메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

Hepatic Deficiency of COP9 Signalosome Subunit 8 Induces Ubiquitin-Proteasome System Impairment and Bim-Mediated Apoptosis in Murine Livers

Author keywords

[No Author keywords available]

Indexed keywords

BIM PROTEIN; COP9 SIGNALOSOME; COP9 SIGNALOSOME SUBUNIT 8 PROTEIN; PROTEASOME; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN CIS; RECEPTOR PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84879702339     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067793     Document Type: Article
Times cited : (10)

References (59)
  • 1
    • 84872865382 scopus 로고    scopus 로고
    • Posttranslational modification and quality control
    • 10.1161/CIRCRESAHA.112.268706
    • Wang X, Pattison JS, Su H, (2013) Posttranslational modification and quality control. Circ Res 112: 367-381. doi:10.1161/CIRCRESAHA.112.268706. PubMed: 23329792.
    • (2013) Circ Res , vol.112 , pp. 367-381
    • Wang, X.1    Pattison, J.S.2    Su, H.3
  • 2
    • 84872679130 scopus 로고    scopus 로고
    • Ubiquitin receptors and protein quality control
    • 10.1016/j.yjmcc.2012.09.012
    • Wang X, Terpstra EJ, (2013) Ubiquitin receptors and protein quality control. J Mol Cell Cardiol 55: 73-84. doi:10.1016/j.yjmcc.2012.09.012. PubMed: 23046644.
    • (2013) J Mol Cell Cardiol , vol.55 , pp. 73-84
    • Wang, X.1    Terpstra, E.J.2
  • 3
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • 10.1093/emboj/21.11.2636
    • Cascio P, Call M, Petre BM, Walz T, Goldberg AL, (2002) Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J 21: 2636-2645. doi:10.1093/emboj/21.11.2636. PubMed: 12032076.
    • (2002) EMBO J , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 4
    • 79954590790 scopus 로고    scopus 로고
    • Enhancement of proteasome function by PA28α overexpression protects against oxidative stress
    • 10.1096/fj.10-160895
    • Li J, Powell SR, Wang X, (2011) Enhancement of proteasome function by PA28α overexpression protects against oxidative stress. FASEB J 25: 883-893. doi:10.1096/fj.10-160895. PubMed: 21098724.
    • (2011) FASEB J , vol.25 , pp. 883-893
    • Li, J.1    Powell, S.R.2    Wang, X.3
  • 5
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • 10.1172/JCI45709
    • Li J, Horak KM, Su H, Sanbe A, Robbins J, et al. (2011) Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J Clin Invest 121: 3689-3700. doi:10.1172/JCI45709. PubMed: 21841311.
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5
  • 6
    • 56449125383 scopus 로고    scopus 로고
    • Hepatocellular carcinoma and the ubiquitin-proteasome system
    • 10.1016/j.bbadis.2008.08.003
    • Dawson SP, (2008) Hepatocellular carcinoma and the ubiquitin-proteasome system. Biochim Biophys Acta 1782: 775-784. doi:10.1016/j.bbadis.2008.08.003. PubMed: 18778769.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 775-784
    • Dawson, S.P.1
  • 7
    • 77954477478 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system plays an important role during various stages of the coronavirus infection cycle
    • 10.1128/JVI.00485-10
    • Raaben M, Posthuma CC, Verheije MH, te Lintelo EG, Kikkert M, et al. (2010) The ubiquitin-proteasome system plays an important role during various stages of the coronavirus infection cycle. J Virol 84: 7869-7879. doi:10.1128/JVI.00485-10. PubMed: 20484504.
    • (2010) J Virol , vol.84 , pp. 7869-7879
    • Raaben, M.1    Posthuma, C.C.2    Verheije, M.H.3    te Lintelo, E.G.4    Kikkert, M.5
  • 8
    • 77954469341 scopus 로고    scopus 로고
    • The proteasome inhibitor Velcade enhances rather than reduces disease in mouse hepatitis coronavirus-infected mice
    • 10.1128/JVI.00486-10
    • Raaben M, Grinwis GC, Rottier PJ, de Haan CA, (2010) The proteasome inhibitor Velcade enhances rather than reduces disease in mouse hepatitis coronavirus-infected mice. J Virol 84: 7880-7885. doi:10.1128/JVI.00486-10. PubMed: 20484516.
