메뉴 건너뛰기




Volumn 5, Issue JUL, 2014, Pages

A high-content RNAi screen identifies ubiquitin modifiers that regulate TNF-dependent nuclear accumulation of NF-κB

Author keywords

Apoptosis; High content; JNK; NF B; SiRNA screen; TNF; Ubiquitin

Indexed keywords


EID: 84905666717     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00322     Document Type: Article
Times cited : (2)

References (36)
  • 1
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: a beautiful pathway
    • doi: 10.1126/science.1071924
    • Chen G, Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science (2002) 296:1634-5. doi: 10.1126/science.1071924
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 2
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • doi:10.1038/nri1184
    • Aggarwal BB. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol (2003) 3:745-56. doi:10.1038/nri1184
    • (2003) Nat Rev Immunol , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 3
    • 77950345093 scopus 로고    scopus 로고
    • Inflammation 2010 new adventures of an old flame
    • doi:10.1016/j.cell.2010.03.006
    • Medzhitov R. Inflammation 2010: new adventures of an old flame. Cell (2010) 140:771-6. doi:10.1016/j.cell.2010.03.006
    • (2010) Cell , vol.140 , pp. 771-776
    • Medzhitov, R.1
  • 4
    • 77950365906 scopus 로고    scopus 로고
    • Nonresolving inflammation
    • doi:10.1016/j.cell.2010.02.029
    • Nathan C, Ding A. Nonresolving inflammation. Cell (2010) 140:871-82. doi:10.1016/j.cell.2010.02.029
    • (2010) Cell , vol.140 , pp. 871-882
    • Nathan, C.1    Ding, A.2
  • 5
    • 77950346282 scopus 로고    scopus 로고
    • Immunity, inflammation, and cancer
    • doi:10.1016/j.cell.2010.01.025
    • Grivennikov SI, Greten FR, Karin M. Immunity, inflammation, and cancer. Cell (2010) 140:883-99. doi:10.1016/j.cell.2010.01.025
    • (2010) Cell , vol.140 , pp. 883-899
    • Grivennikov, S.I.1    Greten, F.R.2    Karin, M.3
  • 6
    • 0024281428 scopus 로고
    • A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF
    • doi:10.1016/0092-8674(88)90486-2
    • Kriegler M, Perez C, Defay K, Albert I, Lu SD. A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell (1988) 53:45-53. doi:10.1016/0092-8674(88)90486-2
    • (1988) Cell , vol.53 , pp. 45-53
    • Kriegler, M.1    Perez, C.2    Defay, K.3    Albert, I.4    Lu, S.D.5
  • 7
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • doi:10.1126/science.283.5401.543
    • Jiang Y, Woronicz JD, Liu W, Goeddel DV. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science (1999) 283:543-6. doi:10.1126/science.283.5401.543
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 8
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • doi:10.1016/0092-8674(95)90070-5
    • Hsu H, Xiong J, Goeddel DV. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell (1995) 81:495-504. doi:10.1016/0092-8674(95)90070-5
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 9
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • doi:10.1016/S0092-8674(03)00521-X
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell (2003) 114:181-90. doi:10.1016/S0092-8674(03)00521-X
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 10
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • doi:10.1016/S1074-7613(00)80252-6
    • Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity (1996) 4:387-96. doi:10.1016/S1074-7613(00)80252-6
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 11
    • 0035965232 scopus 로고    scopus 로고
    • Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-kappa B activation and protection from cell death
    • doi:10.1074/jbc.M104837200
    • Tada K, Okazaki T, Sakon S, Kobarai T, Kurosawa K, Yamaoka S, et al. Critical roles of TRAF2 and TRAF5 in tumor necrosis factor-induced NF-kappa B activation and protection from cell death. J Biol Chem (2001) 276:36530-4. doi:10.1074/jbc.M104837200
    • (2001) J Biol Chem , vol.276 , pp. 36530-36534
    • Tada, K.1    Okazaki, T.2    Sakon, S.3    Kobarai, T.4    Kurosawa, K.5    Yamaoka, S.6
  • 12
    • 54049155149 scopus 로고    scopus 로고
    • c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation
    • doi:10.1074/jbc.C800128200
    • Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation. J Biol Chem (2008) 283:24295-9. doi:10.1074/jbc.C800128200
    • (2008) J Biol Chem , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1    Goncharov, T.2    Fedorova, A.V.3    Dynek, J.N.4    Zobel, K.5    Deshayes, K.6
  • 13
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • doi:10.1007/s00018-004-4129-5
    • Fang S, Weissman AM. A field guide to ubiquitylation. Cell Mol Life Sci (2004) 61:1546-61. doi:10.1007/s00018-004-4129-5
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 14
    • 80054852212 scopus 로고    scopus 로고
    • TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer
    • doi:10.1111/j.1600-065X.2011.01066.x
    • Walczak H. TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer. Immunol Rev (2011) 244:9-28. doi:10.1111/j.1600-065X.2011.01066.x
    • (2011) Immunol Rev , vol.244 , pp. 9-28
    • Walczak, H.1
  • 15
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • doi:10.1016/j.molcel.2004.08.008
    • Kanayama A, Seth RB, Sun L, Ea CK, Hong M, Shaito A, et al. TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol Cell (2004) 15:535-48. doi:10.1016/j.molcel.2004.08.008
    • (2004) Mol Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.K.4    Hong, M.5    Shaito, A.6
  • 16
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • doi:10.1016/j.molcel.2006.03.026
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell (2006) 22:245-57. doi:10.1016/j.molcel.2006.03.026
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 17
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation
    • doi:10.1074/jbc.M600620200
    • Li H, Kobayashi M, Blonska M, You Y, Lin X. Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation. J Biol Chem (2006) 281:13636-43. doi:10.1074/jbc.M600620200
    • (2006) J Biol Chem , vol.281 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 18
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • doi:10.1038/ncb1384
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol (2006) 8:398-406. doi:10.1038/ncb1384
    • (2006) Nat Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 19
    • 79952498248 scopus 로고    scopus 로고
    • TNFR1-induced activation of the classical NF-kappaB pathway
    • doi:10.1111/j.1742-4658.2011.08015.x
    • Wajant H, Scheurich P. TNFR1-induced activation of the classical NF-kappaB pathway. FEBS J (2011) 278:862-76. doi:10.1111/j.1742-4658.2011.08015.x
    • (2011) FEBS J , vol.278 , pp. 862-876
    • Wajant, H.1    Scheurich, P.2
  • 20
    • 84862248877 scopus 로고    scopus 로고
    • Lubac a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses
    • doi:10.1016/j.micinf.2012.01.011
    • Tokunaga F, Iwai K. LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses. Microbes Infect (2012) 14:563-72. doi:10.1016/j.micinf.2012.01.011
    • (2012) Microbes Infect , vol.14 , pp. 563-572
    • Tokunaga, F.1    Iwai, K.2
  • 21
    • 82755198022 scopus 로고    scopus 로고
    • Proliferative versus apoptotic functions of caspase-8 hetero or homo: the caspase-8 dimer controls cell fate
    • doi:10.1016/j.bbapap.2011.06.005
    • van Raam BJ, Salvesen GS. Proliferative versus apoptotic functions of caspase-8 hetero or homo: the caspase-8 dimer controls cell fate. Biochim Biophys Acta (2012) 1824:113-22. doi:10.1016/j.bbapap.2011.06.005
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 113-122
    • van Raam, B.J.1    Salvesen, G.S.2
  • 22
    • 0034743199 scopus 로고    scopus 로고
    • NF-kappaB signals induce the expression of c-FLIP
    • doi:10.1128/MCB.21.16.5299-5305.2001
    • Micheau O, Lens S, Gaide O, Alevizopoulos K, Tschopp J. NF-kappaB signals induce the expression of c-FLIP. Mol Cell Biol (2001) 21:5299-305. doi:10.1128/MCB.21.16.5299-5305.2001
    • (2001) Mol Cell Biol , vol.21 , pp. 5299-5305
    • Micheau, O.1    Lens, S.2    Gaide, O.3    Alevizopoulos, K.4    Tschopp, J.5
  • 23
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation
    • doi:10.1073/pnas.93.13.6721
    • Song HY, Rothe M, Goeddel DV. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation. Proc Natl Acad Sci U S A (1996) 93:6721-5. doi:10.1073/pnas.93.13.6721
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 24
    • 0030026698 scopus 로고    scopus 로고
    • A20 zinc finger protein inhibits TNF and IL-1 signaling
    • Jaattela M, Mouritzen H, Elling F, Bastholm L. A20 zinc finger protein inhibits TNF and IL-1 signaling. J Immunol (1996) 156:1166-73.
    • (1996) J Immunol , vol.156 , pp. 1166-1173
    • Jaattela, M.1    Mouritzen, H.2    Elling, F.3    Bastholm, L.4
  • 25
    • 21744455599 scopus 로고    scopus 로고
    • The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C elegans and S cerevisiae
    • doi:10.1038/nature03662
    • Kurz T, Ozlu N, Rudolf F, O'Rourke SM, Luke B, Hofmann K, et al. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature (2005) 435:1257-61. doi:10.1038/nature03662
    • (2005) Nature , vol.435 , pp. 1257-1261
    • Kurz, T.1    Ozlu, N.2    Rudolf, F.3    O'Rourke, S.M.4    Luke, B.5    Hofmann, K.6
  • 26
    • 0033068154 scopus 로고    scopus 로고
    • The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
    • doi:10.1101/gad.13.3.270
    • Winston JT, Strack P, Beer-Romero P, Chu CY, Elledge SJ, Harper JW. The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. Genes Dev (1999) 13:270-83. doi:10.1101/gad.13.3.270
