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Volumn 15, Issue 1, 2014, Pages 46-61

The IκB kinase complex in NF-κB regulation and beyond

Author keywords

Cancer; Development; Differentiation; Immunity; Inflammation

Indexed keywords

I KAPPA B KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; UBIQUITIN;

EID: 84894534156     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1002/embr.201337983     Document Type: Review
Times cited : (427)

References (171)
  • 1
    • 84858726313 scopus 로고    scopus 로고
    • Regulation of cell death and autophagy by ikk and nf-kappab: Critical mechanisms in immune function and cancer
    • Baldwin AS (2012) Regulation of cell death and autophagy by IKK and NF-kappaB: critical mechanisms in immune function and cancer. Immunol Rev 246: 327-345
    • (2012) Immunol Rev , vol.246 , pp. 327-345
    • Baldwin, A.S.1
  • 2
    • 33750454819 scopus 로고    scopus 로고
    • Mutations in the nf-kappab signaling pathway: Implications for human disease
    • Courtois G, Gilmore TD (2006) Mutations in the NF-kappaB signaling pathway: implications for human disease. Oncogene 25: 6831-6843
    • (2006) Oncogene , vol.25 , pp. 6831-6843
    • Courtois, G.1    Gilmore, T.D.2
  • 3
    • 84856641109 scopus 로고    scopus 로고
    • Nf-kappab the first quarter-century: Remarkable progress and outstanding questions
    • Hayden MS, Ghosh S (2012) NF-kappaB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev 26: 203-234
    • (2012) Genes Dev , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 4
    • 84858744393 scopus 로고    scopus 로고
    • It takes two to tango: Ikappabs, the multifunctional partners of nf-kappab
    • Hinz M, Arslan SC, Scheidereit C (2012) It takes two to tango: IkappaBs, the multifunctional partners of NF-kappaB. Immunol Rev 246: 59-76
    • (2012) Immunol Rev , vol.246 , pp. 59-76
    • Hinz, M.1    Arslan, S.C.2    Scheidereit, C.3
  • 5
    • 84858739354 scopus 로고    scopus 로고
    • Regulation of nf-kappab by ubiquitination and degradation of the ikappabs
    • Kanarek N, Ben-Neriah Y (2012) Regulation of NF-kappaB by ubiquitination and degradation of the IkappaBs. Immunol Rev 246: 77-94
    • (2012) Immunol Rev , vol.246 , pp. 77-94
    • Kanarek, N.1    Ben-Neriah, Y.2
  • 6
    • 0033199348 scopus 로고    scopus 로고
    • Nf-kappab p105 is a target of ikappab kinases and controls signal induction of bcl-3-p50 complexes
    • Heissmeyer V, Krappmann D, Wulczyn FG, Scheidereit C (1999) NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes. EMBO J 18: 4766-4778
    • (1999) EMBO J , vol.18 , pp. 4766-4778
    • Heissmeyer, V.1    Krappmann, D.2    Wulczyn, F.G.3    Scheidereit, C.4
  • 7
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of ikappabalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen ZJ, Parent L, Maniatis T (1996) Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 84: 853-862
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 8
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive ikappab kinase that activates the transcription factor nf-kappab
    • DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M (1997) A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 388: 548-554
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 11
    • 0030611595 scopus 로고    scopus 로고
    • Ikappab kinase-beta: Nf-kappab activation and complex formation with ikappab kinase-alpha and nik
    • Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV (1997) IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK. Science 278: 866-869
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 12
    • 0030613551 scopus 로고    scopus 로고
    • The ikappab kinase complex (ikk) contains two kinase subunits, ikkalpha and ikkbeta, necessary for ikappab phosphorylation and nf-kappab activation
    • Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M (1997) The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91: 243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 13
    • 0032575379 scopus 로고    scopus 로고
    • Direct phosphorylation of ikappab by ikkalpha and ikkbeta: Discrimination between free and nf-kappabbound substrate
    • Zandi E, Chen Y, Karin M (1998) Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaBbound substrate. Science 281: 1360-1363
    • (1998) Science , vol.281 , pp. 1360-1363
    • Zandi, E.1    Chen, Y.2    Karin, M.3
  • 14
    • 0032541657 scopus 로고    scopus 로고
    • Ikk-gamma is an essential regulatory subunit of the ikappab kinase complex
    • Rothwarf DM, Zandi E, Natoli G, Karin M (1998) IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex. Nature 395: 297-300
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 15