    • (2010) J Virol , vol.84 , pp. 7880-7885
    • Raaben, M.1    Grinwis, G.C.2    Rottier, P.J.3    de Haan, C.A.4
  • 9
    • 79957801753 scopus 로고    scopus 로고
    • Proteasome inhibitor treatment in alcoholic liver disease
    • 10.3748/wjg.v17.i20.2558
    • Bardag-Gorce F, (2011) Proteasome inhibitor treatment in alcoholic liver disease. World J Gastroenterol 17: 2558-2562. doi:10.3748/wjg.v17.i20.2558. PubMed: 21633661.
    • (2011) World J Gastroenterol , vol.17 , pp. 2558-2562
    • Bardag-Gorce, F.1
  • 10
    • 0344824691 scopus 로고    scopus 로고
    • The COP9 signalosome
    • 10.1146/annurev.cellbio.19.111301.112449
    • Wei N, Deng XW, (2003) The COP9 signalosome. Annu Rev Cell Dev Biol 19: 261-286. doi:10.1146/annurev.cellbio.19.111301.112449. PubMed: 14570571.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 261-286
    • Wei, N.1    Deng, X.W.2
  • 11
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • 10.1016/S0092-8674(03)00722-0
    • Cope GA, Deshaies RJ, (2003) COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114: 663-671. doi:10.1016/S0092-8674(03)00722-0. PubMed: 14505567.
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 12
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
    • 10.1126/science.1059780
    • Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, et al. (2001) Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. Science 292: 1382-1385. doi:10.1126/science.1059780. PubMed: 11337588.
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1    Cope, G.2    Shevchenko, A.3    Serino, G.4    Tsuge, T.5
  • 13
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: more than a protease
    • 10.1016/j.tibs.2008.09.004
    • Wei N, Serino G, Deng XW, (2008) The COP9 signalosome: more than a protease. Trends Biochem Sci 33: 592-600. doi:10.1016/j.tibs.2008.09.004. PubMed: 18926707.
    • (2008) Trends Biochem Sci , vol.33 , pp. 592-600
    • Wei, N.1    Serino, G.2    Deng, X.W.3
  • 14
    • 84865527126 scopus 로고    scopus 로고
    • Deconjugation of Nedd8 from Cul1 is directly regulated by Skp1-F-box and substrate, and the COP9 signalosome inhibits deneddylated SCF by a noncatalytic mechanism
    • 10.1074/jbc.M112.352484
    • Emberley ED, Mosadeghi R, Deshaies RJ, (2012) Deconjugation of Nedd8 from Cul1 is directly regulated by Skp1-F-box and substrate, and the COP9 signalosome inhibits deneddylated SCF by a noncatalytic mechanism. J Biol Chem 287: 29679-29689. doi:10.1074/jbc.M112.352484. PubMed: 22767593.
    • (2012) J Biol Chem , vol.287 , pp. 29679-29689
    • Emberley, E.D.1    Mosadeghi, R.2    Deshaies, R.J.3
  • 15
    • 84055200369 scopus 로고    scopus 로고
    • Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activity
    • 10.1091/mbc.E11-03-0251
    • Choo YY, Boh BK, Lou JJ, Eng J, Leck YC, et al. (2011) Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activity. Mol Biol Cell 22: 4706-4715. doi:10.1091/mbc.E11-03-0251. PubMed: 22013077.
    • (2011) Mol Biol Cell , vol.22 , pp. 4706-4715
    • Choo, Y.Y.1    Boh, B.K.2    Lou, J.J.3    Eng, J.4    Leck, Y.C.5
  • 16
    • 35548940309 scopus 로고    scopus 로고
    • COP9 signalosome subunit 8 is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence
    • 10.1038/ni1514
    • Menon S, Chi H, Zhang H, Deng XW, Flavell RA, et al. (2007) COP9 signalosome subunit 8 is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence. Nat Immunol 8: 1236-1245. doi:10.1038/ni1514. PubMed: 17906629.
