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Volumn 416, Issue 1, 2008, Pages 117-127

Identification of lysine residues critical for the transcriptional activity and polyubiquitination of the NF-κB family member RelB

Author keywords

Co factor; Gene expression; Nuclear factor B (NF B); Protein stability; RelB; Ubiquitination

Indexed keywords

293 CELLS; B CELLS; CELL LINES; CO-FACTOR; DEATH DOMAIN; DNA BINDING; DNA METHYLTRANSFERASE; DUAL ROLE; HUMAN EMBRYONIC KIDNEYS; IONOMYCIN; KEY COMPONENT; LYSINE RESIDUES; MOLECULAR MECHANISM; NUCLEAR FACTORS; NUCLEAR LOCALIZATION; POLYUBIQUITINATION; PROTEASOMAL DEGRADATION; PROTEIN STABILITY; RELB; SIGNALLING PATHWAYS; TARGET GENES; TARGET SITES; TRANSCRIPTIONAL ACTIVITY; UBIQUITIN; UBIQUITINATION;

EID: 56049119389     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080432     Document Type: Article
Times cited : (13)

References (24)
  • 1
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden, M. S. 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
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh, S. and Karin, M. (2002) Missing pieces in the NF-κB puzzle. Cell 109, S81-S96
    • (2002) Cell , vol.109
    • Ghosh, S.1    Karin, M.2
  • 4
    • 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
  • 5
    • 33749459830 scopus 로고    scopus 로고
    • Daxx represses expression of a subset of anti-apoptotic genes regulated by nuclear factor-κB
    • Croxton, R., Puto, L. A., de Belle, I., Thomas, M., Torii, S., Hanaii, F., Cuddy, M. and Reed, J. C. (2006) Daxx represses expression of a subset of anti-apoptotic genes regulated by nuclear factor-κB. Cancer Res. 66, 9026-9035
    • (2006) Cancer Res , vol.66 , pp. 9026-9035
    • Croxton, R.1    Puto, L.A.2    de Belle, I.3    Thomas, M.4    Torii, S.5    Hanaii, F.6    Cuddy, M.7    Reed, J.C.8
  • 6
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB
    • Chen, L. F., Mu, Y. and Greene, W. C. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB. EMBO J. 21, 6539-6548
    • (2002) EMBO J , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 7
    • 0036203419 scopus 로고    scopus 로고
    • The phosphorylation status of nuclear NF-κB determines its association with CBP/p300 or HDAC-1
    • Zhong, H., May, M. J., Jimi, E. and Ghosh, S. (2002) The phosphorylation status of nuclear NF-κB determines its association with CBP/p300 or HDAC-1. Mol. Cell 9, 625-636
    • (2002) Mol. Cell , vol.9 , pp. 625-636
    • Zhong, H.1    May, M.J.2    Jimi, E.3    Ghosh, S.4
  • 8
    • 0042525909 scopus 로고    scopus 로고
    • Essential role of RelA Ser311 phosphorylation by ζ PKC in NF-κB transcriptional activation
    • Duran, A., Diaz-Meco, M. T. and Moscat, J. (2003) Essential role of RelA Ser311 phosphorylation by ζ PKC in NF-κB transcriptional activation. EMBO J. 22, 3910-3918
    • (2003) EMBO J , vol.22 , pp. 3910-3918
    • Duran, A.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 9
    • 27544473311 scopus 로고    scopus 로고
    • The ubiquitin ligase HectH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation
    • Adhikary, S., Marinoni, F., Hock, A., Hulleman, E., Popov, N., Beier, R., Bernard, S., Quarto, M., Capra, M., Goettig, S. et al. (2005) The ubiquitin ligase HectH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation. Cell 123, 409-421
    • (2005) Cell , vol.123 , pp. 409-421
    • Adhikary, S.1    Marinoni, F.2    Hock, A.3    Hulleman, E.4    Popov, N.5    Beier, R.6    Bernard, S.7    Quarto, M.8    Capra, M.9    Goettig, S.10
  • 10
    • 0035819033 scopus 로고    scopus 로고
    • Signal-specific and phosphorylation-dependent RelB degradation: A potential mechanism of NF-κB control
    • Marienfeld, R., Berberich-Siebelt, F., Berberich, I., Denk, A., Serfling, E. and Neumann, M. (2001) Signal-specific and phosphorylation-dependent RelB degradation: a potential mechanism of NF-κB control. Oncogene 20, 8142-8147
    • (2001) Oncogene , vol.20 , pp. 8142-8147
    • Marienfeld, R.1    Berberich-Siebelt, F.2    Berberich, I.3    Denk, A.4    Serfling, E.5    Neumann, M.6
  • 12
    • 0141865759 scopus 로고    scopus 로고
    • Critical role of RelB serine 368 for dimerization and p100 stabilization