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of nemo, a component of the ikappab kinase complex essential for nf-kappab activation
    • Yamaoka S, Courtois G, Bessia C, Whiteside ST, Weil R, Agou F, Kirk HE, Kay RJ, Israel A (1998) Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93: 1231-1240
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israel, A.9
  • 18
    • 56349164232 scopus 로고    scopus 로고
    • Nonredundant and complementary functions of traf2 and traf3 in a ubiquitination cascade that activates nik-dependent alternative nf-kappab signaling
    • Vallabhapurapu S, Matsuzawa A, Zhang W, Tseng PH, Keats JJ, Wang H, Vignali DA, Bergsagel PL, Karin M (2008) Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling. Nat Immunol 9: 1364-1370
    • (2008) Nat Immunol , vol.9 , pp. 1364-1370
    • Vallabhapurapu, S.1    Matsuzawa, A.2    Zhang, W.3    Tseng, P.H.4    Keats, J.J.5    Wang, H.6    Vignali, D.A.7    Bergsagel, P.L.8    Karin, M.9
  • 20
    • 84858735072 scopus 로고    scopus 로고
    • The noncanonical nf-kappab pathway
    • Sun SC (2012) The noncanonical NF-kappaB pathway. Immunol Rev 246: 125-140
    • (2012) Immunol Rev , vol.246 , pp. 125-140
    • Sun, S.C.1
  • 22
    • 77957252647 scopus 로고    scopus 로고
    • The ikk complex, a central regulator of nf-kappab activation
    • Israel A (2010) The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb Perspect Biol 2: a000158
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Israel, A.1
  • 23
    • 33750443289 scopus 로고    scopus 로고
    • Ikappab kinase complexes: Gateways to nf-kappab activation and transcription
    • Scheidereit C (2006) IkappaB kinase complexes: gateways to NF-kappaB activation and transcription. Oncogene 25: 6685-6705
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 24
    • 1942484963 scopus 로고    scopus 로고
    • Ikappab kinase-alpha acts in the epidermis to control skeletal and craniofacial morphogenesis
    • Sil AK, Maeda S, Sano Y, Roop DR, Karin M (2004) IkappaB kinase-alpha acts in the epidermis to control skeletal and craniofacial morphogenesis. Nature 428: 660-664
    • (2004) Nature , vol.428 , pp. 660-664
    • Sil, A.K.1    Maeda, S.2    Sano, Y.3    Roop, D.R.4    Karin, M.5
  • 25
    • 0032583947 scopus 로고    scopus 로고
    • Nf-kappab-inducing kinase activates ikk-alpha by phosphorylation of ser-176
    • Ling L, Cao Z, Goeddel DV (1998) NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176. Proc Natl Acad Sci U S A 95: 3792-3797
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 26
    • 8544230698 scopus 로고    scopus 로고
    • A novel ubiquitin-like domain in ikappab kinase beta is required for functional activity of the kinase
    • May MJ, Larsen SE, Shim JH, Madge LA, Ghosh S (2004) A novel ubiquitin-like domain in IkappaB kinase beta is required for functional activity of the kinase. J Biol Chem 279: 45528-45539
    • (2004) J Biol Chem , vol.279 , pp. 45528-45539
    • May, M.J.1    Larsen, S.E.2    Shim, J.H.3    Madge, L.A.4    Ghosh, S.5
  • 30
    • 51249095133 scopus 로고    scopus 로고
    • The ikk-related kinases: From innate immunity to oncogenesis
    • Clement JF, Meloche S, Servant MJ (2008) The IKK-related kinases: from innate immunity to oncogenesis. Cell Res 18: 889-899
    • (2008) Cell Res , vol.18 , pp. 889-899
    • Clement, J.F.1    Meloche, S.2    Servant, M.J.3
  • 34
    • 84863840549 scopus 로고    scopus 로고
    • Nemo ensures signaling specificity of the pleiotropic ikkbeta by directing its kinase activity toward ikappabalpha
    • Schrofelbauer B, Polley S, Behar M, Ghosh G, Hoffmann A (2012) NEMO ensures signaling specificity of the pleiotropic IKKbeta by directing its kinase activity toward IkappaBalpha. Mol Cell 47: 111-121
    • (2012) Mol Cell , vol.47 , pp. 111-121
    • Schrofelbauer, B.1    Polley, S.2    Behar, M.3    Ghosh, G.4    Hoffmann, A.5
  • 35
    • 3142546430 scopus 로고    scopus 로고
    • The trimerization domain of nemo is composed of the interacting c-terminal cc2 and lz coiled-coil subdomains
    • Agou F, Traincard F, Vinolo E, Courtois G, Yamaoka S, Israel A, Veron M (2004) The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains. J Biol Chem 279: 27861-27869
    • (2004) J Biol Chem , vol.279 , pp. 27861-27869
    • Agou, F.1    Traincard, F.2    Vinolo, E.3    Courtois, G.4    Yamaoka, S.5    Israel, A.6    Veron, M.7
  • 36
    • 0037332580 scopus 로고    scopus 로고
    • Tetrameric oligomerization of ikappab kinase gamma (ikkgamma) is obligatory for ikk complex activity and nf-kappab activation
    • Tegethoff S, Behlke J, Scheidereit C (2003) Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation. Mol Cell Biol 23: 2029-2041
