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Volumn 13, Issue 5, 2006, Pages 759-772

Good cop, bad cop: The different faces of NF-κB

Author keywords

Cancer; NF B; Phosphorylation; Post translational modification; Signal transduction; Tumor suppressor

Indexed keywords

ANTINEOPLASTIC AGENT; BETA CATENIN; CYCLIN DEPENDENT KINASE INHIBITOR 1; DAUNORUBICIN; DOXORUBICIN; GLUCOCORTICOID; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 45; HYPOXIA INDUCIBLE FACTOR 2ALPHA; I KAPPA B ALPHA; I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; I KAPPA B KINASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; MITOGEN ACTIVATED PROTEIN KINASE; MYELOID DIFFERENTIATION FACTOR 88; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEASOME INHIBITOR; PROTEIN BAX; PROTEIN KINASE B; PROTEIN P50; PROTEIN P53; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR RELA; TRANSCRIPTION FACTOR RELB; TUMOR NECROSIS FACTOR ALPHA; UNINDEXED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 33645971047     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401838     Document Type: Review
Times cited : (439)

References (100)
  • 1
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden MS and Ghosh S (2004) Signaling to NF-κB. Genes Dev. 18: 2195-2224
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-κB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G and Karin M (2004) The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25: 280-288
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 3
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl HL (1999) Activators and target genes of Rel/NF-κB transcription factors. Oncogene 18: 6853-6866
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 4
    • 1642553460 scopus 로고    scopus 로고
    • To be, or not to be: NF-κB is the answer - Role of Rel/NF- κB in the regulation of apoptosis
    • Kucharczak J, Simmons MJ, Fan YJ and Gelinas C (2003) To be, or not to be: NF-κB is the answer - role of Rel/NF- κB in the regulation of apoptosis. Oncogene 22: 8961-8982
    • (2003) Oncogene , vol.22 , pp. 8961-8982
    • Kucharczak, J.1    Simmons, M.J.2    Fan, Y.J.3    Gelinas, C.4
  • 5
    • 0346505340 scopus 로고    scopus 로고
    • The IKK NF-κB system: A treasure trove for drug development
    • Karin M, Yamamoto Y and Wang QM (2004) The IKK NF-κB system: A treasure trove for drug development. Nat. Rev. Drug Discov. 3: 17-26
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 17-26
    • Karin, M.1    Yamamoto, Y.2    Wang, Q.M.3
  • 6
    • 14544269951 scopus 로고    scopus 로고
    • NF-κB in human disease: Current inhibitors and prospects for de novo structure based design of inhibitors
    • Pande V and Ramos MJ (2005) NF-κB in human disease: Current inhibitors and prospects for de novo structure based design of inhibitors. Curr. Med. Chem. 12: 357-374
    • (2005) Curr. Med. Chem. , vol.12 , pp. 357-374
    • Pande, V.1    Ramos, M.J.2
  • 8
    • 0442323562 scopus 로고    scopus 로고
    • NF-κB: Tumor promoter or suppressor?
    • Perkins ND (2004) NF-κB: Tumor promoter or suppressor? Trends Cell. Biol. 14: 64-69
    • (2004) Trends Cell. Biol. , vol.14 , pp. 64-69
    • Perkins, N.D.1
  • 9
    • 0031461976 scopus 로고    scopus 로고
    • Achieving transcriptional specificity with NF-κB
    • Perkins ND (1997) Achieving transcriptional specificity with NF-κB. Int. J. Biochem. Cell. Biol. 29: 1433-1448
    • (1997) Int. J. Biochem. Cell. Biol. , vol.29 , pp. 1433-1448
    • Perkins, N.D.1
  • 10
    • 0038771214 scopus 로고    scopus 로고
    • Modulation of NF-κB activity by exchange of dimers
    • Saccani S, Pantano S and Natoli G (2003) Modulation of NF-κB activity by exchange of dimers. Mol. Cell 11: 1563-1574
    • (2003) Mol. Cell , vol.11 , pp. 1563-1574
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 11
    • 11844269840 scopus 로고    scopus 로고
    • Phosphorylation of NF-κB and IκB proteins: Implications in cancer and inflammation
    • Viatour P, Merville MP, Bours V and Chariot A (2005) Phosphorylation of NF-κB and IκB proteins: Implications in cancer and inflammation. Trends Biochem. Sci. 30: 43-52