    • Maier, H. J., Marienfeld, R., Wirth, T. and Baumann, B. (2003) Critical role of RelB serine 368 for dimerization and p100 stabilization. J. Biol. Chem. 278, 39242-39250
    • (2003) J. Biol. Chem , vol.278 , pp. 39242-39250
    • Maier, H.J.1    Marienfeld, R.2    Wirth, T.3    Baumann, B.4
  • 14
    • 38049028109 scopus 로고    scopus 로고
    • The phosphorylation of serine 68 in the IKK-binding domain of NEMO interferes with the structure of the IKK-complex and the TNF-α -induced NF-κB activity
    • Palkowitsch, L., Leidner, J., Ghosh, S. and Marienfeld, R. B. (2008) The phosphorylation of serine 68 in the IKK-binding domain of NEMO interferes with the structure of the IKK-complex and the TNF-α -induced NF-κB 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
  • 15
    • 0032496144 scopus 로고    scopus 로고
    • The mutant plasmacytoma cell line S107 allows the identification of distinct pathways leading to NF-κB activation
    • Baumann, B., Kistler, B., Kirillov, A., Bergman, Y. and Wirth, T. (1998) The mutant plasmacytoma cell line S107 allows the identification of distinct pathways leading to NF-κB activation. J. Biol. Chem. 273, 11448-11455
    • (1998) J. Biol. Chem , vol.273 , pp. 11448-11455
    • Baumann, B.1    Kistler, B.2    Kirillov, A.3    Bergman, Y.4    Wirth, T.5
  • 16
    • 0028152894 scopus 로고
    • Constitutive and inducible Rel/NF-κB activities in mouse thymus and spleen
    • Weih, F., Carrasco, D. and Bravo, R. (1994) Constitutive and inducible Rel/NF-κB activities in mouse thymus and spleen. Oncogene 9, 3289-3297
    • (1994) Oncogene , vol.9 , pp. 3289-3297
    • Weih, F.1    Carrasco, D.2    Bravo, R.3
  • 17
    • 0028146086 scopus 로고
    • Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells
    • Lernbecher, T., Kistler, B. and Wirth, T. (1994) Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells. EMBO J. 13, 4060-4069
    • (1994) EMBO J , vol.13 , pp. 4060-4069
    • Lernbecher, T.1    Kistler, B.2    Wirth, T.3
  • 18
    • 0027521432 scopus 로고
    • Distinct NF-κB/Rel transcription factors are responsible for tissue-specific and inducible gene activation
    • Lernbecher, T., Muller, U. and Wirth, T. (1993) Distinct NF-κB/Rel transcription factors are responsible for tissue-specific and inducible gene activation. Nature 365, 767-770
    • (1993) Nature , vol.365 , pp. 767-770
    • Lernbecher, T.1    Muller, U.2    Wirth, T.3
  • 19
    • 17844386319 scopus 로고    scopus 로고
    • IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation
    • Lawrence, T., Bebien, M., Liu, G. Y., 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
  • 20
    • 34547815755 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor signaling by NF-eB p50 ubiquitination blockade
    • Carmody, R. J., Ruan, Q., Palmer, S., Hilliard, B. and Chen, Y. H. (2007) Negative regulation of toll-like receptor signaling by NF-eB p50 ubiquitination blockade. Science 317, 675-678
    • (2007) Science , vol.317 , pp. 675-678
    • Carmody, R.J.1    Ruan, Q.2    Palmer, S.3    Hilliard, B.4    Chen, Y.H.5
  • 21
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund, K. and Dikic, I. (2005) Ubiquitylation and cell signaling. EMBO J 24, 3353-3359
    • (2005) EMBO J , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 22
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals
    • Ikeda, F. and Dikic, I. (2008) Atypical ubiquitin chains: new molecular signals. EMBO Rep. 9, 536-542
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 23
    • 0141621240 scopus 로고    scopus 로고
    • A role for NF-κB essential modifier/IκB kinaseγ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α
    • Tang, E. D., Wang, C. Y., Xiong, Y. and Guan, K. L. (2003) A role for NF-κB essential modifier/IκB kinaseγ (NEMO/IKKγ) ubiquitination in the activation of the IκB kinase complex by tumor necrosis factor-α. 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
  • 24
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase
    • Maine, G. N., Mao, X., Komarck, C. M. and Burstein, E. (2007) COMMD1 promotes the ubiquitination of NF-κB subunits through a cullin-containing ubiquitin ligase. EMBO J. 26, 436-447
    • (2007) EMBO J , vol.26 , pp. 436-447
    • Maine, G.N.1    Mao, X.2    Komarck, C.M.3    Burstein, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.