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Volumn 20, Issue 2, 2003, Pages 99-104

Protein folding and translocation across the endoplasmic reticulum membrane

Author keywords

Degradation; Modification; Protein folding; Translocation; Translocon

Indexed keywords

POLYPEPTIDE; SECRETORY PROTEIN;

EID: 0037666790     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/0968768031000069241     Document Type: Review
Times cited : (38)

References (45)
  • 1
    • 0034664243 scopus 로고    scopus 로고
    • The ER translocon and retrotranslocation: Is the shift into reverse manual or automatic
    • Johnson, A. E. and Haigh, N. G., 2000, The ER translocon and retrotranslocation: is the shift into reverse manual or automatic. Cell, 102, 709-712.
    • (2000) Cell , vol.102 , pp. 709-712
    • Johnson, A.E.1    Haigh, N.G.2
  • 2
    • 0029139091 scopus 로고
    • Protein translocation at the membrane of the endoplasmic reticulum
    • High, S., 1995, Protein translocation at the membrane of the endoplasmic reticulum. Prog. Biophys. Molec. Biol., 63, 233-250.
    • (1995) Prog. Biophys. Molec. Biol. , vol.63 , pp. 233-250
    • High, S.1
  • 3
    • 0034672006 scopus 로고    scopus 로고
    • In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation
    • Goder, V., Crottet, P. and Spiess, M., 2000, In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. EMBO J., 19, 6704-6712.
    • (2000) EMBO J. , vol.19 , pp. 6704-6712
    • Goder, V.1    Crottet, P.2    Spiess, M.3
  • 5
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during co-translational protein translocation at the ER membrane
    • Hamman, B. D., Chen, J.-C., Johnson, E. E. and Johnson, A. E., 1997, The aqueous pore through the translocon has a diameter of 40-60 Å during co-translational protein translocation at the ER membrane. Cell, 89, 535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.-C.2    Johnson, E.E.3    Johnson, A.E.4
  • 6
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K. S., Liao, S., Worrell, V. E., Reinhart, G. D. and Johnson, A. E., 1994, Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell, 78, 461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 7
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon before and early in translocation
    • Hamman, B. D., Hendershot, L. M. and Johnson, A. E., 1998, BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon before and early in translocation. Cell, 92, 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 8
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M. W., Brunner, J. and Dobberstein, B., 1995, The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell, 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 9
    • 0029894267 scopus 로고    scopus 로고
    • Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration
    • Borel, A. C. and Simon, S. M., 1996, Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration. Cell, 85, 379-389.
    • (1996) Cell , vol.85 , pp. 379-389
    • Borel, A.C.1    Simon, S.M.2
  • 10
    • 0030825974 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane protein integration into the endoplasmic reticulum
    • Mothes, W., Heinrich, S. U., Graf, R., Nilsson, I., von Heijne, G., Brunner, J. and Rapoport, T., 1997, Molecular mechanisms of membrane protein integration into the endoplasmic reticulum. Cell, 89, 523-533.
    • (1997) Cell , vol.89 , pp. 523-533
    • Mothes, W.1    Heinrich, S.U.2    Graf, R.3    Nilsson, I.4    Von Heijne, G.5    Brunner, J.6    Rapoport, T.7
  • 11
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H. and Johnson, A. E., 1997, Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell, 90, 31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 12
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A. and Cyr, D. M., 1999, The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J., 18, 1492-1505.
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 13
    • 0029561894 scopus 로고
    • Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain
    • Denzer, A. J., Nabholz, C. E. and Spiess, M., 1995, Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain. EMBO J., 14, 6311-6317.
    • (1995) EMBO J. , vol.14 , pp. 6311-6317
    • Denzer, A.J.1    Nabholz, C.E.2    Spiess, M.3
  • 14
    • 0033570916 scopus 로고    scopus 로고
    • An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator
    • Tector, M. and Hartl, F. U., 1999, An unstable transmembrane segment in the cystic fibrosis transmembrane conductance regulator. EMBO J., 18, 6290-6298.
    • (1999) EMBO J. , vol.18 , pp. 6290-6298
    • Tector, M.1    Hartl, F.U.2
  • 16
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesised glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U. and Helenius, A., 1997, Interactions between newly synthesised glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol., 136, 555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 17
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-α-factor across the ER membrane
    • Matlack, K. E., Misselwitz, B., Plath, K. and Rapoport, T. A., 1999, BiP acts as a molecular ratchet during posttranslational transport of prepro-α-factor across the ER membrane. Cell, 97, 553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 19
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson, J. R. and Stirling, C. J., 2000, LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J., 19, 6440-6452.
    • (2000) EMBO J. , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 20
    • 0032897245 scopus 로고    scopus 로고
    • Protein targeting to the endoplasmic reticulum in yeast. 1997 Fleming Lecture
    • Stirling, C. J., 1999, Protein targeting to the endoplasmic reticulum in yeast. 1997 Fleming Lecture. Microbiology, 145, 991-998.
    • (1999) Microbiology , vol.145 , pp. 991-998
    • Stirling, C.J.1
  • 21
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico, W. J., Waters, M. G. and Blobel, G., 1988, 70K heat shock related proteins stimulate protein translocation into microsomes. Nature, 332, 805-810.
    • (1988) Nature , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 22
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R. J., Koch, B. D., Werner-Washburne, M., Craig, E. A. and Schekman, R., 1988, A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature, 332, 800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 23
