메뉴 건너뛰기




Volumn 12, Issue 12, 2011, Pages 1167-1175

The IκB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 6; MESSENGER RNA; REGNASE 1; RIBONUCLEASE; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG;

EID: 81255154489     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.2137     Document Type: Article
Times cited : (235)

References (40)
  • 1
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805-820 (2010).
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 2
    • 58049193003 scopus 로고    scopus 로고
    • Microbe sensing, positive feedback loops, and the pathogenesis of inflammatory diseases
    • Beutler, B. Microbe sensing, positive feedback loops, and the pathogenesis of inflammatory diseases. Immunol. Rev. 227, 248-263 (2009).
    • (2009) Immunol. Rev. , vol.227 , pp. 248-263
    • Beutler, B.1
  • 3
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • Medzhitov, R. & Horng, T. Transcriptional control of the inflammatory response. Nat. Rev. Immunol. 9, 692-703 (2009).
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2
  • 4
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • DOI 10.1016/j.cell.2006.02.015, PII S0092867406001905
    • Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell 124, 783-801 (2006). (Pubitemid 43261452)
    • (2006) Cell , vol.124 , Issue.4 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 6
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin in NF-κB regulatory pathways
    • Skaug, B., Jiang, X. & Chen, Z.J. The role of ubiquitin in NF-κB regulatory pathways. Annu. Rev. Biochem. 78, 769-796 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 7
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia, Z.P. et al. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 461, 114-119 (2009).
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1
  • 8
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591-596 (2011).
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 9
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
    • Ikeda, F. et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis. Nature 471, 637-641 (2011).
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 10
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
    • Tokunaga, F. et al. SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex. Nature 471, 633-636 (2011).
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1
  • 11
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • DOI 10.1146/annurev.immunol.18.1.621
    • Karin, M. & Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663 (2000). (Pubitemid 30365393)
    • (2000) Annual Review of Immunology , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 12
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden, M.S. & Ghosh, S. Shared principles in NF-κB signaling. Cell 132, 344-362 (2008).
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 13
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: Tipping the scales of cancer
    • DOI 10.1038/nrc2396, PII NRC2396
    • Frescas, D. & Pagano, M. Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer. Nat. Rev. Cancer 8, 438-449 (2008). (Pubitemid 351744963)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.6 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 14
    • 80051959463 scopus 로고    scopus 로고
    • NF-kappaB is 25
    • Baltimore, D. NF-kappaB is 25. Nat. Immunol. 12, 683-685 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 683-685
    • Baltimore, D.1
  • 15
    • 80051987703 scopus 로고    scopus 로고
    • Crosstalk in NF-κB signaling pathways
    • Oeckinghaus, A., Hayden, M.S. & Ghosh, S. Crosstalk in NF-κB signaling pathways. Nat. Immunol. 12, 695-708 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 695-708
    • Oeckinghaus, A.1    Hayden, M.S.2    Ghosh, S.3
  • 16
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea, C.K., Deng, L., Xia, Z.P., Pineda, G. & Chen, Z.J. Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245-257 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 17
    • 61849157254 scopus 로고    scopus 로고
    • TNFR signaling: Ubiquitin-conjugated TRAFfic signals control stop-and-go for MAPK signaling complexes
    • Karin, M. & Gallagher, E. TNFR signaling: ubiquitin-conjugated TRAFfic signals control stop-and-go for MAPK signaling complexes. Immunol. Rev. 228, 225-240 (2009).
    • (2009) Immunol. Rev. , vol.228 , pp. 225-240
    • Karin, M.1    Gallagher, E.2
  • 18
    • 40949102111 scopus 로고    scopus 로고
    • Post-transcriptional control of cytokine production
    • DOI 10.1038/ni1584, PII NI1584
    • Anderson, P. Post-transcriptional control of cytokine production. Nat. Immunol. 9, 353-359 (2008). (Pubitemid 351405104)
    • (2008) Nature Immunology , vol.9 , Issue.4 , pp. 353-359
    • Anderson, P.1
  • 19
    • 60749124122 scopus 로고    scopus 로고
    • The stability of mRNA influences the temporal order of the induction of genes encoding inflammatory molecules
    • Hao, S. & Baltimore, D. The stability of mRNA influences the temporal order of the induction of genes encoding inflammatory molecules. Nat. Immunol. 10, 281-288 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 281-288
    • Hao, S.1    Baltimore, D.2
  • 20
    • 72949123583 scopus 로고    scopus 로고