    • (2003) Mol Cell Biol , vol.23 , pp. 2029-2041
    • Tegethoff, S.1    Behlke, J.2    Scheidereit, C.3
  • 42
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of ikk
    • Chen ZJ (2012) Ubiquitination in signaling to and activation of IKK. Immunol Rev 246: 95-106
    • (2012) Immunol Rev , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 43
    • 84858113865 scopus 로고    scopus 로고
    • No one can whistle a symphony alone-how different ubiquitin linkages cooperate to orchestrate nf-kappab activity
    • Schmukle AC, Walczak H (2012) No one can whistle a symphony alone-how different ubiquitin linkages cooperate to orchestrate NF-kappaB activity. J Cell Sci 125: 549-559
    • (2012) J Cell Sci , vol.125 , pp. 549-559
    • Schmukle, A.C.1    Walczak, H.2
  • 48
    • 70350020147 scopus 로고    scopus 로고
    • Nemo specifically recognizes k63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine E, Fontan E, Chiaravalli J, Lopez T, Lakisic G, Veron M, Agou F, Israel A (2009) NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J 28: 2885-2895
    • (2009) EMBO J , vol.28 , pp. 2885-2895
    • Laplantine, E.1    Fontan, E.2    Chiaravalli, J.3    Lopez, T.4    Lakisic, G.5    Veron, M.6    Agou, F.7    Israel, A.8
  • 49
    • 40849140675 scopus 로고    scopus 로고
    • Solution structure of nemo zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation
    • Cordier F, Vinolo E, Veron M, Delepierre M, Agou F (2008) Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation. J Mol Biol 377: 1419-1432
    • (2008) J Mol Biol , vol.377 , pp. 1419-1432
    • Cordier, F.1    Vinolo, E.2    Veron, M.3    Delepierre, M.4    Agou, F.5
  • 51
    • 84863621364 scopus 로고    scopus 로고
    • Analysis of nuclear factor-kappab (nf-kappab) essential modulator (nemo) binding to linear and lysine-linked ubiquitin chains and its role in the activation of nf-kappab
    • Kensche T, Tokunaga F, Ikeda F, Goto E, Iwai K, Dikic I (2012) Analysis of nuclear factor-kappaB (NF-kappaB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-kappaB. J Biol Chem 287: 23626-23634
    • (2012) J Biol Chem , vol.287 , pp. 23626-23634
    • Kensche, T.1    Tokunaga, F.2    Ikeda, F.3    Goto, E.4    Iwai, K.5    Dikic, I.6
  • 53
    • 36148967696 scopus 로고    scopus 로고
    • Signal responsiveness of ikappab kinases is determined by cdc37-assisted transient interaction with hsp90
    • Hinz M, Broemer M, Arslan SC, Otto A, Mueller EC, Dettmer R, Scheidereit C (2007) Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90. J Biol Chem 282: 32311-32319
    • (2007) J Biol Chem , vol.282 , pp. 32311-32319
    • Hinz, M.1    Broemer, M.2    Arslan, S.C.3    Otto, A.4    Mueller, E.C.5    Dettmer, R.6    Scheidereit, C.7
  • 55
    • 0035965199 scopus 로고    scopus 로고
    • Complete reconstitution of human ikappab kinase (ikk) complex in yeast. Assessment of its stoichiometry and the role of ikkgamma on the complex activity in the absence of stimulation
    • Miller BS, Zandi E (2001) Complete reconstitution of human IkappaB kinase (IKK) complex in yeast. Assessment of its stoichiometry and the role of IKKgamma on the complex activity in the absence of stimulation. J Biol Chem 276: 36320-36326
    • (2001) J Biol Chem , vol.276 , pp. 36320-36326
    • Miller, B.S.1    Zandi, E.2
  • 58
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of nf-kappab transcription factors in the immune system
    • Vallabhapurapu S, Karin M (2009) Regulation and function of NF-kappaB transcription factors in the immune system. Annu Rev Immunol 27: 693-733
    • (2009) Annu Rev Immunol , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 60
    • 84860672660 scopus 로고    scopus 로고
    • Kaposi's sarcoma associated herpesvirus encoded viral flice inhibitory protein k13 activates nf-kappab pathway independent of traf6, tak1 and lubac
    • Matta H, Gopalakrishnan R, Graham C, Tolani B, Khanna A, Yi H, Suo Y, Chaudhary PM (2012) Kaposi's sarcoma associated herpesvirus encoded viral FLICE inhibitory protein K13 activates NF-kappaB pathway independent of TRAF6, TAK1 and LUBAC. PLoS ONE 7: e36601
    • (2012) PLoS ONE , vol.7
    • Matta, H.1    Gopalakrishnan, R.2    Graham, C.3    Tolani, B.4    Khanna, A.5    Yi, H.6    Suo, Y.7    Chaudhary, P.M.8
  • 61
    • 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
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103: 351-361
    • (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    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 63
    • 0346496017 scopus 로고    scopus 로고
    • Differential regulation of interleukin 1 receptor and toll-like receptor signaling by mekk3
