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Volumn 425, Issue 11, 2013, Pages 1934-1945

A structural basis for selective dimerization by NF-κB RelB

Author keywords

dimer interface; gene expression; NF B; transcription factor; x ray crystallography

Indexed keywords

I KAPPA B; TRANSCRIPTION FACTOR;

EID: 84877713439     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.02.020     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • M.S. Hayden, and S. Ghosh Shared principles in NF-kappaB signaling Cell 132 2008 344 362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 33750448661 scopus 로고    scopus 로고
    • Transcriptional regulation via the NF-kappaB signaling module
    • A. Hoffmann, G. Natoli, and G. Ghosh Transcriptional regulation via the NF-kappaB signaling module Oncogene 25 2006 6706 6716
    • (2006) Oncogene , vol.25 , pp. 6706-6716
    • Hoffmann, A.1    Natoli, G.2    Ghosh, G.3
  • 3
    • 84858720808 scopus 로고    scopus 로고
    • Dimer-specific regulatory mechanisms within the NF-kappaB family of transcription factors
    • S.T. Smale Dimer-specific regulatory mechanisms within the NF-kappaB family of transcription factors Immunol. Rev. 246 2012 193 204
    • (2012) Immunol. Rev. , vol.246 , pp. 193-204
    • Smale, S.T.1
  • 4
    • 84858724192 scopus 로고    scopus 로고
    • NF-kappaB regulation: Lessons from structures
    • G. Ghosh, V.Y. Wang, D.B. Huang, and A. Fusco NF-kappaB regulation: lessons from structures Immunol. Rev. 246 2012 36 58
    • (2012) Immunol. Rev. , vol.246 , pp. 36-58
    • Ghosh, G.1    Wang, V.Y.2    Huang, D.B.3    Fusco, A.4
  • 5
    • 0031573470 scopus 로고    scopus 로고
    • The role of DNA in the mechanism of NFkappaB dimer formation: Crystal structures of the dimerization domains of the p50 and p65 subunits
    • D.B. Huang, T. Huxford, Y.Q. Chen, and G. Ghosh The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits Structure 5 1997 1427 1436
    • (1997) Structure , vol.5 , pp. 1427-1436
    • Huang, D.B.1    Huxford, T.2    Chen, Y.Q.3    Ghosh, G.4
  • 6
    • 0035854279 scopus 로고    scopus 로고
    • Analysis of the NF-kappaB p50 dimer interface by diversity screening
    • D.J. Hart, R.E. Speight, J.D. Sutherland, and J.M. Blackburn Analysis of the NF-kappaB p50 dimer interface by diversity screening J. Mol. Biol. 310 2001 563 575
    • (2001) J. Mol. Biol. , vol.310 , pp. 563-575
    • Hart, D.J.1    Speight, R.E.2    Sutherland, J.D.3    Blackburn, J.M.4
  • 8
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • S. Ghosh, and M. Karin Missing pieces in the NF-kappaB puzzle Cell 109 2002 S81 S96
    • (2002) Cell , vol.109
    • Ghosh, S.1    Karin, M.2
  • 9
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway
    • U. Senftleben, Y. Cao, G. Xiao, F.R. Greten, G. Krahn, and G. Bonizzi Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway Science 293 2001 1495 1499
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1    Cao, Y.2    Xiao, G.3    Greten, F.R.4    Krahn, G.5    Bonizzi, G.6
  • 10
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • G. Bonizzi, and M. Karin The two NF-kappaB activation pathways and their role in innate and adaptive immunity Trends Immunol. 25 2004 280 288
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 11
    • 0035881959 scopus 로고    scopus 로고
    • Essential role of RelB in germinal center and marginal zone formation and proper expression of homing chemokines
    • D.S. Weih, Z.B. Yilmaz, and F. Weih Essential role of RelB in germinal center and marginal zone formation and proper expression of homing chemokines J. Immunol. 167 2001 1909 1919
    • (2001) J. Immunol. , vol.167 , pp. 1909-1919
    • Weih, D.S.1    Yilmaz, Z.B.2    Weih, F.3
  • 12
    • 0037413709 scopus 로고    scopus 로고
    • RelB is required for Peyer's patch development: Differential regulation of p52-RelB by lymphotoxin and TNF
    • Z.B. Yilmaz, D.S. Weih, V. Sivakumar, and F. Weih RelB is required for Peyer's patch development: differential regulation of p52-RelB by lymphotoxin and TNF EMBO J. 22 2003 121 130