    • (1999) Genes Dev , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 27
    • 0034723296 scopus 로고    scopus 로고
    • Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination
    • doi:10.1074/jbc.275.4.2877
    • Suzuki H, Chiba T, Suzuki T, Fujita T, Ikenoue T, Omata M, et al. Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination. J Biol Chem (2000) 275:2877-84. doi:10.1074/jbc.275.4.2877
    • (2000) J Biol Chem , vol.275 , pp. 2877-2884
    • Suzuki, H.1    Chiba, T.2    Suzuki, T.3    Fujita, T.4    Ikenoue, T.5    Omata, M.6
  • 28
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • doi:10.1016/j.molcel.2009.10.013
    • Haas TL, Emmerich CH, Gerlach B, Schmukle AC, Cordier SM, Rieser E, et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol Cell (2009) 36:831-44. doi:10.1016/j.molcel.2009.10.013
    • (2009) Mol Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6
  • 29
    • 73549097550 scopus 로고    scopus 로고
    • A quantitative RNAi screen for JNK modifiers identifies PVR as a novel regulator of Drosophila immune signaling
    • doi:10.1371/journal.ppat.1000655
    • Bond D, Foley E. A quantitative RNAi screen for JNK modifiers identifies PVR as a novel regulator of Drosophila immune signaling. PLoS Pathog (2009) 5:e1000655. doi:10.1371/journal.ppat.1000655
    • (2009) PLoS Pathog , vol.5
    • Bond, D.1    Foley, E.2
  • 30
    • 26244434134 scopus 로고    scopus 로고
    • Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB
    • doi:10.1016/j.cellsig.2005.03.017
    • Tzimas C, Michailidou G, Arsenakis M, Kieff E, Mosialos G, Hatzivassiliou EG. Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB. Cell Signal (2006) 18:83-92. doi:10.1016/j.cellsig.2005.03.017
    • (2006) Cell Signal , vol.18 , pp. 83-92
    • Tzimas, C.1    Michailidou, G.2    Arsenakis, M.3    Kieff, E.4    Mosialos, G.5    Hatzivassiliou, E.G.6
  • 31
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • doi:10.1016/S0092-8674(00)00126-4
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell (2000) 103:351-61. doi:10.1016/S0092-8674(00)00126-4
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6
  • 32
    • 84872202679 scopus 로고    scopus 로고
    • Deubiquitination of NF-kappaB by ubiquitin-specific protease-7 promotes transcription
    • doi:10.1073/pnas.1208446110
    • Colleran A, Collins PE, O'Carroll C, Ahmed A, Mao X, Mcmanus B, et al. Deubiquitination of NF-kappaB by ubiquitin-specific protease-7 promotes transcription. Proc Natl Acad Sci U S A (2013) 110:618-23. doi:10.1073/pnas.1208446110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 618-623
    • Colleran, A.1    Collins, P.E.2    O'Carroll, C.3    Ahmed, A.4    Mao, X.5    Mcmanus, B.6
  • 33
    • 33749023011 scopus 로고    scopus 로고
    • Minimizing the risk of reporting false positives in large-scale RNAi screens
    • doi:10.1038/nmeth1006-777
    • Echeverri CJ, Beachy PA, Baum B, Boutros M, Buchholz F, Chanda SK, et al. Minimizing the risk of reporting false positives in large-scale RNAi screens. Nat Methods (2006) 3:777-9. doi:10.1038/nmeth1006-777
    • (2006) Nat Methods , vol.3 , pp. 777-779
    • Echeverri, C.J.1    Beachy, P.A.2    Baum, B.3    Boutros, M.4    Buchholz, F.5    Chanda, S.K.6
  • 34
    • 84884695491 scopus 로고    scopus 로고
    • Limited agreement of independent RNAi screens for virus-required host genes owes more to false-negative than false-positive factors
    • doi:10.1371/journal.pcbi.1003235
    • Hao L, He Q, Wang Z, Craven M, Newton MA, Ahlquist P. Limited agreement of independent RNAi screens for virus-required host genes owes more to false-negative than false-positive factors. PLoS Comput Biol (2013) 9:e1003235. doi:10.1371/journal.pcbi.1003235
    • (2013) PLoS Comput Biol , vol.9
    • Hao, L.1    He, Q.2    Wang, Z.3    Craven, M.4    Newton, M.A.5    Ahlquist, P.6
  • 35
    • 0035968303 scopus 로고    scopus 로고
    • A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains
    • doi:10.1074/jbc.M100354200
    • Zapata JM, Pawlowski K, Haas E, Ware CF, Godzik A, Reed JC. A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains. J Biol Chem (2001) 276:24242-52. doi:10.1074/jbc.M100354200
    • (2001) J Biol Chem , vol.276 , pp. 24242-24252
    • Zapata, J.M.1    Pawlowski, K.2    Haas, E.3    Ware, C.F.4    Godzik, A.5    Reed, J.C.6
  • 36
    • 84891434091 scopus 로고    scopus 로고
    • Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis
    • doi:10.1128/MCB.00465-13
    • Zaman MM, Nomura T, Takagi T, Okamura T, Jin W, Shinagawa T, et al. Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis. Mol Cell Biol (2013) 33:4971-84. doi:10.1128/MCB.00465-13
    • (2013) Mol Cell Biol , vol.33 , pp. 4971-4984
    • Zaman, M.M.1    Nomura, T.2    Takagi, T.3    Okamura, T.4    Jin, W.5    Shinagawa, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.