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 43-52
    • Viatour, P.1    Merville, M.P.2    Bours, V.3    Chariot, A.4
  • 13
    • 10644248286 scopus 로고    scopus 로고
    • Post-translational modification of RelA(p65) NF-κB
    • Campbell KJ and Perkins ND (2004) Post-translational modification of RelA(p65) NF-κB. Biochem. Soc. Trans. 32: 1087-1089
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 1087-1089
    • Campbell, K.J.1    Perkins, N.D.2
  • 14
    • 0037044575 scopus 로고    scopus 로고
    • The IκB-NF-κB signaling module: Temporal control and selective gene activation
    • Hoffmann A, Levchenko A, Scott ML and Baltimore D (2002) The IκB-NF-κB signaling module: Temporal control and selective gene activation. Science 298: 1241-1245
    • (2002) Science , vol.298 , pp. 1241-1245
    • Hoffmann, A.1    Levchenko, A.2    Scott, M.L.3    Baltimore, D.4
  • 15
    • 0142105387 scopus 로고    scopus 로고
    • Genetic analysis of NF-κB/Rel transcription factors defines functional specificities
    • Hoffmann A, Leung TH and Baltimore D (2003) Genetic analysis of NF-κB/ Rel transcription factors defines functional specificities. EMBO J. 22: 5530-5539
    • (2003) EMBO J. , vol.22 , pp. 5530-5539
    • Hoffmann, A.1    Leung, T.H.2    Baltimore, D.3
  • 17
    • 6344264987 scopus 로고    scopus 로고
    • Lipopolysaccharide activation of the TPL-2/MEK/extracellular signal-regulated kinase mitogen-activated protein kinase cascade is regulated by IκB kinase-induced proteolysis of NF-κB1 p105
    • Beinke S, Robinson MJ, Hugunin M and Ley SC (2004) Lipopolysaccharide activation of the TPL-2/MEK/extracellular signal-regulated kinase mitogen-activated protein kinase cascade is regulated by IκB kinase-induced proteolysis of NF-κB1 p105. Mol. Cell. Biol. 24: 9658-9667
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9658-9667
    • Beinke, S.1    Robinson, M.J.2    Hugunin, M.3    Ley, S.C.4
  • 18
    • 0242298578 scopus 로고    scopus 로고
    • CK2 is a C-terminal IκB kinase responsible for NF-κB activation during the UV response
    • Kato T, Delhase M, Hoffmann A and Karin M (2003) CK2 is a C-terminal IκB kinase responsible for NF-κB activation during the UV response. Mol. Cell 12: 829-839
    • (2003) Mol. Cell , vol.12 , pp. 829-839
    • Kato, T.1    Delhase, M.2    Hoffmann, A.3    Karin, M.4
  • 19
    • 0037112514 scopus 로고    scopus 로고
    • Protein kinase CK2 promotes aberrant activation of nuclear factor-κB, transformed phenotype, and survival of breast cancer cells
    • Romieu-Mourez R, Landesman-Bollag E, Seldin DC and Sonenshein GE (2002) Protein kinase CK2 promotes aberrant activation of nuclear factor-κB, transformed phenotype, and survival of breast cancer cells. Cancer Res. 62: 6770-6778
    • (2002) Cancer Res. , vol.62 , pp. 6770-6778
    • Romieu-Mourez, R.1    Landesman-Bollag, E.2    Seldin, D.C.3    Sonenshein, G.E.4
  • 20
    • 0242664121 scopus 로고    scopus 로고
    • IκB kinase-independent IκBα degradation pathway: Functional NF-κB activity and implications for cancer therapy
    • Tergaonkar V, Bottero V, Ikawa M, Li QT and Verma IM (2003) IκB kinase-independent IκBα degradation pathway: Functional NF-κB activity and implications for cancer therapy. Mol. Cell. Biol. 23: 8070-8083
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8070-8083
    • Tergaonkar, V.1    Bottero, V.2    Ikawa, M.3    Li, Q.T.4    Verma, I.M.5
  • 22
    • 0034655179 scopus 로고    scopus 로고
    • Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress
    • Schoonbroodt S, Ferreira V, Best-Belpomme M, Boelaert JR, Legrand-Poels S, Korner M and Piette J (2000) Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress. J. Immunol. 164: 4292-4300
    • (2000) J. Immunol. , vol.164 , pp. 4292-4300
    • Schoonbroodt, S.1    Ferreira, V.2    Best-Belpomme, M.3    Boelaert, J.R.4    Legrand-Poels, S.5    Korner, M.6    Piette, J.7
  • 23
    • 0034708775 scopus 로고    scopus 로고
    • Pervanadate-induced nuclear factor-κB activation requires tyrosine phosphorylation and degradation of IκBα. Comparison with tumor necrosis factor-α
