메뉴 건너뛰기




Volumn 40, Issue 12, 2008, Pages 2865-2879

Decreased ER-associated degradation of α-TCR induced by Grp78 depletion with the SubAB cytotoxin

Author keywords

Cytotoxin; endoplasmic reticulum (ER); ER associated degradation (ERAD); Subtilase; T cell receptor (TCR); Unfolded protein response (UPR)

Indexed keywords

AB5 SUBTILASE CYTOTOXIN; ACTIVATING TRANSCRIPTION FACTOR 3; ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; ADENOSINE TRIPHOSPHATASE; CASPASE; CYTOTOXIN; FAT DROPLET; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; INITIATION FACTOR 2ALPHA; PROTEIN P97; STRESS ACTIVATED PROTEIN KINASE; T LYMPHOCYTE RECEPTOR ALPHA CHAIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ELF 2 ALPHA; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN; X BOX BINDING PROTEIN 1;

EID: 51249096553     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.06.003     Document Type: Article
Times cited : (23)

References (63)
  • 1
    • 4444313480 scopus 로고    scopus 로고
    • Checkpoints in ER-associated degradation: excuse me, which way to the proteasome?
    • Ahner A., and Brodsky J.L. Checkpoints in ER-associated degradation: excuse me, which way to the proteasome?. Trends Cell Biol 14 (2004) 474-478
    • (2004) Trends Cell Biol , vol.14 , pp. 474-478
    • Ahner, A.1    Brodsky, J.L.2
  • 2
    • 0025012782 scopus 로고
    • A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum
    • Bonifacino J.S., Suzuki C.K., and Klausner R.D. A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science 247 (1990) 79-82
    • (1990) Science , vol.247 , pp. 79-82
    • Bonifacino, J.S.1    Suzuki, C.K.2    Klausner, R.D.3
  • 3
    • 0024345717 scopus 로고
    • Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly
    • Bonifacino J.S., Suzuki C.K., Lippincott-Schwartz J., Weissman A.M., and Klausner R.D. Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly. J Cell Biol 109 (1989) 73-83
    • (1989) J Cell Biol , vol.109 , pp. 73-83
    • Bonifacino, J.S.1    Suzuki, C.K.2    Lippincott-Schwartz, J.3    Weissman, A.M.4    Klausner, R.D.5
  • 4
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: a matter of life or death
    • Boyce M., and Yuan J. Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 133 (2006) 363-373
    • (2006) Cell Death Differ , vol.133 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0028963278 scopus 로고
    • Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiator factor 2 alpha by the stressed endoplasmic reticulum
    • Brostrom M.A., Prostko C.R., Gmitter D., and Brostrom C.O. Independent signaling of grp78 gene transcription and phosphorylation of eukaryotic initiator factor 2 alpha by the stressed endoplasmic reticulum. J Biol Chem 270 (1995) 4127-4132
    • (1995) J Biol Chem , vol.270 , pp. 4127-4132
    • Brostrom, M.A.1    Prostko, C.R.2    Gmitter, D.3    Brostrom, C.O.4
  • 7
    • 37349040367 scopus 로고    scopus 로고
    • Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly
    • Buchkovich N.J., Maguire T.G., Yu Y., Paton A.W., Paton J.C., and Alwine J.C. Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly. J Virol 82 (2008) 31-39
    • (2008) J Virol , vol.82 , pp. 31-39
    • Buchkovich, N.J.1    Maguire, T.G.2    Yu, Y.3    Paton, A.W.4    Paton, J.C.5    Alwine, J.C.6
  • 8
    • 0033637082 scopus 로고    scopus 로고
    • Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway
    • Casagrande R., Stern P., Diehn M., Shamu C., Osario M., Zuniga M., et al. Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol Cell 5 (2000) 729-735
    • (2000) Mol Cell , vol.5 , pp. 729-735
    • Casagrande, R.1    Stern, P.2    Diehn, M.3    Shamu, C.4    Osario, M.5    Zuniga, M.6
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162 (1987) 156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 51249091000 scopus 로고    scopus 로고
    • Clathrin-dependent trafficking of subtilase cytotoxin, a novel AB(5) toxin that targets the endoplasmic reticulum chaperone BiP