    • Huang Q, Yang J, Lin Y, Walker C, Cheng J, Liu ZG, Su B (2004) Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3. Nat Immunol 5: 98-103
    • (2004) Nat Immunol , vol.5 , pp. 98-103
    • Huang, Q.1    Yang, J.2    Lin, Y.3    Walker, C.4    Cheng, J.5    Liu, Z.G.6    Su, B.7
  • 67
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of ikappab kinase activity through ikkbeta subunit phosphorylation
    • Delhase M, Hayakawa M, Chen Y, Karin M (1999) Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science 284: 309-313
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 68
    • 58149178554 scopus 로고    scopus 로고
    • Traf6 autoubiquitination-independent activation of the nfkappab and mapk pathways in response to il-1 and rankl
    • Walsh MC, Kim GK, Maurizio PL, Molnar EE, Choi Y (2008) TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL. PLoS ONE 3: e4064
    • (2008) PLoS ONE , vol.3
    • Walsh, M.C.1    Kim, G.K.2    Maurizio, P.L.3    Molnar, E.E.4    Choi, Y.5
  • 70
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of ikk activation by tnfalpha and il-1beta
    • Xu M, Skaug B, Zeng W, Chen ZJ (2009) A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta. Mol Cell 36: 302-314
    • (2009) Mol Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 73
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in nf-kappab activation
    • Iwai K (2012) Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol 22: 355-364
    • (2012) Trends Cell Biol , vol.22 , pp. 355-364
    • Iwai, K.1
  • 80
    • 0141621240 scopus 로고    scopus 로고
    • A role for nf-kappab essential modifier/ikappab kinase-gamma (nemo/ikkgamma) ubiquitination in the activation of the ikappab kinase complex by tumor necrosis factor-alpha
    • Tang ED, Wang CY, Xiong Y, Guan KL (2003) A role for NF-kappaB essential modifier/IkappaB kinase-gamma (NEMO/IKKgamma) ubiquitination in the activation of the IkappaB kinase complex by tumor necrosis factor-alpha. J Biol Chem 278: 37297-37305
    • (2003) J Biol Chem , vol.278 , pp. 37297-37305
    • Tang, E.D.1    Wang, C.Y.2    Xiong, Y.3    Guan, K.L.4
  • 81
    • 33646034316 scopus 로고    scopus 로고
    • Activation of ikk by tnfalpha requires site-specific ubiquitination of rip1 and polyubiquitin binding by nemo
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ (2006) Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 22: 245-257
    • (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
  • 83
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of lys 63-linked polyubiquitination by nemo is a key event in nf-kappab activation [corrected]
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD (2006) Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol 8: 398-406
    • (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
  • 85
    • 77957333810 scopus 로고    scopus 로고
    • A cytoplasmic atm-traf6-ciap1 module links nuclear dna damage signaling to ubiquitin-mediated nf-kappab activation
    • Hinz M, Stilmann M, Arslan SC, Khanna KK, Dittmar G, Scheidereit C (2010) A cytoplasmic ATM-TRAF6-cIAP1 module links nuclear DNA damage signaling to ubiquitin-mediated NF-kappaB activation. Mol Cell 40: 63-74
    • (2010) Mol Cell , vol.40 , pp. 63-74
    • Hinz, M.1    Stilmann, M.2    Arslan, S.C.3    Khanna, K.K.4    Dittmar, G.5    Scheidereit, C.6
  • 86
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of nemo/ikkgamma by sumo-1 and ubiquitin mediates nf-kappab activation by genotoxic stress
    • Huang TT, Wuerzberger-Davis SM, Wu ZH, Miyamoto S (2003) Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 115: 565-576
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 88
    • 84877757564 scopus 로고    scopus 로고
    • Molecular basis of nf-kappab signaling
    • Napetschnig J, Wu H (2013) Molecular basis of NF-kappaB signaling. Annu Rev Biophys 42: 443-468
    • (2013) Annu Rev Biophys , vol.42 , pp. 443-468
    • Napetschnig, J.1    Wu, H.2
  • 89
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the myd88-irak4-irak2 complex in tlr/il-1r signalling
    • Lin SC, Lo YC, Wu H (2010) Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 465: 885-890
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 90
    • 79961133270 scopus 로고    scopus 로고
    • Mavs forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146: 448-461
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6
  • 92
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • WuH(2013) Higher-order assemblies in a new paradigm of signal transduction. Cell 153: 287-292
    • (2013) Cell , vol.153 , pp. 287-292
    • Wu, H.1
  • 93
    • 38049028109 scopus 로고    scopus 로고