    • (2003) EMBO J. , vol.22 , pp. 121-130
    • Yilmaz, Z.B.1    Weih, D.S.2    Sivakumar, V.3    Weih, F.4
  • 13
    • 84869411578 scopus 로고    scopus 로고
    • Control of RelB during dendritic cell activation integrates canonical and noncanonical NF-kappaB pathways
    • V.F. Shih, J. Davis-Turak, M. Macal, J.Q. Huang, J. Ponomarenko, and J.D. Kearns Control of RelB during dendritic cell activation integrates canonical and noncanonical NF-kappaB pathways Nat. Immunol. 13 2012 1162 1170
    • (2012) Nat. Immunol. , vol.13 , pp. 1162-1170
    • Shih, V.F.1    Davis-Turak, J.2    Macal, M.3    Huang, J.Q.4    Ponomarenko, J.5    Kearns, J.D.6
  • 14
    • 0038771214 scopus 로고    scopus 로고
    • Modulation of NF-kappaB activity by exchange of dimers
    • S. Saccani, S. Pantano, and G. Natoli Modulation of NF-kappaB activity by exchange of dimers Mol. Cell 11 2003 1563 1574
    • (2003) Mol. Cell , vol.11 , pp. 1563-1574
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 16
    • 24344436818 scopus 로고    scopus 로고
    • NF-kappaB RelB forms an intertwined homodimer
    • D.B. Huang, D. Vu, and G. Ghosh NF-kappaB RelB forms an intertwined homodimer Structure 13 2005 1365 1373
    • (2005) Structure , vol.13 , pp. 1365-1373
    • Huang, D.B.1    Vu, D.2    Ghosh, G.3
  • 17
    • 34748858470 scopus 로고    scopus 로고
    • X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites
    • A.K. Moorthy, D.B. Huang, V.Y. Wang, D. Vu, and G. Ghosh X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites J. Mol. Biol. 373 2007 723 734
    • (2007) J. Mol. Biol. , vol.373 , pp. 723-734
    • Moorthy, A.K.1    Huang, D.B.2    Wang, V.Y.3    Vu, D.4    Ghosh, G.5
  • 18
    • 59649121227 scopus 로고    scopus 로고
    • NF-kappaB p52:RelB heterodimer recognizes two classes of kappaB sites with two distinct modes
    • A.J. Fusco, D.B. Huang, D. Miller, V.Y. Wang, D. Vu, and G. Ghosh NF-kappaB p52:RelB heterodimer recognizes two classes of kappaB sites with two distinct modes EMBO Rep. 10 2009 152 159
    • (2009) EMBO Rep. , vol.10 , pp. 152-159
    • Fusco, A.J.1    Huang, D.B.2    Miller, D.3    Wang, V.Y.4    Vu, D.5    Ghosh, G.6
  • 20
    • 4143141894 scopus 로고    scopus 로고
    • Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding
    • D.Y. Chirgadze, M. Demydchuk, M. Becker, S. Moran, and M. Paoli Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding Structure 12 2004 1489 1494
    • (2004) Structure , vol.12 , pp. 1489-1494
    • Chirgadze, D.Y.1    Demydchuk, M.2    Becker, M.3    Moran, S.4    Paoli, M.5
  • 21
    • 0027333345 scopus 로고
    • A novel NF-kappa B complex containing p65 homodimers: Implications for transcriptional control at the level of subunit dimerization
    • P.A. Ganchi, S.C. Sun, W.C. Greene, and D.W. Ballard A novel NF-kappa B complex containing p65 homodimers: implications for transcriptional control at the level of subunit dimerization Mol. Cell. Biol. 13 1993 7826 7835
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7826-7835
    • Ganchi, P.A.1    Sun, S.C.2    Greene, W.C.3    Ballard, D.W.4
  • 22
    • 0036235547 scopus 로고    scopus 로고
    • Mutational analysis of the v-Rel dimerization interface reveals a critical role for v-Rel homodimers in transformation
    • A.S. Liss, and H.R. Bose Jr Mutational analysis of the v-Rel dimerization interface reveals a critical role for v-Rel homodimers in transformation J. Virol. 76 2002 4928 4939
    • (2002) J. Virol. , vol.76 , pp. 4928-4939
    • Liss, A.S.1    Bose, Jr.H.R.2
  • 24
    • 42149185026 scopus 로고    scopus 로고
    • Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation
    • L.A. Puto, and J.C. Reed Daxx represses RelB target promoters via DNA methyltransferase recruitment and DNA hypermethylation Genes Dev. 22 2008 998 1010
    • (2008) Genes Dev. , vol.22 , pp. 998-1010
    • Puto, L.A.1    Reed, J.C.2
  • 29
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.