    • Mukhopadhyay A, Manna SK and Aggarwal BB (2000) Pervanadate-induced nuclear factor-κB activation requires tyrosine phosphorylation and degradation of IκBα. Comparison with tumor necrosis factor-α. J. Biol. Chem. 275: 8549-8555
    • (2000) J. Biol. Chem. , vol.275 , pp. 8549-8555
    • Mukhopadhyay, A.1    Manna, S.K.2    Aggarwal, B.B.3
  • 24
    • 0035911153 scopus 로고    scopus 로고
    • Activation of nuclear factor κB and Bcl-x survival gene expression by nerve growth factor requires tyrosine phosphorylation of IκBα
    • Bui NT, Livolsi A, Peyron JF and Prehn JH (2001) Activation of nuclear factor κB and Bcl-x survival gene expression by nerve growth factor requires tyrosine phosphorylation of IκBα. J. Cell. Biol. 152: 753-764
    • (2001) J. Cell. Biol. , vol.152 , pp. 753-764
    • Bui, N.T.1    Livolsi, A.2    Peyron, J.F.3    Prehn, J.H.4
  • 25
    • 0032491410 scopus 로고    scopus 로고
    • Tumor necrosis factor-α activation of nuclear transcription factor-κB in marrow macrophages is mediated by c-Src tyrosine phosphorylation of IκBα
    • Abu-Amer Y, Ross FP, McHugh KP, Livolsi A, Peyron JF and Teitelbaum SL (1998) Tumor necrosis factor-α activation of nuclear transcription factor-κB in marrow macrophages is mediated by c-Src tyrosine phosphorylation of IκBα. J. Biol. Chem. 273: 29417-29423
    • (1998) J. Biol. Chem. , vol.273 , pp. 29417-29423
    • Abu-Amer, Y.1    Ross, F.P.2    McHugh, K.P.3    Livolsi, A.4    Peyron, J.F.5    Teitelbaum, S.L.6
  • 26
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKK gamma by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress
    • Huang TT, Wuerzbrger-Davis SM, Wu ZH and Miyamoto S (2003) Sequential modification of NEMO/IKK gamma by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress. Cell 115: 565-576
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzbrger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 27
    • 2942716907 scopus 로고    scopus 로고
    • P53 induces NF-κB activation by an IκB kinase-independent mechanism involving phosphorylation of p65 by ribosomal S6 kinase 1
    • Bohuslav J, Chen LF, Kwon H, Mu Y and Greene WC (2004) p53 induces NF-κB activation by an IκB kinase-independent mechanism involving phosphorylation of p65 by ribosomal S6 kinase 1. J. Biol. Chem. 279: 26115-26125
    • (2004) J. Biol. Chem. , vol.279 , pp. 26115-26125
    • Bohuslav, J.1    Chen, L.F.2    Kwon, H.3    Mu, Y.4    Greene, W.C.5
  • 28
    • 2442429408 scopus 로고    scopus 로고
    • Transient and selective NF-κB p65 serine 536 phosphorylation induced by T cell costimulation is mediated by IκB kinase β and controls the kinetics of p65 nuclear import
    • Mattioli I, Sebald A, Bucher C, Charles RP, Nakano H, Doi T, Kracht M and Schmitz ML (2004) Transient and selective NF-κB p65 serine 536 phosphorylation induced by T cell costimulation is mediated by IκB kinase β and controls the kinetics of p65 nuclear import. J. Immunol. 172: 6336-6344
    • (2004) J. Immunol. , vol.172 , pp. 6336-6344
    • Mattioli, I.1    Sebald, A.2    Bucher, C.3    Charles, R.P.4    Nakano, H.5    Doi, T.6    Kracht, M.7    Schmitz, M.L.8
  • 29
    • 27144459692 scopus 로고    scopus 로고
    • Phosphorylation of RelA/p65 on serine 536 defines an IκBα -independent NF-κB pathway
    • Sasaki CY, Barberi TJ, Ghosh P and Longo DL (2005) Phosphorylation of RelA/p65 on serine 536 defines an IκBα -independent NF-κB pathway. J. Biol. Chem. 280: 34538-34547
    • (2005) J. Biol. Chem. , vol.280 , pp. 34538-34547
    • Sasaki, C.Y.1    Barberi, T.J.2    Ghosh, P.3    Longo, D.L.4
  • 30
    • 17844386319 scopus 로고    scopus 로고
    • IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation
    • Lawrence T, Bebien M, Liu GY, Nizet V and Karin M (2005) IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation. Nature 434: 1138-1143
    • (2005) Nature , vol.434 , pp. 1138-1143
    • Lawrence, T.1    Bebien, M.2    Liu, G.Y.3    Nizet, V.4    Karin, M.5
  • 31
    • 3142771914 scopus 로고    scopus 로고
    • Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response
    • Saccani S, Marazzi I, Beg AA and Natoli G (2004) Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. J. Exp. Med. 200: 107-113