    • Chong D.C., Paton J.C., Thorpe C.M., and Paton A.W. Clathrin-dependent trafficking of subtilase cytotoxin, a novel AB(5) toxin that targets the endoplasmic reticulum chaperone BiP. Cell Microbiol (2007)
    • (2007) Cell Microbiol
    • Chong, D.C.1    Paton, J.C.2    Thorpe, C.M.3    Paton, A.W.4
  • 11
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L., and Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4 (2003) 181-191
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 12
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S., Ferrone M., Yang C., Jensen J.P., Tiwari S., and Weissman A.M. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 98 (2001) 14422-14427
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 13
    • 0037343387 scopus 로고    scopus 로고
    • Recognition of a single transmembrane degron by sequential quality control checkpoints
    • Fayadat L., and Kopito R.R. Recognition of a single transmembrane degron by sequential quality control checkpoints. Mol Biol Cell 14 (2003) 1268-1278
    • (2003) Mol Biol Cell , vol.14 , pp. 1268-1278
    • Fayadat, L.1    Kopito, R.R.2
  • 14
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R., Jarosch E., Urban J., Volkwein C., and Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2 (2000) 379-384
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 16
    • 0037320333 scopus 로고    scopus 로고
    • IRE1: a role in UPREgulation of ER degradation
    • Hampton R.Y. IRE1: a role in UPREgulation of ER degradation. Dev Cell 4 (2003) 144-146
    • (2003) Dev Cell , vol.4 , pp. 144-146
    • Hampton, R.Y.1
  • 17
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • Harding H.P., Calfon M., Urano F., Novoa I., and Ron D. Transcriptional and translational control in the Mammalian unfolded protein response. Annu Rev Cell Dev Biol 18 (2002) 575-599
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 18
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397 (1999) 271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 19
    • 36048993417 scopus 로고    scopus 로고
    • Blunted activation of NF-kappaB and NF-kappaB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response
    • Hayakawa K., Hiramatsu N., Okamura M., Yao J., Paton A.W., Paton J.C., et al. Blunted activation of NF-kappaB and NF-kappaB-dependent gene expression by geranylgeranylacetone: involvement of unfolded protein response. Biochem Biophys Res Commun 365 (2008) 47-53
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 47-53
    • Hayakawa, K.1    Hiramatsu, N.2    Okamura, M.3    Yao, J.4    Paton, A.W.5    Paton, J.C.6
  • 20
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K., Yoshida H., Yanagi H., Yura T., and Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10 (1999) 3787-3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 21
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien J., and Weissman J.S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313 (2006) 104-107
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 23
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • Huppa J.B., and Ploegh H.L. The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7 (1997) 113-122
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 24
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z., and Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22 (2003) 2309-2317
    • (2003) EMBO J , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 25
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee A.S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35 (2005) 373-381
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 26
    • 0037099034 scopus 로고    scopus 로고
    • A role for mammalian Ubc6 homologues in ER-associated protein degradation
    • Lenk U., Yu H., Walter J., Gelman M.S., Hartmann E., Kopito R.R., et al. A role for mammalian Ubc6 homologues in ER-associated protein degradation. J Cell Sci 115 (2002) 3007-3014
    • (2002) J Cell Sci , vol.115 , pp. 3007-3014
    • Lenk, U.1    Yu, H.2    Walter, J.3    Gelman, M.S.4    Hartmann, E.5    Kopito, R.R.6
  • 27