    • Phosphorylation of serine 68 in the ikappab kinase (ikk)-binding domain of nemo interferes with the structure of the ikk complex and tumor necrosis factor-alpha-induced nf-kappab activity
    • Palkowitsch L, Leidner J, Ghosh S, Marienfeld RB (2008) Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-alpha-induced NF-kappaB activity. J Biol Chem 283: 76-86
    • (2008) J Biol Chem , vol.283 , pp. 76-86
    • Palkowitsch, L.1    Leidner, J.2    Ghosh, S.3    Marienfeld, R.B.4
  • 94
    • 33744948611 scopus 로고    scopus 로고
    • Regulation of ikappab kinase (ikk) complex by ikkgamma-dependent phosphorylation of the t-loop and c terminus of ikkbeta
    • Schomer-Miller B, Higashimoto T, Lee YK, Zandi E (2006) Regulation of IkappaB kinase (IKK) complex by IKKgamma-dependent phosphorylation of the T-loop and C terminus of IKKbeta. J Biol Chem 281: 15268-15276
    • (2006) J Biol Chem , vol.281 , pp. 15268-15276
    • Schomer-Miller, B.1    Higashimoto, T.2    Lee, Y.K.3    Zandi, E.4
  • 95
    • 33846528701 scopus 로고    scopus 로고
    • Negative feedback loop in t cell activation through ikappab kinase-induced phosphorylation and degradation of bcl10
    • Lobry C, Lopez T, Israel A, Weil R (2007) Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10. Proc Natl Acad Sci U S A 104: 908-913
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 908-913
    • Lobry, C.1    Lopez, T.2    Israel, A.3    Weil, R.4
  • 97
    • 34547924464 scopus 로고    scopus 로고
    • Optineurin negatively regulates tnfalpha-induced nf-kappab activation by competing with nemo for ubiquitinated rip
    • Zhu G, Wu CJ, Zhao Y, Ashwell JD (2007) Optineurin negatively regulates TNFalpha-induced NF-kappaB activation by competing with NEMO for ubiquitinated RIP. Curr Biol 17: 1438-1443
    • (2007) Curr Biol , vol.17 , pp. 1438-1443
    • Zhu, G.1    Wu, C.J.2    Zhao, Y.3    Ashwell, J.D.4
  • 99
    • 84867032420 scopus 로고    scopus 로고
    • P47 negatively regulates ikk activation by inducing the lysosomal degradation of polyubiquitinated nemo
    • Shibata Y, Oyama M, Kozuka-Hata H, Han X, Tanaka Y, Gohda J, Inoue J (2012) p47 negatively regulates IKK activation by inducing the lysosomal degradation of polyubiquitinated NEMO. Nat Commun 3: 1061
    • (2012) Nat Commun , vol.3 , pp. 1061
    • Shibata, Y.1    Oyama, M.2    Kozuka-Hata, H.3    Han, X.4    Tanaka, Y.5    Gohda, J.6    Inoue, J.7
  • 100
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of nf-kappab by deubiquitinases
    • Harhaj EW, Dixit VM (2012) Regulation of NF-kappaB by deubiquitinases. Immunol Rev 246: 107-124
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 101
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase cezanne
    • Bremm A, Freund SM, Komander D (2010) Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat Struct Mol Biol 17: 939-947
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 103
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappab activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G, Tan X, Wang H, Sun W, Shi Y, Burlingame S, Gu X, Cao G, Zhang T, Qin J, Yang J (2010) Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 285: 969-978
    • (2010) J Biol Chem , vol.285 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6    Gu, X.7    Cao, G.8    Zhang, T.9    Qin, J.10    Yang, J.11
  • 107
    • 79960468868 scopus 로고    scopus 로고
    • Nf-kappab induction of the sumo protease senp2: A negative feedback loop to attenuate cell survival response to genotoxic stress
    • Lee MH, Mabb AM, Gill GB, Yeh ET, Miyamoto S (2011) NF-kappaB induction of the SUMO protease SENP2: a negative feedback loop to attenuate cell survival response to genotoxic stress. Mol Cell 43: 180-191
    • (2011) Mol Cell , vol.43 , pp. 180-191
    • Lee, M.H.1    Mabb, A.M.2    Gill, G.B.3    Yeh, E.T.4    Miyamoto, S.5
  • 108
    • 0033537739 scopus 로고    scopus 로고
    • Severe liver degeneration in mice lacking the ikappab kinase 2 gene
    • Li Q, Van Antwerp D, Mercurio F, Lee KF, Verma IM (1999) Severe liver degeneration in mice lacking the IkappaB kinase 2 gene. Science 284: 321-325
    • (1999) Science , vol.284 , pp. 321-325
    • Li, Q.1    Van Antwerp, D.2    Mercurio, F.3    Lee, K.F.4    Verma, I.M.5
  • 109
    • 0033532386 scopus 로고    scopus 로고
    • The ikkbeta subunit of ikappab kinase (ikk) is essential for nuclear factor kappab activation and prevention of apoptosis
    • Li ZW, Chu W, Hu Y, Delhase M, Deerinck T, Ellisman M, Johnson R, Karin M (1999) The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis. J Exp Med 189: 1839-1845
    • (1999) J Exp Med , vol.189 , pp. 1839-1845