    • (2004) J. Exp. Med. , vol.200 , pp. 107-113
    • Saccani, S.1    Marazzi, I.2    Beg, A.A.3    Natoli, G.4
  • 32
    • 6344241039 scopus 로고    scopus 로고
    • SMRT derepression by the IκB kinase α: A prerequisite to NF-κB transcription and survival
    • Hoberg JE, Yeung F and Mayo MW (2004) SMRT derepression by the IκB kinase α: A prerequisite to NF-κB transcription and survival. Mol. Cell 16: 245-255
    • (2004) Mol. Cell , vol.16 , pp. 245-255
    • Hoberg, J.E.1    Yeung, F.2    Mayo, M.W.3
  • 33
    • 15944379896 scopus 로고    scopus 로고
    • Formation of an IKKα-dependent transcription complex is required for estrogen receptor-mediated gene activation
    • Park KJ, Krishnan V, O'Malley BW, Yamamoto Y and Gaynor RB (2005) Formation of an IKKα-dependent transcription complex is required for estrogen receptor-mediated gene activation. Mol. Cell 18: 71-82
    • (2005) Mol. Cell , vol.18 , pp. 71-82
    • Park, K.J.1    Krishnan, V.2    O'Malley, B.W.3    Yamamoto, Y.4    Gaynor, R.B.5
  • 34
    • 22544461297 scopus 로고    scopus 로고
    • Convergent actions of IκB kinase β and protein kinase Cδ modulate mRNA stability through phosphorylation of 14-3-3β complexed with tristetraprolin
    • Gringhuis SI, Garcia-Vallejo JJ, van Het Hof B and van Dijk W (2005) Convergent actions of IκB kinase β and protein kinase Cδ modulate mRNA stability through phosphorylation of 14-3-3β complexed with tristetraprolin. Mol. Cell. Biol. 25: 6454-6463
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6454-6463
    • Gringhuis, S.I.1    Garcia-Vallejo, J.J.2    van Het Hof, B.3    van Dijk, W.4
  • 37
    • 0346497823 scopus 로고    scopus 로고
    • NF-κB RelA opposes epidermal proliferation driven by TNFR1 and JNK
    • Zhang JY, Green CL, Tao S and Khavari PA (2004) NF-κB RelA opposes epidermal proliferation driven by TNFR1 and JNK. Genes Dev. 18: 17-22
    • (2004) Genes Dev. , vol.18 , pp. 17-22
    • Zhang, J.Y.1    Green, C.L.2    Tao, S.3    Khavari, P.A.4
  • 38
    • 0035809983 scopus 로고    scopus 로고
    • IKK α controls formation of the epidermis independently of NF-κB
    • Hu YL, Baud V, Oga T, Kim KII, Yoshida K and Karin M (2001) IKK α controls formation of the epidermis independently of NF-κB. Nature 410: 710-714
    • (2001) Nature , vol.410 , pp. 710-714
    • Hu, Y.L.1    Baud, V.2    Oga, T.3    Kim, K.I.I.4    Yoshida, K.5    Karin, M.6
  • 40
    • 17144420466 scopus 로고    scopus 로고
    • Activity of hypoxia-inducible factor 2α is regulated by association with the NF-κB essential modulator
    • Bracken CP, Whitelaw ML and Peet DJ (2005) Activity of hypoxia-inducible factor 2α is regulated by association with the NF-κB essential modulator. J. Biol. Chem. 280: 14240-14251
    • (2005) J. Biol. Chem. , vol.280 , pp. 14240-14251
    • Bracken, C.P.1    Whitelaw, M.L.2    Peet, D.J.3
  • 41
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38
    • Madrid LV, Mayo MW, Reuther JY and Baldwin AS (2001) Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38. J. Biol. Chem. 276: 18934-18940
    • (2001) J. Biol. Chem. , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin, A.S.4
  • 42
    • 27144477415 scopus 로고    scopus 로고
    • Activated AKT regulates NF-κB activation, p53 inhibition and cell survival in HTLV-1-transformed cells
    • Jeong SJ, Pise-Masison CA, Radonovich MF, Park HU and Brady JN (2005) Activated AKT regulates NF-κB activation, p53 inhibition and cell survival in HTLV-1-transformed cells. Oncogene 24: 6719-6728
    • (2005) Oncogene , vol.24 , pp. 6719-6728
    • Jeong, S.J.1    Pise-Masison, C.A.2    Radonovich, M.F.3    Park, H.U.4    Brady, J.N.5
  • 43
    • 0037064052 scopus 로고    scopus 로고
    • IKKβ and phosphatidylinositol 3-kinase/Akt participate in non-pathogenic Gram-negative enteric bacteria-induced RelA phosphorylation and NF-κB activation in both primary and intestinal epithelial cell lines
    • Haller D, Russo MP, Sartor RB and Jobin C (2002) IKKβ and phosphatidylinositol 3-kinase/Akt participate in non-pathogenic Gram-negative enteric bacteria-induced RelA phosphorylation and NF-κB activation in both primary and intestinal epithelial cell lines. J. Biol. Chem. 277: 38168-38178
