surface molecules on a differentiating Ly-1+ B cell lymphoma. J. Immunol. 138, 3075-3082.
    • (1987) J. Immunol. , vol.138 , pp. 3075-3082
    • Ovnic, M.1    Corley, R.B.2
  • 34
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham, H. R. B. (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.B.1
  • 35
    • 0025006089 scopus 로고
    • The biological effects of IgM hexamer formation
    • Randall, T. D., King, L. B. and Corley, R. B. (1990). The biological effects of IgM hexamer formation. Eur. J. Immunol. 20, 1971-1979.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 1971-1979
    • Randall, T.D.1    King, L.B.2    Corley, R.B.3
  • 36
    • 0026597551 scopus 로고
    • J chain synthesis and secretion of hexameric IgM is differentially regulated by LPS and IL-5
    • Randall, T. D., Parkhouse, R. M. E. and Corley, R. B. (1992). J chain synthesis and secretion of hexameric IgM is differentially regulated by LPS and IL-5. Proc. Nat. Acad. Sci. USA 89, 962-966.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 962-966
    • Randall, T.D.1    Parkhouse, R.M.E.2    Corley, R.B.3
  • 37
    • 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
  • 38
    • 0020037889 scopus 로고
    • Immunocytochemical localization of galactosyl-transferase in HeLa cells: Codistribution with thiamine phyrophosphatase in trans-Golgi cysternae
    • Roth, J. and Berger, E. G. (1982). Immunocytochemical localization of galactosyl-transferase in HeLa cells: codistribution with thiamine phyrophosphatase in trans-Golgi cysternae. J. Cell Biol. 92, 223-229.
    • (1982) J. Cell Biol. , vol.92 , pp. 223-229
    • Roth, J.1    Berger, E.G.2
  • 39
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 40
    • 0026486823 scopus 로고
    • Polymerization of secretory IgM in B lymphocytes is prevented by a prior targeting to a degradation pathway
    • Shachar, I., Amitay, R., Rabinovich, E., Haimovich, J. and Bar-Nun, S. (1992). Polymerization of secretory IgM in B lymphocytes is prevented by a prior targeting to a degradation pathway. J. Biol. Chem. 267, 24241-24247.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24241-24247
    • Shachar, I.1    Amitay, R.2    Rabinovich, E.3    Haimovich, J.4    Bar-Nun, S.5
  • 41
    • 0028104975 scopus 로고
    • Thiol-reducing agents and calcium perturbants alter intracellular sorting of immunoglobulin M
    • Shachar, I., Rabinovich, E., Kerem, A. and Bar-Nun, S. (1994). Thiol-reducing agents and calcium perturbants alter intracellular sorting of immunoglobulin M. J. Biol. Chem. 269, 27344-27350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27344-27350
    • Shachar, I.1    Rabinovich, E.2    Kerem, A.3    Bar-Nun, S.4
  • 42
  • 43
    • 0018582566 scopus 로고
    • Plasma cell immunoglobulin M molecules. Their biosynthesis, assembly and intracellular transport
    • Tartakoff, A. and Vassalli, P. (1979). Plasma cell immunoglobulin M molecules. Their biosynthesis, assembly and intracellular transport. J. Cell Biol. 83, 284-299.
    • (1979) J. Cell Biol. , vol.83 , pp. 284-299
    • Tartakoff, A.1    Vassalli, P.2
  • 44
    • 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
  • 45
    • 0029017509 scopus 로고
    • Assembly of IgM. Role of disulfide bonding and noncovalent interactions
    • Wiersma, E. J. and Shulman, M. J. (1995). Assembly of IgM. Role of disulfide bonding and noncovalent interactions. J. Immunol. 154, 5265-5272.
    • (1995) J. Immunol. , vol.154 , pp. 5265-5272
    • Wiersma, E.J.1    Shulman, M.J.2
  • 46
    • 0027055716 scopus 로고
    • Circulating low molecular weight IgM - A disease marker in autoimmune, infective, immunodeficient and B cell lymphoproliferative disorders
    • Xu, H. and Roberts-Thomson, P. J. (1992). Circulating low molecular weight IgM - a disease marker in autoimmune, infective, immunodeficient and B cell lymphoproliferative disorders. Disease Markers 10, 115-141.
    • (1992) Disease Markers , vol.10 , pp. 115-141
    • Xu, H.1    Roberts-Thomson, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.