    • 33746500168 scopus 로고    scopus 로고
    • GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
    • Luo S., Mao C., Lee B., and Lee A.S. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol Cell Biol 26 (2006) 5688-5697
    • (2006) Mol Cell Biol , vol.26 , pp. 5688-5697
    • Luo, S.1    Mao, C.2    Lee, B.3    Lee, A.S.4
  • 28
    • 0036556684 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum as a sensor for cellular stress
    • Ma Y., and Hendershot L.M. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress Chaperones 7 (2002) 222-229
    • (2002) Cell Stress Chaperones , vol.7 , pp. 222-229
    • Ma, Y.1    Hendershot, L.M.2
  • 29
    • 33845970591 scopus 로고    scopus 로고
    • Two distinct cytotoxic activities of subtilase cytotoxin produced by shiga-toxigenic Escherichia coli
    • Morinaga N., Yahiro K., Matsuura G., Watanabe M., Nomura F., Moss J., et al. Two distinct cytotoxic activities of subtilase cytotoxin produced by shiga-toxigenic Escherichia coli. Infect Immun 75 (2007) 488-496
    • (2007) Infect Immun , vol.75 , pp. 488-496
    • Morinaga, N.1    Yahiro, K.2    Matsuura, G.3    Watanabe, M.4    Nomura, F.5    Moss, J.6
  • 30
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng D.T., Spear E.D., and Walter P. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J Cell Biol 150 (2000) 77-88
    • (2000) J Cell Biol , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 31
    • 33747371085 scopus 로고    scopus 로고
    • Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates
    • Nowis D., McConnell E., and Wojcik C. Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates. Exp Cell Res 312 (2006) 2921-2932
    • (2006) Exp Cell Res , vol.312 , pp. 2921-2932
    • Nowis, D.1    McConnell, E.2    Wojcik, C.3
  • 32
    • 34250312427 scopus 로고    scopus 로고
    • TNF potentiates anticancer activity of bortezomib (Velcade(R)) through reduced expression of proteasome subunits and dysregulation of unfolded protein response
    • Nowis D., McConnell E.J., Dierlam L., Palamarchuk A., Lass A., and Wojcik C. TNF potentiates anticancer activity of bortezomib (Velcade(R)) through reduced expression of proteasome subunits and dysregulation of unfolded protein response. Int J Cancer 121 (2007) 431-441
    • (2007) Int J Cancer , vol.121 , pp. 431-441
    • Nowis, D.1    McConnell, E.J.2    Dierlam, L.3    Palamarchuk, A.4    Lass, A.5    Wojcik, C.6
  • 33
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • Oyadomari S., Araki E., and Mori M. Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis 7 (2002) 335-345
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 34
    • 33747175431 scopus 로고    scopus 로고
    • Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload
    • Oyadomari S., Yun C., Fisher E.A., Kreglinger N., Kreibich G., Oyadomari M., et al. Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload. Cell 126 (2006) 727-739
    • (2006) Cell , vol.126 , pp. 727-739
    • Oyadomari, S.1    Yun, C.2    Fisher, E.A.3    Kreglinger, N.4    Kreibich, G.5    Oyadomari, M.6
  • 35
    • 33749522548 scopus 로고    scopus 로고
    • AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP
    • Paton A.W., Beddoe T., Thorpe C.M., Whisstock J.C., Wilce M.C., Rossjohn J., et al. AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP. Nature 443 (2006) 548-552
    • (2006) Nature , vol.443 , pp. 548-552
    • Paton, A.W.1    Beddoe, T.2    Thorpe, C.M.3    Whisstock, J.C.4    Wilce, M.C.5    Rossjohn, J.6
  • 36
    • 3142696899 scopus 로고    scopus 로고
    • A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli
    • Paton A.W., Srimanote P., Talbot U.M., Wang H., and Paton J.C. A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli. J Exp Med 200 (2004) 35-46
    • (2004) J Exp Med , vol.200 , pp. 35-46
    • Paton, A.W.1    Srimanote, P.2    Talbot, U.M.3    Wang, H.4    Paton, J.C.5
  • 37
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway 1
    • Schulze A., Standera S., Buerger E., Kikkert M., van V.S., Wiertz E., et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway 1. J Mol Biol 354 (2005) 1021-1027