    • (2002) J. Biol. Chem. , vol.277 , pp. 38168-38178
    • Haller, D.1    Russo, M.P.2    Sartor, R.B.3    Jobin, C.4
  • 44
    • 0032488837 scopus 로고    scopus 로고
    • P38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor κB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe W, Plaisance S, Boone E, De Bosscher K, Schmitz ML, Fiers W and Haegeman G (1998) p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor κB p65 transactivation mediated by tumor necrosis factor. J. Biol. Chem. 273: 3285-3290
    • (1998) J. Biol. Chem. , vol.273 , pp. 3285-3290
    • Vanden Berghe, W.1    Plaisance, S.2    Boone, E.3    De Bosscher, K.4    Schmitz, M.L.5    Fiers, W.6    Haegeman, G.7
  • 45
    • 0036143654 scopus 로고    scopus 로고
    • P38-dependent marking of inflammatory genes for increased NF-κB recruitment
    • Saccani S, Pantano S and Natoli G (2002) p38-dependent marking of inflammatory genes for increased NF-κB recruitment. Nat. Immunol. 3: 69-75
    • (2002) Nat. Immunol. , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 47
    • 5644264889 scopus 로고    scopus 로고
    • The nuclear factor κB subunits RelA/p65 and c-Rel potentiate but are not required for Ras-induced cellular transformation
    • Hanson JL, Hawke NA, Kashatus D and Baldwin AS (2004) The nuclear factor κB subunits RelA/p65 and c-Rel potentiate but are not required for Ras-induced cellular transformation. Cancer Res. 64: 7248-7255
    • (2004) Cancer Res. , vol.64 , pp. 7248-7255
    • Hanson, J.L.1    Hawke, N.A.2    Kashatus, D.3    Baldwin, A.S.4
  • 48
    • 0037711555 scopus 로고    scopus 로고
    • Mutations within a conserved protein kinase A recognition sequence confer temperature-sensitive and partially defective activities onto mouse c-Rel
    • Gapuzan M-E, Pitoc GA and Gilmore TD (2003) Mutations within a conserved protein kinase A recognition sequence confer temperature-sensitive and partially defective activities onto mouse c-Rel. Biochem. Biophys. Res. Commun. 307: 92-99
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 92-99
    • Gapuzan, M.-E.1    Pitoc, G.A.2    Gilmore, T.D.3
  • 49
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA
    • Ryo A, Suizu F, Yoshida Y, Perrem K, Liou YC, Wulf G, Rottapel R, Yamaoka S and Lu KP (2003) Regulation of NF-κB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA. Mol. Cell 12: 1413-1426
    • (2003) Mol. Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1    Suizu, F.2    Yoshida, Y.3    Perrem, K.4    Liou, Y.C.5    Wulf, G.6    Rottapel, R.7    Yamaoka, S.8    Lu, K.P.9
  • 50
    • 2942702021 scopus 로고    scopus 로고
    • Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-κB activation by protein phosphatase 4-mediated NF-κB p65 Thr dephosphorylation
    • Yeh PY, Yeh KH, Chuang SE, Song YC and Cheng AL (2004) Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-κB activation by protein phosphatase 4-mediated NF-κB p65 Thr dephosphorylation. J. Biol. Chem. 279: 26143-26148
    • (2004) J. Biol. Chem. , vol.279 , pp. 26143-26148
    • Yeh, P.Y.1    Yeh, K.H.2    Chuang, S.E.3    Song, Y.C.4    Cheng, A.L.5
  • 51
    • 17144422434 scopus 로고    scopus 로고
    • Regulation of NF-κB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor
    • Rocha S, Garrett MD, Campbell KJ, Schumm K and Perkins ND (2005) Regulation of NF-κB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor. EMBO J. 24: 1157-1169
    • (2005) EMBO J. , vol.24 , pp. 1157-1169
    • Rocha, S.1    Garrett, M.D.2    Campbell, K.J.3    Schumm, K.4    Perkins, N.D.5
  • 52
    • 0041324898 scopus 로고    scopus 로고
    • The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: Molecular mechanisms for gene repression
    • De Bosscher K, Vanden Berghe W and Haegeman G (2003) The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: Molecular mechanisms for gene repression. Endocr. Rev. 24: 488-522
    • (2003) Endocr. Rev. , vol.24 , pp. 488-522
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 53
    • 1842526076 scopus 로고    scopus 로고
    • Active repression of antiapoptotic gene expression by RelA(p65) NF-κB