    • Li, Z.W.1    Chu, W.2    Hu, Y.3    Delhase, M.4    Deerinck, T.5    Ellisman, M.6    Johnson, R.7    Karin, M.8
  • 110
    • 34247874508 scopus 로고    scopus 로고
    • Interleukin-1-induced nfkappab activation is nemo-dependent but does not require ikkbeta
    • Solt LA, Madge LA, Orange JS, May MJ (2007) Interleukin-1-induced NFkappaB activation is NEMO-dependent but does not require IKKbeta. J Biol Chem 282: 8724-8733
    • (2007) J Biol Chem , vol.282 , pp. 8724-8733
    • Solt, L.A.1    Madge, L.A.2    Orange, J.S.3    May, M.J.4
  • 112
    • 54349102235 scopus 로고    scopus 로고
    • Ikkalpha, a critical regulator of epidermal differentiation and a suppressor of skin cancer
    • Descargues P, Sil AK, Karin M (2008) IKKalpha, a critical regulator of epidermal differentiation and a suppressor of skin cancer. EMBO J 27: 2639-2647
    • (2008) EMBO J , vol.27 , pp. 2639-2647
    • Descargues, P.1    Sil, A.K.2    Karin, M.3
  • 113
    • 33751217161 scopus 로고    scopus 로고
    • A critical role for i kappab kinase alpha in the development of human and mouse squamous cell carcinomas
    • Liu B, Park E, Zhu F, Bustos T, Liu J, Shen J, Fischer SM, Hu Y (2006) A critical role for I kappaB kinase alpha in the development of human and mouse squamous cell carcinomas. Proc Natl Acad Sci U S A 103: 17202-17207
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17202-17207
    • Liu, B.1    Park, E.2    Zhu, F.3    Bustos, T.4    Liu, J.5    Shen, J.6    Fischer, S.M.7    Hu, Y.8
  • 117
    • 84858722471 scopus 로고    scopus 로고
    • Dna damage-dependent nf-kappab activation: Nemo turns nuclear signaling inside out
    • McCool KW, Miyamoto S (2012) DNA damage-dependent NF-kappaB activation: NEMO turns nuclear signaling inside out. Immunol Rev 246: 311-326
    • (2012) Immunol Rev , vol.246 , pp. 311-326
    • McCool, K.W.1    Miyamoto, S.2
  • 118
    • 17844386319 scopus 로고    scopus 로고
    • Ikkalpha limits macrophage nf-kappab activation and contributes to the resolution of inflammation
    • Lawrence T, Bebien M, Liu GY, Nizet V, Karin M (2005) IKKalpha limits macrophage NF-kappaB 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
  • 119
    • 0032589462 scopus 로고    scopus 로고
    • Ikappab kinases phosphorylate nf-kappab p65 subunit on serine 536 in the transactivation domain
    • Sakurai H, Chiba H, Miyoshi H, Sugita T, Toriumi W (1999) IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 274: 30353-30356
    • (1999) J Biol Chem , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 120
    • 68749103771 scopus 로고    scopus 로고
    • The nf-kappab-independent functions of ikk subunits in immunity and cancer
    • Chariot A (2009) The NF-kappaB-independent functions of IKK subunits in immunity and cancer. Trends Cell Biol 19: 404-413
    • (2009) Trends Cell Biol , vol.19 , pp. 404-413
    • Chariot, A.1
  • 122
    • 33749263685 scopus 로고    scopus 로고
    • Ikkalpha stabilizes cytosolic beta-catenin by inhibiting both canonical and non-canonical degradation pathways
    • Carayol N, Wang CY (2006) IKKalpha stabilizes cytosolic beta-catenin by inhibiting both canonical and non-canonical degradation pathways. Cell Signal 18: 1941-1946
    • (2006) Cell Signal , vol.18 , pp. 1941-1946
    • Carayol, N.1    Wang, C.Y.2
  • 125
    • 0032588186 scopus 로고    scopus 로고
    • Nf-kappab controls cell growth and differentiation through transcriptional regulation of cyclin d1
    • Guttridge DC, Albanese C, Reuther JY, Pestell RG, Baldwin AS Jr (1999) NF-kappaB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol Cell Biol 19: 5785-5799
    • (1999) Mol Cell Biol , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1    Albanese, C.2    Reuther, J.Y.3    Pestell, R.G.4    Baldwin Jr., A.S.5
  • 126
    • 0032588170 scopus 로고    scopus 로고
    • Nf-kappab function in growth control: Regulation of cyclin d1 expression and g0/g1-to-s-phase transition
    • Hinz M, Krappmann D, Eichten A, Heder A, Scheidereit C, Strauss M (1999) NF-kappaB function in growth control: regulation of cyclin D1 expression and G0/G1-to-S-phase transition. Mol Cell Biol 19: 2690-2698
    • (1999) Mol Cell Biol , vol.19 , pp. 2690-2698
    • Hinz, M.1    Krappmann, D.2    Eichten, A.3    Heder, A.4    Scheidereit, C.5    Strauss, M.6
  • 127
    • 26644457201 scopus 로고    scopus 로고
    • Ikappab kinase alpha regulates subcellular distribution and turnover of cyclin d1 by phosphorylation
    • Kwak YT, Li R, Becerra CR, Tripathy D, Frenkel EP, Verma UN (2005) IkappaB kinase alpha regulates subcellular distribution and turnover of cyclin D1 by phosphorylation. J Biol Chem 280: 33945-33952
    • (2005) J Biol Chem , vol.280 , pp. 33945-33952