    • (2005) J Mol Biol , vol.354 , pp. 1021-1027
    • Schulze, A.1    Standera, S.2    Buerger, E.3    Kikkert, M.4    van, V.S.5    Wiertz, E.6
  • 38
    • 4444232905 scopus 로고    scopus 로고
    • The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum
    • Shen X., Zhang K., and Kaufman R.J. The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum. J Chem Neuroanat 28 (2004) 79-92
    • (2004) J Chem Neuroanat , vol.28 , pp. 79-92
    • Shen, X.1    Zhang, K.2    Kaufman, R.J.3
  • 39
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y., Vattem K.M., Sood R., An J., Liang J., Stramm L., et al. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol Cell Biol 18 (1998) 7499-7509
    • (1998) Mol Cell Biol , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6
  • 40
    • 17144365102 scopus 로고    scopus 로고
    • Hemolytic uremic syndrome; pathogenesis, treatment, and outcome
    • Siegler R., and Oakes R. Hemolytic uremic syndrome; pathogenesis, treatment, and outcome. Curr Opin Pediatr 17 (2005) 200-204
    • (2005) Curr Opin Pediatr , vol.17 , pp. 200-204
    • Siegler, R.1    Oakes, R.2
  • 41
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 42
    • 21544443134 scopus 로고    scopus 로고
    • Protective immunization of mice with an active-site mutant of subtilase cytotoxin of Shiga toxin-producing Escherichia coli
    • Talbot U.M., Paton J.C., and Paton A.W. Protective immunization of mice with an active-site mutant of subtilase cytotoxin of Shiga toxin-producing Escherichia coli. Infect Immun 73 (2005) 4432-4436
    • (2005) Infect Immun , vol.73 , pp. 4432-4436
    • Talbot, U.M.1    Paton, J.C.2    Paton, A.W.3
  • 43
  • 44
    • 0035844139 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)
    • Tiwari S., and Weissman A.M. Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J Biol Chem 276 (2001) 16193-16200
    • (2001) J Biol Chem , vol.276 , pp. 16193-16200
    • Tiwari, S.1    Weissman, A.M.2
  • 45
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., and Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000) 249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 46
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B., Ye Y., and Rapoport T.A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3 (2002) 246-255
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 47
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz G.K., Rolls M.M., and Rapoport T.A. Structural organization of the endoplasmic reticulum. EMBO Rep 3 (2002) 944-950
    • (2002) EMBO Rep , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 48
    • 35348860134 scopus 로고    scopus 로고
    • Pathologic changes in mice induced by subtilase cytotoxin, a potent new Escherichia coli AB5 toxin that targets the endoplasmic reticulum
    • Wang H., Paton J.C., and Paton A.W. Pathologic changes in mice induced by subtilase cytotoxin, a potent new Escherichia coli AB5 toxin that targets the endoplasmic reticulum. J Infect Dis 196 (2007) 1093-1101
    • (2007) J Infect Dis , vol.196 , pp. 1093-1101
    • Wang, H.1    Paton, J.C.2    Paton, A.W.3
  • 49
    • 0025193361 scopus 로고
    • The gamma and epsilon subunits of the CD3 complex inhibit pre-Golgi degradation of newly synthesized T cell antigen receptors
    • Wileman T., Carson G.R., Concino M., Ahmed A., and Terhorst C. The gamma and epsilon subunits of the CD3 complex inhibit pre-Golgi degradation of newly synthesized T cell antigen receptors. J Cell Biol 110 (1990) 973-986
    • (1990) J Cell Biol , vol.110 , pp. 973-986
    • Wileman, T.1    Carson, G.R.2    Concino, M.3    Ahmed, A.4    Terhorst, C.5
  • 50
    • 0027157153 scopus 로고
    • Associations between subunit ectodomains promote T cell antigen receptor assembly and protect against degradation in the ER
    • Wileman T., Kane L.P., Young J., Carson G.R., and Terhorst C. Associations between subunit ectodomains promote T cell antigen receptor assembly and protect against degradation in the ER. J Cell Biol 122 (1993) 67-78