    • Campbell KJ, Rocha S and Perkins ND (2004) Active repression of antiapoptotic gene expression by RelA(p65) NF-κB. Mol. Cell 13: 853-865
    • (2004) Mol. Cell , vol.13 , pp. 853-865
    • Campbell, K.J.1    Rocha, S.2    Perkins, N.D.3
  • 54
    • 20144365514 scopus 로고    scopus 로고
    • Nuclear factor-κB induced by doxorubicin is deficient in phosphorylation and acetylation and represses nuclear factor-κB-dependent transcription in cancer cells
    • Ho WC, Dickson KM and Barker PA (2005) Nuclear factor-κB induced by doxorubicin is deficient in phosphorylation and acetylation and represses nuclear factor-κB-dependent transcription in cancer cells. Cancer Res. 65: 4273-4281
    • (2005) Cancer Res. , vol.65 , pp. 4273-4281
    • Ho, W.C.1    Dickson, K.M.2    Barker, P.A.3
  • 58
    • 18244379306 scopus 로고    scopus 로고
    • Interactions of NF-κB with chromatin: The art of being at the right place at the right time
    • Natoli G, Saccani S, Bosisio D and Marazzi I (2005) Interactions of NF-κB with chromatin: The art of being at the right place at the right time. Nat. Immunol. 6: 439-445
    • (2005) Nat. Immunol. , vol.6 , pp. 439-445
    • Natoli, G.1    Saccani, S.2    Bosisio, D.3    Marazzi, I.4
  • 60
    • 0035929147 scopus 로고    scopus 로고
    • Nucleosome sliding via TBP DNA binding in vivo
    • Lomvardas S and Thanos D (2001) Nucleosome sliding via TBP DNA binding in vivo. Cell 106: 685-696
    • (2001) Cell , vol.106 , pp. 685-696
    • Lomvardas, S.1    Thanos, D.2
  • 61
    • 3042834382 scopus 로고    scopus 로고
    • The IκB kinase complex and NF-κB act as master regulators of lipopolysaccharide-induced gene expression and control subordinate activation of AP-1
    • Krappmann D, Wegener E, Sunami Y, Esen M, Thiel A, Mordmuller B and Scheidereit C (2004) The IκB kinase complex and NF-κB act as master regulators of lipopolysaccharide-induced gene expression and control subordinate activation of AP-1. Mol. Cell. Biol. 24: 6488-6500
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6488-6500
    • Krappmann, D.1    Wegener, E.2    Sunami, Y.3    Esen, M.4    Thiel, A.5    Mordmuller, B.6    Scheidereit, C.7
  • 62
    • 4644252538 scopus 로고    scopus 로고
    • One nucleotide in a κB site can determine cofactor specificity for NF-κB dimers
    • Leung TH, Hoffmann A and Baltimore D (2004) One nucleotide in a κB site can determine cofactor specificity for NF-κB dimers. Cell 118: 453-464
    • (2004) Cell , vol.118 , pp. 453-464
    • Leung, T.H.1    Hoffmann, A.2    Baltimore, D.3
  • 63
    • 0141780826 scopus 로고    scopus 로고
    • NF-κB mediates inhibition of mesenchymal cell differentiation through a posttranscriptional gene silencing mechanism
    • Sitcheran R, Cogswell PC and Baldwin Jr AS (2003) NF-κB mediates inhibition of mesenchymal cell differentiation through a posttranscriptional gene silencing mechanism. Genes Dev. 17: 2368-2373
    • (2003) Genes Dev. , vol.17 , pp. 2368-2373
    • Sitcheran, R.1    Cogswell, P.C.2    Baldwin Jr., A.S.3
  • 65
    • 21744444276 scopus 로고    scopus 로고
    • Nucleolar sequestration of RelA (p65) regulates NF-κB-driven transcription and apoptosis
    • Stark LA and Dunlop MG (2005) Nucleolar sequestration of RelA (p65) regulates NF-κB-driven transcription and apoptosis. Mol. Cell. Biol. 25: 5985-6004
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5985-6004
    • Stark, L.A.1    Dunlop, M.G.2
  • 66
    • 26444605834 scopus 로고    scopus 로고
    • IKK/NF-κB signaling: Balancing life and death - A new approach to cancer therapy
    • Luo JL, Kamata H and Karin M (2005) IKK/NF-κB signaling: Balancing life and death - a new approach to cancer therapy. J. Clin. Invest. 115: 2625-2632
    • (2005) J. Clin. Invest. , vol.115 , pp. 2625-2632
    • Luo, J.L.1    Kamata, H.2    Karin, M.3
  • 68
    • 0036599406 scopus 로고    scopus 로고
    • P53 stabilization is decreased upon NFκB activation: A role for NFκB in acquisition of resistance to chemotherapy
    • Tergaonkar V, Pando M, Vafa O, Wahl G and Verma I (2002) p53 stabilization is decreased upon NFκB activation: A role for NFκB in acquisition of resistance to chemotherapy. Cancer Cell 1: 493-503