    • Kwak, Y.T.1    Li, R.2    Becerra, C.R.3    Tripathy, D.4    Frenkel, E.P.5    Verma, U.N.6
  • 128
    • 84872587266 scopus 로고    scopus 로고
    • Inactivation of bad by ikk inhibits tnfalpha-induced apoptosis independently of nf-kappab activation
    • Yan J, Xiang J, Lin Y, Ma J, Zhang J, Zhang H, Sun J, Danial NN, Liu J, Lin A (2013) Inactivation of BAD by IKK inhibits TNFalpha-induced apoptosis independently of NF-kappaB activation. Cell 152: 304-315
    • (2013) Cell , vol.152 , pp. 304-315
    • Yan, J.1    Xiang, J.2    Lin, Y.3    Ma, J.4    Zhang, J.5    Zhang, H.6    Sun, J.7    Danial, N.N.8    Liu, J.9    Lin, A.10
  • 130
    • 79953773106 scopus 로고    scopus 로고
    • Ikk-dependent, nf-kappab-independent control of autophagic gene expression
    • Comb WC, Cogswell P, Sitcheran R, Baldwin AS (2011) IKK-dependent, NF-kappaB-independent control of autophagic gene expression. Oncogene 30: 1727-1732
    • (2011) Oncogene , vol.30 , pp. 1727-1732
    • Comb, W.C.1    Cogswell, P.2    Sitcheran, R.3    Baldwin, A.S.4
  • 132
    • 84859023600 scopus 로고    scopus 로고
    • P85alpha sh2 domain phosphorylation by ikk promotes feedback inhibition of pi3k and akt in response to cellular starvation
    • Comb WC, Hutti JE, Cogswell P, Cantley LC, Baldwin AS (2012) p85alpha SH2 domain phosphorylation by IKK promotes feedback inhibition of PI3K and Akt in response to cellular starvation. Mol Cell 45: 719-730
    • (2012) Mol Cell , vol.45 , pp. 719-730
    • Comb, W.C.1    Hutti, J.E.2    Cogswell, P.3    Cantley, L.C.4    Baldwin, A.S.5
  • 133
    • 34447131534 scopus 로고    scopus 로고
    • Regulation of mammalian target of rapamycin activity in pten-inactive prostate cancer cells by i kappa b kinase alpha
    • Dan HC, Adli M, Baldwin AS (2007) Regulation of mammalian target of rapamycin activity in PTEN-inactive prostate cancer cells by I kappa B kinase alpha. Cancer Res 67: 6263-6269
    • (2007) Cancer Res , vol.67 , pp. 6263-6269
    • Dan, H.C.1    Adli, M.2    Baldwin, A.S.3
  • 135
    • 35648970074 scopus 로고    scopus 로고
    • Ikappab kinase alpha kinase activity is required for self-renewal of erbb2/her2-transformed mammary tumorinitiating cells
    • Cao Y, Luo JL, Karin M (2007) IkappaB kinase alpha kinase activity is required for self-renewal of ErbB2/Her2-transformed mammary tumorinitiating cells. Proc Natl Acad Sci U S A 104: 15852-15857
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15852-15857
    • Cao, Y.1    Luo, J.L.2    Karin, M.3
  • 138
    • 6344241039 scopus 로고    scopus 로고
    • Smrt derepression by the ikappab kinase alpha: A prerequisite to nf-kappab transcription and survival
    • Hoberg JE, Yeung F, Mayo MW (2004) SMRT derepression by the IkappaB kinase alpha: a prerequisite to NF-kappaB 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
  • 139
    • 30744458869 scopus 로고    scopus 로고
    • Ikappab kinase alpha-mediated derepression of smrt potentiates acetylation of rela/p65 by p300
    • Hoberg JE, Popko AE, Ramsey CS, Mayo MW (2006) IkappaB kinase alpha-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300. Mol Cell Biol 26: 457-471
    • (2006) Mol Cell Biol , vol.26 , pp. 457-471
    • Hoberg, J.E.1    Popko, A.E.2    Ramsey, C.S.3    Mayo, M.W.4
  • 142
    • 34047248402 scopus 로고    scopus 로고
    • Phosphorylation of cbp by ikkalpha promotes cell growth by switching the binding preference of cbp from p53 to nf-kappab
    • Huang WC, Ju TK, Hung MC, Chen CC (2007) Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB. Mol Cell 26: 75-87
    • (2007) Mol Cell , vol.26 , pp. 75-87
    • Huang, W.C.1    Ju, T.K.2    Hung, M.C.3    Chen, C.C.4
  • 143
    • 43049139541 scopus 로고    scopus 로고
    • P53 regulates glucose metabolism through an ikk-nf-kappab pathway and inhibits cell transformation
    • Kawauchi K, Araki K, Tobiume K, Tanaka N (2008) p53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation. Nat Cell Biol 10: 611-618
    • (2008) Nat Cell Biol , vol.10 , pp. 611-618
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 144
    • 62549161375 scopus 로고    scopus 로고
    • Loss of p53 enhances catalytic activity of ikkbeta through o-linked beta-n-acetyl glucosamine modification
    • Kawauchi K, Araki K, Tobiume K, Tanaka N (2009) Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification. Proc Natl Acad Sci U S A 106: 3431-3436
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3431-3436
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 154
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, Robert J, Rush J, Hochstrasser M, Finley D, Peng J (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137: 133-145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7