    • (1993) J Cell Biol , vol.122 , pp. 67-78
    • Wileman, T.1    Kane, L.P.2    Young, J.3    Carson, G.R.4    Terhorst, C.5
  • 51
    • 0242626544 scopus 로고    scopus 로고
    • BiP-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes
    • Winkeler A., Godderz D., Herzog V., and Schmitz A. BiP-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes. FEBS Lett 554 (2003) 439-442
    • (2003) FEBS Lett , vol.554 , pp. 439-442
    • Winkeler, A.1    Godderz, D.2    Herzog, V.3    Schmitz, A.4
  • 52
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • Wojcik C., Rowicka M., Kudlicki A., Nowis D., McConnell E., Kujawa M., et al. Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol Biol Cell 17 (2006) 4606-4618
    • (2006) Mol Biol Cell , vol.17 , pp. 4606-4618
    • Wojcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5    Kujawa, M.6
  • 53
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik C., Schroeter D., Wilk S., Lamprecht J., and Paweletz N. Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur J Cell Biol 71 (1996) 311-318
    • (1996) Eur J Cell Biol , vol.71 , pp. 311-318
    • Wojcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 54
    • 2342517449 scopus 로고    scopus 로고
    • Apoptosis induced in L1210 leukaemia cells by an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik C., Stoklosa T., Giermasz A., Golab J., Zagozdzon R., Kawiak J., et al. Apoptosis induced in L1210 leukaemia cells by an inhibitor of the chymotrypsin-like activity of the proteasome. Apoptosis 2 (1997) 455-462
    • (1997) Apoptosis , vol.2 , pp. 455-462
    • Wojcik, C.1    Stoklosa, T.2    Giermasz, A.3    Golab, J.4    Zagozdzon, R.5    Kawiak, J.6
  • 55
    • 48749112866 scopus 로고    scopus 로고
    • Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signaling pathways
    • Wolfson J.J., May K.L., Thorpe C.M., Jandhyala D.M., Paton J.C., and Paton A.W. Subtilase cytotoxin activates PERK, IRE1 and ATF6 endoplasmic reticulum stress-signaling pathways. Cell Microbiol 10 (2008) 1775-1786
    • (2008) Cell Microbiol , vol.10 , pp. 1775-1786
    • Wolfson, J.J.1    May, K.L.2    Thorpe, C.M.3    Jandhyala, D.M.4    Paton, J.C.5    Paton, A.W.6
  • 56
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the unfolded protein response
    • Wu J., and Kaufman R.J. From acute ER stress to physiological roles of the unfolded protein response. Cell Death Differ 13 (2006) 374-384
    • (2006) Cell Death Differ , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 57
    • 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. 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 (1998) 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
  • 58
    • 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. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414 (2001) 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 59
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y., Meyer H.H., and Rapoport T.A. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162 (2003) 71-84
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 60
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H., Haze K., Yanagi H., Yura T., and Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273 (1998) 33741-33749
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 61
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 62
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H., Kaung G., Kobayashi S., and Kopito R.R. Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J Biol Chem 272 (1997) 20800-20804
    • (1997) J Biol Chem , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 63
    • 0033601349 scopus 로고    scopus 로고
    • The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor
    • Yu H., and Kopito R.R. The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor. J Biol Chem 274 (1999) 36852-36858
    • (1999) J Biol Chem , vol.274 , pp. 36852-36858
    • Yu, H.1    Kopito, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.