    • (2007) Nat Immunol , vol.8 , pp. 1236-1245
    • Menon, S.1    Chi, H.2    Zhang, H.3    Deng, X.W.4    Flavell, R.A.5
  • 17
    • 79451475816 scopus 로고    scopus 로고
    • Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice
    • 10.1161/CIRCRESAHA.110.230607
    • Su H, Li J, Menon S, Liu J, Kumarapeli AR, et al. (2011) Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice. Circ Res 108: 40-50. doi:10.1161/CIRCRESAHA.110.230607. PubMed: 21051661.
    • (2011) Circ Res , vol.108 , pp. 40-50
    • Su, H.1    Li, J.2    Menon, S.3    Liu, J.4    Kumarapeli, A.R.5
  • 18
    • 80855148621 scopus 로고    scopus 로고
    • COP9 signalosome regulates autophagosome maturation
    • 10.1161/CIRCULATIONAHA.111.048934
    • Su H, Li F, Ranek MJ, Wei N, Wang X, (2011) COP9 signalosome regulates autophagosome maturation. Circulation 124: 2117-2128. doi:10.1161/CIRCULATIONAHA.111.048934. PubMed: 21986281.
    • (2011) Circulation , vol.124 , pp. 2117-2128
    • Su, H.1    Li, F.2    Ranek, M.J.3    Wei, N.4    Wang, X.5
  • 19
    • 78651344108 scopus 로고    scopus 로고
    • COP9 signalosome subunit 8 is required for postnatal hepatocyte survival and effective proliferation
    • 10.1038/cdd.2010.98
    • Lei D, Li F, Su H, Tian Z, Ye B, et al. (2011) COP9 signalosome subunit 8 is required for postnatal hepatocyte survival and effective proliferation. Cell Death Differ 18: 259-270. doi:10.1038/cdd.2010.98. PubMed: 20689553.
    • (2011) Cell Death Differ , vol.18 , pp. 259-270
    • Lei, D.1    Li, F.2    Su, H.3    Tian, Z.4    Ye, B.5
  • 20
    • 77955591462 scopus 로고    scopus 로고
    • Hepatocyte death: a clear and present danger
    • 10.1152/physrev.00061.2009
    • Malhi H, Guicciardi ME, Gores GJ, (2010) Hepatocyte death: a clear and present danger. Physiol Rev 90: 1165-1194. doi:10.1152/physrev.00061.2009. PubMed: 20664081.
    • (2010) Physiol Rev , vol.90 , pp. 1165-1194
    • Malhi, H.1    Guicciardi, M.E.2    Gores, G.J.3
  • 21
    • 79953270811 scopus 로고    scopus 로고
    • Traveling Bax and forth from mitochondria to control apoptosis
    • 10.1016/j.cell.2011.03.025
    • Soriano ME, Scorrano L, (2011) Traveling Bax and forth from mitochondria to control apoptosis. Cell 145: 15-17. doi:10.1016/j.cell.2011.03.025. PubMed: 21458662.
    • (2011) Cell , vol.145 , pp. 15-17
    • Soriano, M.E.1    Scorrano, L.2
  • 22
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • 10.1016/S0092-8674(04)00046-7
    • Danial NN, Korsmeyer SJ, (2004) Cell death: critical control points. Cell 116: 205-219. doi:10.1016/S0092-8674(04)00046-7. PubMed: 14744432.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 23
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • 10.1038/nrc883
    • Cory S, Adams JM, (2002) The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2: 647-656. doi:10.1038/nrc883. PubMed: 12209154.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 24
    • 33846964621 scopus 로고    scopus 로고
    • Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak
    • 10.1126/science.1133289
    • Willis SN, Fletcher JI, Kaufmann T, van Delft MF, Chen L, et al. (2007) Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315: 856-859. doi:10.1126/science.1133289. PubMed: 17289999.
    • (2007) Science , vol.315 , pp. 856-859
    • Willis, S.N.1    Fletcher, J.I.2    Kaufmann, T.3    van Delft, M.F.4    Chen, L.5
  • 25
    • 33751513394 scopus 로고    scopus 로고
    • Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies
    • 10.1038/ncb1499
    • Kim H, Rafiuddin-Shah M, Tu HC, Jeffers JR, Zambetti GP, et al. (2006) Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies. Nat Cell Biol 8: 1348-1358. doi:10.1038/ncb1499. PubMed: 17115033.
