메뉴 건너뛰기




Volumn 14, Issue 19, 2005, Pages 2787-2799

Endoplasmic reticulum stress compromises the ubiquitin-proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; UBIQUITIN;

EID: 26444494585     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddi312     Document Type: Article
Times cited : (181)

References (45)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R.W. and Lomas, D.A. (1997) Conformational disease. Lancet 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 2
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci., 4, 49-60.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 3
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuordegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover, A. and Brundin, P. (2003) The ubiquitin proteasome system in neuordegenerative diseases: Sometimes the chicken, sometimes the egg. Neuron, 40, 427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 4
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M.Y. and Goldberg, A.L. (2001) Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron, 29, 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 6
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M. and Kopito, R.R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science, 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 7
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M. and Masucci, M.G. (2000) Short-lived green fluorescent proteins for quantifying ubiquitin/ proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 18, 538-543.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 8
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • Plemper, R.K. and Wolf, D.H. (1999) Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci., 24, 266-270.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 9
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia, R. and Braakman, I. (2003) Quality control in the endoplasmic reticulum protein factory. Nature, 426, 891-894.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 10
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski, D.T. and Kaufman, R.J. (2004) A trip to the ER: Coping with stress. Trends Cell Biol., 14, 20-28.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 12
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B.A. and Yuan, J. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature, 403, 98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 13
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., Zeng, H., Urano, F., Till, J.H., Hubbard, S.R., Harding, H.P., Clark, S.G. and Ron, D. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature, 415, 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 15
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y. and Takahashi, R. (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell, 105, 891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 16
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A. and Ichijo, H. (2002) ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev., 16, 1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 17
  • 18
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz, C., Russelakis-Carneiro, M., Maundrell, K., Castilla, J. and Soto, C. (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J., 22, 5435-5445.
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 19
    • 2142768895 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z α 1-antitrypsin deficiency
    • Lawless, M.W., Greene, C.M., Mulgrew, A., Taggart, C.C., O'Neill, S.J. and McElvaney, N.G. (2004) Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z α 1-antitrypsin deficiency. J. Immunol., 172, 5722-5726.
    • (2004) J. Immunol. , vol.172 , pp. 5722-5726
    • Lawless, M.W.1    Greene, C.M.2    Mulgrew, A.3    Taggart, C.C.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 20
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana, N.R., Zemskov, E.A., Wang, G. and Nukina, N. (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10, 1049-1059.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 22
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten, K., de Vrij, F.M., Verhoef, L.G., Fischer, D.F., van Leeuwen, F. W., Hol, E.M., Masucci, M.G. and Dantuma, N.P. (2002) Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol., 157, 417-427.
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1    de Vrij, F.M.2    Verhoef, L.G.3    Fischer, D.F.4    van Leeuwen, F.W.5    Hol, E.M.6    Masucci, M.G.7    Dantuma, N.P.8
  • 24
    • 0141650794 scopus 로고    scopus 로고
    • Monitoring the ubiquitin/proteasome system in conformational diseases
    • Lindsten, K. and Dantuma, N.P. (2003) Monitoring the ubiquitin/ proteasome system in conformational diseases. Ageing Res. Rev., 2, 433-449.
    • (2003) Ageing Res. Rev. , vol.2 , pp. 433-449
    • Lindsten, K.1    Dantuma, N.P.2
  • 25
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • Yang, M., Omura, S., Bonifacino, J.S. and Weissman, A.M. (1998) Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med., 187, 835-846.
    • (1998) J. Exp. Med. , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 26
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • Gilon, T., Chomsky, O. and Kulka, R.G. (2000) Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair. Mol. Cell. Biol., 20, 7214-7219.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 27
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L. and Kopito, R.R. (1998) Aggresomes: A cellular response to misfolded proteins. J. Cell Biol., 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 28
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman, A.B., Yoo, S.Y., Dantuma, N.P. and Zoghbi, H.Y. (2005) Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum. Mol. Genet., 20, 679-691.
    • (2005) Hum. Mol. Genet. , vol.20 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 29
    • 0032567339 scopus 로고    scopus 로고
    • Generation of destabilized green fluorescent protein as a transcription reporter
    • Li, X., Zhao, X., Fang, Y., Jiang, X., Duong, T., Fan, C., Huang, C.C. and Kain, S.R. (1998) Generation of destabilized green fluorescent protein as a transcription reporter. J. Biol. Chem., 273, 34970-34975.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34970-34975
    • Li, X.1    Zhao, X.2    Fang, Y.3    Jiang, X.4    Duong, T.5    Fan, C.6    Huang, C.C.7    Kain, S.R.8
  • 31
    • 1242269804 scopus 로고    scopus 로고
    • Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12
    • Hitomi, J., Katayama, T., Taniguchi, M., Honda, A., Imaizumi, K. and Tohyama, M. (2004) Apoptosis induced by endoplasmic reticulum stress depends on activation of caspase-3 via caspase-12. Neurosci. Lett. 357, 127-130.
    • (2004) Neurosci. Lett. , vol.357 , pp. 127-130
    • Hitomi, J.1    Katayama, T.2    Taniguchi, M.3    Honda, A.4    Imaizumi, K.5    Tohyama, M.6
  • 34
    • 0035680611 scopus 로고    scopus 로고
    • Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin
    • French, B.A., van Leeuwen, F., Riley, N.E., Yuan, Q.X., Bardag-Gorce, F., Gaal, K., Lue, Y.H., Marceau, N. and French, S.W. (2001) Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol., 71, 241-246.
    • (2001) Exp. Mol. Pathol. , vol.71 , pp. 241-246
    • French, B.A.1    van Leeuwen, F.2    Riley, N.E.3    Yuan, Q.X.4    Bardag-Gorce, F.5    Gaal, K.6    Lue, Y.H.7    Marceau, N.8    French, S.W.9
  • 37
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R.T., Remotti, H., Stevens, J.L. and Ron, D. (1998) CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev., 12, 982-995.
    • (1998) Genes Dev. , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5    Remotti, H.6    Stevens, J.L.7    Ron, D.8
  • 38
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing, M.E., Rajan, R.S., Bence, N.F. and Kopito, R.R. (2002) A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J. Biol. Chem., 277, 34150-34160.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 39
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant α-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli, L., O'Farrell, C., Lockhart, P.J., Baptista, M., Kehoe, K., Vink, L., Choi, P., Wolozin, B., Farrer, M., Hardy, J. et al. (2002) Parkin protects against the toxicity associated with mutant α-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons. Neuron, 36, 1007-1019.
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6    Choi, P.7    Wolozin, B.8    Farrer, M.9    Hardy, J.10
  • 40
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N. and Goldberg, A.L. (2004) Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell, 14, 95-104.
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 41
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef, L.G., Lindsten, K., Masucci, M.G. and Dantuma, N.P. (2002) Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet., 11, 2689-2700.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 42
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken, E., Romijn, E.P., Maggioni, C., Mezghrani, A.. Sitia, R., Braakman, I. and Heck, A.J. (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
    • van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 43
    • 6344225824 scopus 로고    scopus 로고
    • The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum
    • Shim, J., Umemura, T., Nothstein, E. and Rongo, C. (2004) The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum. Mol. Biol. Cell, 15, 4818-4828.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4818-4828
    • Shim, J.1    Umemura, T.2    Nothstein, E.3    Rongo, C.4
  • 44
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon, T., Chomsky, O. and Kulka, R.G. (1998) Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J., 17, 2759-2766.
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.