  • 155
    • 15944379896 scopus 로고    scopus 로고
    • Formation of an ikkalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation
    • Park KJ, Krishnan V, O'Malley BW, Yamamoto Y, Gaynor RB (2005) Formation of an IKKalpha-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
  • 156
    • 70349987565 scopus 로고    scopus 로고
    • Ikkalpha negatively regulates irf-5 function in a myd88-traf6 pathway
    • Balkhi MY, Fitzgerald KA, Pitha PM (2010) IKKalpha negatively regulates IRF-5 function in a MyD88-TRAF6 pathway. Cell Signal 22: 117-127
    • (2010) Cell Signal , vol.22 , pp. 117-127
    • Balkhi, M.Y.1    Fitzgerald, K.A.2    Pitha, P.M.3
  • 159
    • 3843135237 scopus 로고    scopus 로고
    • Ikappab kinase alpha and p65/rela contribute to optimal epidermal growth factor-induced c-fos gene expression independent of ikappabalpha degradation
    • Anest V, Cogswell PC, Baldwin AS Jr (2004) IkappaB kinase alpha and p65/RelA contribute to optimal epidermal growth factor-induced c-fos gene expression independent of IkappaBalpha degradation. J Biol Chem 279: 31183-31189
    • (2004) J Biol Chem , vol.279 , pp. 31183-31189
    • Anest, V.1    Cogswell, P.C.2    Baldwin Jr., A.S.3
  • 161
    • 0038511129 scopus 로고    scopus 로고
    • Histone h3 phosphorylation by ikk-alpha is critical for cytokine-induced gene expression
    • Yamamoto Y, Verma UN, Prajapati S, Kwak YT, Gaynor RB (2003) Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature 423: 655-659
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 163
    • 6344264987 scopus 로고    scopus 로고
    • Lipopolysaccharide activation of the tpl-2/mek/extracellular signal-regulated kinase mitogen-activated protein kinase cascade is regulated by ikappab kinase-induced proteolysis of nf-kappab1 p105
    • Beinke S, Robinson MJ, Hugunin M, Ley SC (2004) Lipopolysaccharide activation of the TPL-2/MEK/extracellular signal-regulated kinase mitogen-activated protein kinase cascade is regulated by IkappaB kinase-induced proteolysis of NF-kappaB1 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
  • 164
    • 2942707765 scopus 로고    scopus 로고
    • Ikappab kinase is an essential component of the tpl2 signaling pathway
    • Waterfield M, Jin W, Reiley W, Zhang M, Sun SC (2004) IkappaB kinase is an essential component of the Tpl2 signaling pathway. Mol Cell Biol 24: 6040-6048
    • (2004) Mol Cell Biol , vol.24 , pp. 6040-6048
    • Waterfield, M.1    Jin, W.2    Reiley, W.3    Zhang, M.4    Sun, S.C.5
  • 165
    • 22544461297 scopus 로고    scopus 로고
    • Convergent actions of i kappa b kinase beta and protein kinase c delta modulate mrna stability through phosphorylation of 14-3-3 beta complexed with tristetraprolin
    • Gringhuis SI, Garcia-Vallejo JJ, van Het Hof B, van Dijk W (2005) Convergent actions of I kappa B kinase beta and protein kinase C delta modulate mRNA stability through phosphorylation of 14-3-3 beta 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
  • 167
    • 37549011707 scopus 로고    scopus 로고
    • Ikappab kinase beta-induced phosphorylation of carma1 contributes to carma1 bcl10 malt1 complex formation in b cells
    • Shinohara H, Maeda S, Watarai H, Kurosaki T (2007) IkappaB kinase beta-induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. J Exp Med 204: 3285-3293
    • (2007) J Exp Med , vol.204 , pp. 3285-3293
    • Shinohara, H.1    Maeda, S.2    Watarai, H.3    Kurosaki, T.4
  • 168
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme cyld by ikappab kinase gamma-dependent phosphorylation
    • Reiley W, Zhang M, Wu X, Granger E, Sun SC (2005) Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation. Mol Cell Biol 25: 3886-3895
    • (2005) Mol Cell Biol , vol.25 , pp. 3886-3895
    • Reiley, W.1    Zhang, M.2    Wu, X.3    Granger, E.4    Sun, S.C.5
  • 170
    • 0037073679 scopus 로고    scopus 로고
    • Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa b kinase complex
    • Gao Z, Hwang D, Bataille F, Lefevre M, York D, Quon MJ, Ye J (2002) Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex. J Biol Chem 277: 48115-48121
    • (2002) J Biol Chem , vol.277 , pp. 48115-48121
    • Gao, Z.1    Hwang, D.2    Bataille, F.3    Lefevre, M.4    York, D.5    Quon, M.J.6    Ye, J.7
  • 171
    • 48449094278 scopus 로고    scopus 로고
    • Phosphorylation of snap-23 by ikappab kinase 2 regulates mast cell degranulation
    • Suzuki K, Verma IM (2008) Phosphorylation of SNAP-23 by IkappaB kinase 2 regulates mast cell degranulation. Cell 134: 485-495
    • (2008) Cell , vol.134 , pp. 485-495
    • Suzuki, K.1    Verma, I.M.2


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