    • (2006) Nat Cell Biol , vol.8 , pp. 1348-1358
    • Kim, H.1    Rafiuddin-Shah, M.2    Tu, H.C.3    Jeffers, J.R.4    Zambetti, G.P.5
  • 26
    • 54549114986 scopus 로고    scopus 로고
    • BAX activation is initiated at a novel interaction site
    • 10.1038/nature07396
    • Gavathiotis E, Suzuki M, Davis ML, Pitter K, Bird GH, et al. (2008) BAX activation is initiated at a novel interaction site. Nature 455: 1076-1081. doi:10.1038/nature07396. PubMed: 18948948.
    • (2008) Nature , vol.455 , pp. 1076-1081
    • Gavathiotis, E.1    Suzuki, M.2    Davis, M.L.3    Pitter, K.4    Bird, G.H.5
  • 27
    • 0032898369 scopus 로고    scopus 로고
    • Dual roles for glucokinase in glucose homeostasis as determined by liver and pancreatic beta cell-specific gene knockouts using Cre recombinase
    • 10.1074/jbc.274.1.305
    • Postic C, Shiota M, Niswender KD, Jetton TL, Chen Y, et al. (1999) Dual roles for glucokinase in glucose homeostasis as determined by liver and pancreatic beta cell-specific gene knockouts using Cre recombinase. J Biol Chem 274: 305-315. doi:10.1074/jbc.274.1.305. PubMed: 9867845.
    • (1999) J Biol Chem , vol.274 , pp. 305-315
    • Postic, C.1    Shiota, M.2    Niswender, K.D.3    Jetton, T.L.4    Chen, Y.5
  • 28
    • 27944439915 scopus 로고    scopus 로고
    • A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin
    • 16188962
    • Kumarapeli AR, Horak KM, Glasford JW, Li J, Chen Q, et al. (2005) A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin. FASEB J 19: 2051-2053. PubMed: 16188962.
    • (2005) FASEB J , vol.19 , pp. 2051-2053
    • Kumarapeli, A.R.1    Horak, K.M.2    Glasford, J.W.3    Li, J.4    Chen, Q.5
  • 29
    • 47749086687 scopus 로고    scopus 로고
    • RACK1 and CIS mediate the degradation of BimEL in cancer cells
    • 10.1074/jbc.M802360200
    • Zhang W, Cheng GZ, Gong J, Hermanto U, Zong CS, et al. (2008) RACK1 and CIS mediate the degradation of BimEL in cancer cells. J Biol Chem 283: 16416-16426. doi:10.1074/jbc.M802360200. PubMed: 18420585.
    • (2008) J Biol Chem , vol.283 , pp. 16416-16426
    • Zhang, W.1    Cheng, G.Z.2    Gong, J.3    Hermanto, U.4    Zong, C.S.5
  • 30
    • 0033597443 scopus 로고    scopus 로고
    • Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase
    • 10.1126/science.284.5414.657
    • Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, et al. (1999) Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284: 657-661. doi:10.1126/science.284.5414.657. PubMed: 10213691.
    • (1999) Science , vol.284 , pp. 657-661
    • Kamura, T.1    Koepp, D.M.2    Conrad, M.N.3    Skowyra, D.4    Moreland, R.J.5
  • 31
    • 34447135496 scopus 로고    scopus 로고
    • Substrate-mediated regulation of cullin neddylation
    • 10.1074/jbc.M701153200
    • Chew EH, Hagen T, (2007) Substrate-mediated regulation of cullin neddylation. J Biol Chem 282: 17032-17040. doi:10.1074/jbc.M701153200. PubMed: 17439941.
    • (2007) J Biol Chem , vol.282 , pp. 17032-17040
    • Chew, E.H.1    Hagen, T.2
  • 32
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?
    • 10.1038/ncb1203-1029
    • Wolf DA, Zhou C, Wee S, (2003) The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat Cell Biol 5: 1029-1033. doi:10.1038/ncb1203-1029. PubMed: 14647295.
    • (2003) Nat Cell Biol , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 33
    • 1542713819 scopus 로고    scopus 로고
    • The COP9 signalosome: an alternative lid for the 26S proteasome?
    • 10.1016/j.tcb.2003.08.002
    • Li L, Deng XW, (2003) The COP9 signalosome: an alternative lid for the 26S proteasome? Trends Cell Biol 13: 507-509. doi:10.1016/j.tcb.2003.08.002. PubMed: 14507477.