    • Post-transcriptional regulons coordinate the initiation and resolution of inflammation
    • Anderson, P. Post-transcriptional regulons coordinate the initiation and resolution of inflammation. Nat. Rev. Immunol. 10, 24-35 (2010).
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 24-35
    • Anderson, P.1
  • 21
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin
    • Carballo, E., Lai, W.S. & Blackshear, P.J. Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin. Science 281, 1001-1005 (1998). (Pubitemid 28399252)
    • (1998) Science , vol.281 , Issue.5379 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 22
    • 67349167059 scopus 로고    scopus 로고
    • Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay
    • Matsushita, K. et al. Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay. Nature 458, 1185-1190 (2009).
    • (2009) Nature , vol.458 , pp. 1185-1190
    • Matsushita, K.1
  • 25
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β- TrCP
    • Spencer, E., Jiang, J. & Chen, Z.J. Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP. Genes Dev. 13, 284-294 (1999). (Pubitemid 29095800)
    • (1999) Genes and Development , vol.13 , Issue.3 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 26
    • 47049093796 scopus 로고    scopus 로고
    • Interleukin 1α-induced NFκB activation and chemokine mRNA stabilization diverge at IRAK1
    • Hartupee, J., Li, X. & Hamilton, T. Interleukin 1α-induced NFκB activation and chemokine mRNA stabilization diverge at IRAK1. J. Biol. Chem. 283, 15689-15693 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 15689-15693
    • Hartupee, J.1    Li, X.2    Hamilton, T.3
  • 27
    • 67449092565 scopus 로고    scopus 로고
    • Interleukin-1 receptor-associated kinase 2 is critical for lipopolysaccharide-mediated post-transcriptional control
    • Wan, Y. et al. Interleukin-1 receptor-associated kinase 2 is critical for lipopolysaccharide-mediated post-transcriptional control. J. Biol. Chem. 284, 10367-10375 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 10367-10375
    • Wan, Y.1
  • 28
    • 77649138874 scopus 로고    scopus 로고
    • Transcription factors Elk-1 and SRF are engaged in IL1-dependent regulation of ZC3H12A expression
    • Kasza, A. et al. Transcription factors Elk-1 and SRF are engaged in IL1-dependent regulation of ZC3H12A expression. BMC Mol. Biol. 11, 14 (2010).
    • (2010) BMC Mol. Biol. , vol.11 , pp. 14
    • Kasza, A.1
  • 29
    • 33750979012 scopus 로고    scopus 로고
    • Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1
    • DOI 10.1128/MCB.01155-06
    • Paschoud, S. et al. Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1. Mol. Cell. Biol. 26, 8228-8241 (2006). (Pubitemid 44748560)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8228-8241
    • Paschoud, S.1    Dogar, A.M.2    Kuntz, C.3    Grisoni-Neupert, B.4    Richman, L.5    Kuhn, L.C.6
  • 31
    • 48449094278 scopus 로고    scopus 로고
    • Phosphorylation of SNAP-23 by IκB kinase 2 regulates mast cell degranulation
    • Suzuki, K. & Verma, I.M. Phosphorylation of SNAP-23 by IκB kinase 2 regulates mast cell degranulation. Cell 134, 485-495 (2008).
    • (2008) Cell , vol.134 , pp. 485-495
    • Suzuki, K.1    Verma, I.M.2
  • 32
    • 62449257012 scopus 로고    scopus 로고
    • Phosphorylation of p53 by IκB kinase 2 promotes its degradation by β-TrCP
    • Xia, Y. et al. Phosphorylation of p53 by IκB kinase 2 promotes its degradation by β-TrCP. Proc. Natl. Acad. Sci. USA 106, 2629-2634 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2629-2634
    • Xia, Y.1
  • 33
    • 33645841633 scopus 로고    scopus 로고
    • IκB kinase-α is critical for interferon-α production induced by Toll-like receptors 7 and 9
    • Hoshino, K. et al. IκB kinase-α is critical for interferon-α production induced by Toll-like receptors 7 and 9. Nature 440, 949-953 (2006).
    • (2006) Nature , vol.440 , pp. 949-953
    • Hoshino, K.1
  • 34
    • 78650371990 scopus 로고    scopus 로고
    • MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling
    • Liang, J. et al. MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-κB signaling. J. Exp. Med. 207, 2959-2973 (2010).
    • (2010) J. Exp. Med. , vol.207 , pp. 2959-2973
    • Liang, J.1
  • 35
    • 33845368513 scopus 로고    scopus 로고
    • COPASI-A complex pathway simulator
    • Hoops, S. et al. COPASI-a COmplex PAthway SImulator. Bioinformatics 22, 3067-3074 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 3067-3074
    • Hoops, S.1
  • 36
    • 0034661272 scopus 로고    scopus 로고
    • Complete lack of NF-κB activity in IKK1 and IKK2 double-deficient mice: Additional defect in neurulation
    • Li, Q., Estepa, G., Memet, S., Israel, A. & Verma, I.M. Complete lack of NF-κB activity in IKK1 and IKK2 double-deficient mice: additional defect in neurulation. Genes Dev. 14, 1729-1733 (2000). (Pubitemid 30602991)
    • (2000) Genes and Development , vol.14 , Issue.14 , pp. 1729-1733
    • Li, Q.1    Estepa, G.2    Memet, S.3    Israel, A.4    Verma, I.M.5
  • 40
    • 78650214109 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA
    • Tsuchida, T. et al. The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity 33, 765-776 (2010).
    • (2010) Immunity , vol.33 , pp. 765-776
    • Tsuchida, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.