    • 0034597099 scopus 로고    scopus 로고
    • Spontaneous release of cytosolic proteins from posftranslational substrates before their transport into the endoplasmic reticulum
    • Plath, K. and Rapoport, T. A., 2000, Spontaneous release of cytosolic proteins from posftranslational substrates before their transport into the endoplasmic reticulum. J. Cell Biol., 151, 167-178.
    • (2000) J. Cell Biol. , vol.151 , pp. 167-178
    • Plath, K.1    Rapoport, T.A.2
  • 24
    • 0025970051 scopus 로고
    • Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • Deshaies, R. J., Sanders, S. L., Feldheim, D. A. and Schekman, R., 1991, Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature, 349, 806-808.
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.A.3    Schekman, R.4
  • 25
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum
    • Shaw, A. S., Rottier, P. J. M. and Rose, J. K., 1988, Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc. Natl Acad. Sci., 85, 7592-7596.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 26
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A. and Ploegh, H. L., 1996, Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature, 384, 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 27
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway
    • Cabral, C. M., Liu, Y. and Sifers, R. N., 2001, Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem. Sci., 26, 619-624.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 28
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob, C. A., Burda, P., Roth, J. and Aebi, M., 1998, Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J. Cell Biol., 142, 1223-1233.
    • (1998) J. Cell Biol. , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 29
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell, S. R., Hill, K. J. and Cooper, A. A., 2001, Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J. Biol. Chem., 276, 23296-23303.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 30
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist, S., Kim, W., Belden, W. J., Spear, E. D., Barlowe, C. and Ng, D. T., 2001, Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J. Cell Biol., 155, 355-368.
    • (2001) J. Cell Biol. , vol.155 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 31
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
    • Hill, K. and Cooper, A. A., 2000, Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system. EMBO J., 19, 550-561.
    • (2000) EMBO J. , vol.19 , pp. 550-561
    • Hill, K.1    Cooper, A.A.2
  • 32
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang, Y., Nijbroek, G., Sullivan, M. L., McCracken, A. A., Watkins, S. C., Michaelis, S. and Brodsky, J. L., 2001, Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol. Biol. Cell, 12, 1303-1314.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3    McCracken, A.A.4    Watkins, S.C.5    Michaelis, S.6    Brodsky, J.L.7
  • 33
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • De Virgilio, M., Weninger, H. and Ivessa, N. E., 1998, Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem., 273, 9734-9743.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 34
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein
    • Mayer, T. U., Braun, T. and Jentsch, S., 1998, Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J., 17, 3251-3257.
    • (1998) EMBO J. , vol.17 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 35
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai, R. M. and Li, C. C., 2001, Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Natl Cell Biol., 3, 740-744.
    • (2001) Natl. Cell Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 36
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H. and Rapoport, T. A., 2001, The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature, 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 37
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M. and Cyr, D. M., 2001, The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Natl Cell Biol., 3, 100-105.
    • (2001) Natl. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 39
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari, M., Galli, C., Piccaluga, M., Pieren, M. and Paganetti, P., 2002, Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J. Cell Biol., 158, 247-257.
    • (2002) J. Cell Biol. , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, M.3    Pieren, M.4    Paganetti, P.5
  • 40
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulphide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W. I. and Rapoport, T. A., 2001, Protein disulphide 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
  • 41
    • 0028022110 scopus 로고
    • Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences
    • Li, Y., Luo, L., Thomas, D. Y. and Kang, C. Y., 1994, Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences. Virol., 204, 266-278.
    • (1994) Virol. , vol.204 , pp. 266-278
    • Li, Y.1    Luo, L.2    Thomas, D.Y.3    Kang, C.Y.4
  • 42
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator: Effect of disulphide bond formation on N-linked glycosylation
    • Allen, S., Naim, H. Y. and Bulleid, N. J., 1995, Intracellular folding of tissue-type plasminogen activator: effect of disulphide bond formation on N-linked glycosylation. J. Biol. Chem., 270, 4797-4804.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 44
    • 0031916031 scopus 로고    scopus 로고
    • Molecular recognition in procollagen chain assembly
    • McLaughlin, S. H. and Bulleid, N. J., 1998, Molecular recognition in procollagen chain assembly. Matrix Biology, 16, 369-377.
    • (1998) Matrix Biology , vol.16 , pp. 369-377
    • McLaughlin, S.H.1    Bulleid, N.J.2
  • 45
    • 0035844125 scopus 로고    scopus 로고
    • Early events in GPI-anchor addition: Substrate proteins associate with the transamidase subunit Gpi8p
    • Spurway, T. D., Dalley, J. A., High, S. and Bulleid, N. J., 2001, Early events in GPI-anchor addition: substrate proteins associate with the transamidase subunit Gpi8p. J. Biol. Chem., 276, 15975-15982.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15975-15982
    • Spurway, T.D.1    Dalley, J.A.2    High, S.3    Bulleid, N.J.4


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