    • (2003) Trends Cell Biol , vol.13 , pp. 507-509
    • Li, L.1    Deng, X.W.2
  • 34
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • 10.1126/science.292.5521.1552
    • Bence NF, Sampat RM, Kopito RR, (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292: 1552-1555. doi:10.1126/science.292.5521.1552. PubMed: 11375494.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 35
    • 27944450427 scopus 로고    scopus 로고
    • Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake
    • 10.1161/01.RES.0000189262.92896.0b
    • Chen Q, Liu JB, Horak KM, Zheng H, Kumarapeli AR, et al. (2005) Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake. Circ Res 97: 1018-1026. doi:10.1161/01.RES.0000189262.92896.0b. PubMed: 16210548.
    • (2005) Circ Res , vol.97 , pp. 1018-1026
    • Chen, Q.1    Liu, J.B.2    Horak, K.M.3    Zheng, H.4    Kumarapeli, A.R.5
  • 36
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • 16371426
    • Liu J, Chen Q, Huang W, Horak KM, Zheng H, et al. (2006) Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J 20: 362-364. PubMed: 16371426.
    • (2006) FASEB J , vol.20 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5
  • 37
    • 39549120409 scopus 로고    scopus 로고
    • Targeted inactivation of the COP9 signalosome impairs multiple stages of T cell development
    • 10.1084/jem.20070725
    • Panattoni M, Sanvito F, Basso V, Doglioni C, Casorati G, et al. (2008) Targeted inactivation of the COP9 signalosome impairs multiple stages of T cell development. J Exp Med 205: 465-477. doi:10.1084/jem.20070725. PubMed: 18268034.
    • (2008) J Exp Med , vol.205 , pp. 465-477
    • Panattoni, M.1    Sanvito, F.2    Basso, V.3    Doglioni, C.4    Casorati, G.5
  • 38
    • 39749142226 scopus 로고    scopus 로고
    • Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development
    • 10.1111/j.1365-2443.2008.01164.x
    • Oren-Giladi P, Krieger O, Edgar BA, Chamovitz DA, Segal D, (2008) Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development. Genes Cells 13: 221-231. doi:10.1111/j.1365-2443.2008.01164.x. PubMed: 18298797.
    • (2008) Genes Cells , vol.13 , pp. 221-231
    • Oren-Giladi, P.1    Krieger, O.2    Edgar, B.A.3    Chamovitz, D.A.4    Segal, D.5
  • 39
    • 0034192005 scopus 로고    scopus 로고
    • Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development
    • 10.1016/S0168-9525(00)01982-X
    • Deng XW, Dubiel W, Wei N, Hofmann K, Mundt K, et al. (2000) Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development. Trends Genet 16: 202-203. doi:10.1016/S0168-9525(00)01982-X. PubMed: 10782111.
    • (2000) Trends Genet , vol.16 , pp. 202-203
    • Deng, X.W.1    Dubiel, W.2    Wei, N.3    Hofmann, K.4    Mundt, K.5
  • 40
    • 0037117417 scopus 로고    scopus 로고
    • The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1
    • 10.1016/S0960-9822(02)00791-1
    • Yang X, Menon S, Lykke-Andersen K, Tsuge T, Di X, et al. (2002) The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1. Curr Biol 12: 667-672. doi:10.1016/S0960-9822(02)00791-1. PubMed: 11967155.
    • (2002) Curr Biol , vol.12 , pp. 667-672
    • Yang, X.1    Menon, S.2    Lykke-Andersen, K.3    Tsuge, T.4    Di, X.5
  • 41
    • 0033545636 scopus 로고    scopus 로고
    • Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1
    • 10.1038/18230
    • Tomoda K, Kubota Y, Kato J, (1999) Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1. Nature 398: 160-165. doi:10.1038/18230. PubMed: 10086358.
    • (1999) Nature , vol.398 , pp. 160-165
    • Tomoda, K.1    Kubota, Y.2    Kato, J.3
  • 42
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • 10.1016/S0092-8674(03)00316-7
    • Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, et al. (2003) The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113: 357-367. doi:10.1016/S0092-8674(03)00316-7. PubMed: 12732143.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5
  • 43
    • 33846559388 scopus 로고    scopus 로고
    • COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: effects on Cactus, Dorsal and hematopoiesis
    • 10.1111/j.1365-2443.2007.01049.x
    • Harari-Steinberg O, Cantera R, Denti S, Bianchi E, Oron E, et al. (2007) COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: effects on Cactus, Dorsal and hematopoiesis. Genes Cells 12: 183-195. doi:10.1111/j.1365-2443.2007.01049.x. PubMed: 17295838.