    • (2002) Cancer Cell , vol.1 , pp. 493-503
    • Tergaonkar, V.1    Pando, M.2    Vafa, O.3    Wahl, G.4    Verma, I.5
  • 69
    • 0034689773 scopus 로고    scopus 로고
    • Role of NF-κB in p53-mediated programmed cell death
    • Ryan KM, Ernst MK, Rice NR and Vousden KH (2000) Role of NF-κB in p53-mediated programmed cell death. Nature 404: 892-897
    • (2000) Nature , vol.404 , pp. 892-897
    • Ryan, K.M.1    Ernst, M.K.2    Rice, N.R.3    Vousden, K.H.4
  • 70
    • 0038409927 scopus 로고    scopus 로고
    • P53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association of the p52 NF-κB subunit with histone deacetylase 1
    • Rocha S, Martin AM, Meek DW and Perkins ND (2003) p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association of the p52 NF-κB subunit with histone deacetylase 1. Mol. Cell. Biol. 23: 4713-4727
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4713-4727
    • Rocha, S.1    Martin, A.M.2    Meek, D.W.3    Perkins, N.D.4
  • 71
    • 0043172452 scopus 로고    scopus 로고
    • P53- and Mdm2-independent repression of NF-κB transactivation by the ARF tumor suppressor
    • Rocha S, Campbell KJ and Perkins ND (2003) p53- and Mdm2-independent repression of NF-κB transactivation by the ARF tumor suppressor. Mol. Cell 12: 15-25
    • (2003) Mol. Cell , vol.12 , pp. 15-25
    • Rocha, S.1    Campbell, K.J.2    Perkins, N.D.3
  • 72
    • 0037061742 scopus 로고    scopus 로고
    • Immortalized embryonic mouse fibroblasts lacking the RelA subunit of transcription factor NF-κB have a malignantly transformed phenotype
    • Gapuzan M-ER, Yufit PV and Gilmore TD (2002) Immortalized embryonic mouse fibroblasts lacking the RelA subunit of transcription factor NF-κB have a malignantly transformed phenotype. Oncogene 21: 2484-2492
    • (2002) Oncogene , vol.21 , pp. 2484-2492
    • Gapuzan, M.-E.R.1    Yufit, P.V.2    Gilmore, T.D.3
  • 73
    • 26944478633 scopus 로고    scopus 로고
    • Immortalized fibroblasts from NF-κB RelA knockout mice show phenotypic heterogeneity and maintain increased sensitivity to tumor necrosis factor α after transformation by v-Ras
    • Gapuzan M-E, Schmah O, Pollock AD, Hoffmann A and Gilmore TD (2005) Immortalized fibroblasts from NF-κB RelA knockout mice show phenotypic heterogeneity and maintain increased sensitivity to tumor necrosis factor α after transformation by v-Ras. Oncogene 24: 6574-6583
    • (2005) Oncogene , vol.24 , pp. 6574-6583
    • Gapuzan, M.-E.1    Schmah, O.2    Pollock, A.D.3    Hoffmann, A.4    Gilmore, T.D.5
  • 74
    • 3042780178 scopus 로고    scopus 로고
    • Loss of nuclear factor-κB is tumor promoting but does not substitute for loss of p53
    • Ryan KM, O'Prey J and Vousden KH (2004) Loss of nuclear factor-κB is tumor promoting but does not substitute for loss of p53. Cancer Res. 64: 4415-4418
    • (2004) Cancer Res. , vol.64 , pp. 4415-4418
    • Ryan, K.M.1    O'Prey, J.2    Vousden, K.H.3
  • 78
    • 0037192829 scopus 로고    scopus 로고
    • PTEN blocks tumor necrosis factor-induced NF-κB-dependent transcription by inhibiting the transactivation potential of the p65 subunit
    • Mayo MW, Madrid LV, Westerheide SD, Jones DR, Yuan XJ, Baldwin Jr AS and Whang YE (2002) PTEN blocks tumor necrosis factor-induced NF-κB-dependent transcription by inhibiting the transactivation potential of the p65 subunit. J. Biol. Chem. 277: 11116-11125
    • (2002) J. Biol. Chem. , vol.277 , pp. 11116-11125
    • Mayo, M.W.1    Madrid, L.V.2    Westerheide, S.D.3    Jones, D.R.4    Yuan, X.J.5    Baldwin Jr., A.S.6    Whang, Y.E.7
  • 79
    • 0035139943 scopus 로고    scopus 로고
    • Hostile takeovers: Viral appropriation of the NF-κB pathway
    • Hiscott J, Kwon H and Genin P (2001) Hostile takeovers: Viral appropriation of the NF-κB pathway. J. Clin. Invest. 107: 143-151
    • (2001) J. Clin. Invest. , vol.107 , pp. 143-151
    • Hiscott, J.1    Kwon, H.2    Genin, P.3
  • 83
    • 0036782443 scopus 로고    scopus 로고
    • A novel protein overexpressed in hepatoma accelerates export of NF-κB from the nucleus and inhibits p53-dependent apoptosis