    • (2007) Genes Cells , vol.12 , pp. 183-195
    • Harari-Steinberg, O.1    Cantera, R.2    Denti, S.3    Bianchi, E.4    Oron, E.5
  • 44
    • 0035984050 scopus 로고    scopus 로고
    • Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to Tobacco mosaic virus
    • 10.1105/tpc.002493
    • Liu Y, Schiff M, Serino G, Deng XW, Dinesh-Kumar SP, (2002) Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to Tobacco mosaic virus. Plant Cell 14: 1483-1496. doi:10.1105/tpc.002493. PubMed: 12119369.
    • (2002) Plant Cell , vol.14 , pp. 1483-1496
    • Liu, Y.1    Schiff, M.2    Serino, G.3    Deng, X.W.4    Dinesh-Kumar, S.P.5
  • 45
    • 84866905506 scopus 로고    scopus 로고
    • Structural basis for a reciprocal regulation between SCF and CSN
    • 10.1016/j.celrep.2012.08.019
    • Enchev RI, Scott DC, da Fonseca PC, Schreiber A, Monda JK, et al. (2012) Structural basis for a reciprocal regulation between SCF and CSN. Cell Rep 2: 616-627. doi:10.1016/j.celrep.2012.08.019. PubMed: 22959436.
    • (2012) Cell Rep , vol.2 , pp. 616-627
    • Enchev, R.I.1    Scott, D.C.2    da Fonseca, P.C.3    Schreiber, A.4    Monda, J.K.5
  • 46
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series
    • 10.1038/embor.2008.183
    • Rabut G, Peter M, (2008) Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 9: 969-976. doi:10.1038/embor.2008.183. PubMed: 18802447.
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 47
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • 10.1038/nature07884
    • Soucy TA, Smith PG, Milhollen MA, Berger AJ, Gavin JM, et al. (2009) An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 458: 732-736. doi:10.1038/nature07884. PubMed: 19360080.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3    Berger, A.J.4    Gavin, J.M.5
  • 48
    • 79960658440 scopus 로고    scopus 로고
    • C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome
    • 10.1074/jbc.M111.246793
    • Kim YC, DeMartino GN, (2011) C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome. J Biol Chem 286: 26652-26666. doi:10.1074/jbc.M111.246793. PubMed: 21628461.
    • (2011) J Biol Chem , vol.286 , pp. 26652-26666
    • Kim, Y.C.1    DeMartino, G.N.2
  • 49
    • 84873321806 scopus 로고    scopus 로고
    • ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome
    • 10.1074/jbc.M112.424788
    • Kim YC, Li X, Thompson D, DeMartino GN, (2013) ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome. J Biol Chem 288: 3334-3345. doi:10.1074/jbc.M112.424788. PubMed: 23212908.
    • (2013) J Biol Chem , vol.288 , pp. 3334-3345
    • Kim, Y.C.1    Li, X.2    Thompson, D.3    DeMartino, G.N.4
  • 50
    • 1842472483 scopus 로고    scopus 로고
    • Caspase activation inhibits proteasome function during apoptosis
    • 10.1016/S1097-2765(04)00156-X
    • Sun XM, Butterworth M, MacFarlane M, Dubiel W, Ciechanover A, et al. (2004) Caspase activation inhibits proteasome function during apoptosis. Mol Cell 14: 81-93. doi:10.1016/S1097-2765(04)00156-X. PubMed: 15068805.
    • (2004) Mol Cell , vol.14 , pp. 81-93
    • Sun, X.M.1    Butterworth, M.2    MacFarlane, M.3    Dubiel, W.4    Ciechanover, A.5
  • 51
    • 77954215848 scopus 로고    scopus 로고
    • Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits
    • 10.1161/CIRCRESAHA.110.219485
    • Divald A, Kivity S, Wang P, Hochhauser E, Roberts B, et al. (2010) Myocardial ischemic preconditioning preserves postischemic function of the 26S proteasome through diminished oxidative damage to 19S regulatory particle subunits. Circ Res 106: 1829-1838. doi:10.1161/CIRCRESAHA.110.219485. PubMed: 20431057.
    • (2010) Circ Res , vol.106 , pp. 1829-1838
    • Divald, A.1    Kivity, S.2    Wang, P.3    Hochhauser, E.4    Roberts, B.5
  • 52
    • 23644447173 scopus 로고    scopus 로고
    • Consequences of COP9 signalosome and 26S proteasome interaction
    • 10.1111/j.1742-4658.2005.04807.x
    • Huang X, Hetfeld BK, Seifert U, Kähne T, Kloetzel PM, et al. (2005) Consequences of COP9 signalosome and 26S proteasome interaction. FEBS J 272: 3909-3917. doi:10.1111/j.1742-4658.2005.04807.x. PubMed: 16045761.
    • (2005) FEBS J , vol.272 , pp. 3909-3917
    • Huang, X.1    Hetfeld, B.K.2    Seifert, U.3    Kähne, T.4    Kloetzel, P.M.5
  • 53
    • 79958165085 scopus 로고    scopus 로고
    • Induction of p21-dependent senescence by an NAE inhibitor, MLN4924, as a mechanism of growth suppression
    • 21677879
    • Jia L, Li H, Sun Y, (2011) Induction of p21-dependent senescence by an NAE inhibitor, MLN4924, as a mechanism of growth suppression. Neoplasia 13: 561-569. PubMed: 21677879.
    • (2011) Neoplasia , vol.13 , pp. 561-569
    • Jia, L.1    Li, H.2    Sun, Y.3
  • 54
    • 78650355357 scopus 로고    scopus 로고
    • NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells
    • 10.1158/0008-5472.CAN-10-2062
    • Lin JJ, Milhollen MA, Smith PG, Narayanan U, Dutta A, (2010) NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells. Cancer Res 70: 10310-10320. doi:10.1158/0008-5472.CAN-10-2062. PubMed: 21159650.
    • (2010) Cancer Res , vol.70 , pp. 10310-10320
    • Lin, J.J.1    Milhollen, M.A.2    Smith, P.G.3    Narayanan, U.4    Dutta, A.5
  • 55
    • 77956578834 scopus 로고    scopus 로고
    • MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-{kappa}B-dependent lymphoma
    • 10.1182/blood-2010-03-272567
    • Milhollen MA, Traore T, Adams-Duffy J, Thomas MP, Berger AJ, et al. (2010) MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-{kappa}B-dependent lymphoma. Blood 116: 1515-1523. doi:10.1182/blood-2010-03-272567. PubMed: 20525923.
    • (2010) Blood , vol.116 , pp. 1515-1523
    • Milhollen, M.A.1    Traore, T.2    Adams-Duffy, J.3    Thomas, M.P.4    Berger, A.J.5
  • 56
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • 10.1038/nrm2308
    • Youle RJ, Strasser A, (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59. doi:10.1038/nrm2308. PubMed: 18097445.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 57
    • 0032518787 scopus 로고    scopus 로고
    • Bim: a novel member of the Bcl-2 family that promotes apoptosis
    • 10.1093/emboj/17.2.384
    • O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, et al. (1998) Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J 17: 384-395. doi:10.1093/emboj/17.2.384. PubMed: 9430630.
    • (1998) EMBO J , vol.17 , pp. 384-395
    • O'Connor, L.1    Strasser, A.2    O'Reilly, L.A.3    Hausmann, G.4    Adams, J.M.5
  • 58
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • 10.1016/S1097-2765(00)80456-6
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A, (1999) The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 3: 287-296. doi:10.1016/S1097-2765(00)80456-6. PubMed: 10198631.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 59
    • 0036091728 scopus 로고    scopus 로고
    • Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis
    • 10.1128/MCB.22.11.3577-3589.2002
    • Marani M, Tenev T, Hancock D, Downward J, Lemoine NR, (2002) Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis. Mol Cell Biol 22: 3577-3589. doi:10.1128/MCB.22.11.3577-3589.2002. PubMed: 11997495.
    • (2002) Mol Cell Biol , vol.22 , pp. 3577-3589
    • Marani, M.1    Tenev, T.2    Hancock, D.3    Downward, J.4    Lemoine, N.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.