    • Higashitsuji H, Nagao T, Nonoguchi K, Fujii S, Itoh K and Fujita J (2002) A novel protein overexpressed in hepatoma accelerates export of NF-κB from the nucleus and inhibits p53-dependent apoptosis. Cancer Cell 2: 335-346
    • (2002) Cancer Cell , vol.2 , pp. 335-346
    • Higashitsuji, H.1    Nagao, T.2    Nonoguchi, K.3    Fujii, S.4    Itoh, K.5    Fujita, J.6
  • 86
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, Honda S, Maeda S, Chang L, Hirata H and Karin M (2005) Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120: 649-661
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 88
    • 0033565763 scopus 로고    scopus 로고
    • Squamous cell carcinomas and increased apoptosis in skin with inhibited Rel/nuclear factor-κB signaling
    • van Hogerlinden M, Rozell BL, Ährlund-Richter L and Toftgård R (1999) Squamous cell carcinomas and increased apoptosis in skin with inhibited Rel/nuclear factor-κB signaling. Cancer Res. 59: 3299-3303
    • (1999) Cancer Res. , vol.59 , pp. 3299-3303
    • van Hogerlinden, M.1    Rozell, B.L.2    Ährlund-Richter, L.3    Toftgård, R.4
  • 90
    • 13944253943 scopus 로고    scopus 로고
    • CDK4 regulation by TNFR1 and JNK is required for NF-κB-mediated epidermal growth control
    • Zhang JY, Tao S, Kimmel R and Khavari PA (2005) CDK4 regulation by TNFR1 and JNK is required for NF-κB-mediated epidermal growth control. J. Cell. Biol. 168: 561-566
    • (2005) J. Cell. Biol. , vol.168 , pp. 561-566
    • Zhang, J.Y.1    Tao, S.2    Kimmel, R.3    Khavari, P.A.4
  • 91
    • 0037417129 scopus 로고    scopus 로고
    • Divergent gene regulation and growth effects by NF-κB in epithelial and mesenchymal cells of human skin
    • Hinata K, Gervin AM, Zhang YJ and Khavari PA (2003) Divergent gene regulation and growth effects by NF-κB in epithelial and mesenchymal cells of human skin. Oncogene 22: 1955-1964
    • (2003) Oncogene , vol.22 , pp. 1955-1964
    • Hinata, K.1    Gervin, A.M.2    Zhang, Y.J.3    Khavari, P.A.4
  • 92
    • 21244472975 scopus 로고    scopus 로고
    • IKKβ couples hepatocyte death to cytokine-driven compensatory proliferation that promotes chemical hepatocarcinogenesis
    • Maeda S, Kamata H, Luo JL, Leffert H and Karin M (2005) IKKβ couples hepatocyte death to cytokine-driven compensatory proliferation that promotes chemical hepatocarcinogenesis. Cell 121: 977-990
    • (2005) Cell , vol.121 , pp. 977-990
    • Maeda, S.1    Kamata, H.2    Luo, J.L.3    Leffert, H.4    Karin, M.5
  • 95
    • 0035861314 scopus 로고    scopus 로고
    • IKKα provides an essential link between RANK signaling and cyclin D1 expression during mammary gland development
    • Cao YX, Bonizzi G, Seagroves TN, Greten FR, Johnson R, Schmidt EV and Karin M (2001) IKKα provides an essential link between RANK signaling and cyclin D1 expression during mammary gland development. Cell 107: 763-775
    • (2001) Cell , vol.107 , pp. 763-775
    • Cao, Y.X.1    Bonizzi, G.2    Seagroves, T.N.3    Greten, F.R.4    Johnson, R.5    Schmidt, E.V.6    Karin, M.7
  • 98
    • 0032905030 scopus 로고    scopus 로고
    • Control of inducible chemoresistance: Enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-κB
    • Wang CY, Cusack Jr JC, Liu R and Baldwin Jr AS (1999) Control of inducible chemoresistance: Enhanced anti-tumor therapy through increased apoptosis by inhibition of NF-κB. Nat Med 5: 412-417
    • (1999) Nat Med , vol.5 , pp. 412-417
    • Wang, C.Y.1    Cusack Jr., J.C.2    Liu, R.3    Baldwin Jr., A.S.4
  • 99
    • 31044445246 scopus 로고    scopus 로고
    • Inhibition of transcription factor NF-κB signaling proteins IKKβ and p65 through specific cysteine residues by epoxyquinone A monomer: Correlation with its anti-cancer cell growth activity
    • in press
    • Liang M-C, Bardhan S, Porco Jr JA and Gilmore TD (2006) Inhibition of transcription factor NF-κB signaling proteins IKKβ and p65 through specific cysteine residues by epoxyquinone A monomer: Correlation with its anti-cancer cell growth activity. Biochem. Pharmacol., in press
    • (2006) Biochem. Pharmacol.
    • Liang, M.-C.1    Bardhan, S.2    Porco Jr., J.A.3    Gilmore, T.D.4


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