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Volumn 109, Issue 24, 2012, Pages 9378-9383

Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation

Author keywords

Crystallography; Kinase activation

Indexed keywords

I KAPPA B KINASE INHIBITOR; TANK BINDING KINASE 1; UNCLASSIFIED DRUG;

EID: 84862233012     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1121552109     Document Type: Article
Times cited : (177)

References (38)
  • 1
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai T, Akira S (2010) The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors. Nat Immunol 11:373-384.
    • (2010) Nat Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 2
    • 80052184362 scopus 로고    scopus 로고
    • Recognition of nucleic acids by pattern-recognition receptors and its relevance in autoimmunity
    • Kawasaki T, Kawai T, Akira S (2011) Recognition of nucleic acids by pattern-recognition receptors and its relevance in autoimmunity. Immunol Rev 243(1):61-73.
    • (2011) Immunol Rev , vol.243 , Issue.1 , pp. 61-73
    • Kawasaki, T.1    Kawai, T.2    Akira, S.3
  • 3
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • Häcker H, Karin M (2006) Regulation and function of IKK and IKK-related kinases. Sci STKE 2006(357):re13.
    • (2006) Sci STKE , vol.2006 , Issue.357
    • Häcker, H.1    Karin, M.2
  • 4
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden MS, Ghosh S (2008) Shared principles in NF-κB signaling. Cell 132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 5
    • 41549165085 scopus 로고    scopus 로고
    • Are the IKKs and IKK-related kinases TBK1 and IKK-ε similarly activated?
    • Chau TL, et al. (2008) Are the IKKs and IKK-related kinases TBK1 and IKK-ε similarly activated? Trends Biochem Sci 33(4):171-180.
    • (2008) Trends Biochem Sci , vol.33 , Issue.4 , pp. 171-180
    • Chau, T.L.1
  • 6
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TLM, Ryzhakov G, Bloor S, von Muhlinen N, Randow F (2009) The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 10:1215-1221.
    • (2009) Nat Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.M.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 7
    • 80053917869 scopus 로고    scopus 로고
    • Polyubiquitin binding to optineurin is required for optimal activation of TANK-binding kinase 1 and production of interferon β
    • Gleason CE, Ordureau A, Gourlay R, Arthur JSC, Cohen P (2011) Polyubiquitin binding to optineurin is required for optimal activation of TANK-binding kinase 1 and production of interferon β. J Biol Chem 286:35663-35674.
    • (2011) J Biol Chem , vol.286 , pp. 35663-35674
    • Gleason, C.E.1    Ordureau, A.2    Gourlay, R.3    Arthur, J.S.C.4    Cohen, P.5
  • 8
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild P, et al. (2011) Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333:228-233.
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1
  • 9
    • 79952335881 scopus 로고    scopus 로고
    • How cells deploy ubiquitin and autophagy to defend their cytosol from bacterial invasion
    • Randow F (2011) How cells deploy ubiquitin and autophagy to defend their cytosol from bacterial invasion. Autophagy 7:304-309.
    • (2011) Autophagy , vol.7 , pp. 304-309
    • Randow, F.1
  • 10
    • 79251566745 scopus 로고    scopus 로고
    • Novel cross-talk within the IKK family controls innate immunity
    • Clark K, et al. (2011) Novel cross-talk within the IKK family controls innate immunity. Biochem J 434(1):93-104.
    • (2011) Biochem J , vol.434 , Issue.1 , pp. 93-104
    • Clark, K.1
  • 11
    • 84858689774 scopus 로고    scopus 로고
    • Synoviocyte innate immune responses: TANK-binding kinase-1 as a potential therapeutic target in rheumatoid arthritis
    • Hammaker D, Boyle DL, Firestein GS (2012) Synoviocyte innate immune responses: TANK-binding kinase-1 as a potential therapeutic target in rheumatoid arthritis. Rheumatology (Oxford) 51:610-618.
    • (2012) Rheumatology (Oxford) , vol.51 , pp. 610-618
    • Hammaker, D.1    Boyle, D.L.2    Firestein, G.S.3
  • 12
    • 51249095133 scopus 로고    scopus 로고
    • The IKK-related kinases: From innate immunity to oncogenesis
    • Clément J-F, 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
    • Clément, J.-F.1    Meloche, S.2    Servant, M.J.3
  • 13
    • 79951517699 scopus 로고    scopus 로고
    • Emerging roles for the non-canonical IKKs in cancer
    • Shen RR, Hahn WC (2011) Emerging roles for the non-canonical IKKs in cancer. Oncogene 30:631-641.
    • (2011) Oncogene , vol.30 , pp. 631-641
    • Shen, R.R.1    Hahn, W.C.2
  • 14
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase
    • Wang D, et al. (2011) The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. J Virol 85:3758-3766.
    • (2011) J Virol , vol.85 , pp. 3758-3766
    • Wang, D.1
  • 15
    • 79951494608 scopus 로고    scopus 로고
    • TBK1 directly engages Akt/PKB survival signaling to support oncogenic transformation
    • Ou Y-H, et al. (2011) TBK1 directly engages Akt/PKB survival signaling to support oncogenic transformation. Mol Cell 41:458-470.
    • (2011) Mol Cell , vol.41 , pp. 458-470
    • Ou, Y.-H.1
  • 16
    • 83755195759 scopus 로고    scopus 로고
    • MIP-T3 is a negative regulator of innate type I IFN response
    • Ng M-HJ, et al. (2011) MIP-T3 is a negative regulator of innate type I IFN response. J Immunol 187:6473-6482.
    • (2011) J Immunol , vol.187 , pp. 6473-6482
    • Ng, M.-H.J.1
  • 17
    • 79251542927 scopus 로고    scopus 로고
    • Akt contributes to activation of the TRIF-dependent signaling pathways of TLRs by interacting with TANK-binding kinase 1
    • Joung SM, et al. (2011) Akt contributes to activation of the TRIF-dependent signaling pathways of TLRs by interacting with TANK-binding kinase 1. J Immunol 186:499-507.
    • (2011) J Immunol , vol.186 , pp. 499-507
    • Joung, S.M.1
  • 18
    • 80054694130 scopus 로고    scopus 로고
    • Activation of STAT6 by STING is critical for antiviral innate immunity
    • Chen H, et al. (2011) Activation of STAT6 by STING is critical for antiviral innate immunity. Cell 147:436-446.
    • (2011) Cell , vol.147 , pp. 436-446
    • Chen, H.1
  • 19
    • 70449091786 scopus 로고    scopus 로고
    • Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1
    • Barbie DA, et al. (2009) Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1. Nature 462(7269):108-112.
    • (2009) Nature , vol.462 , Issue.7269 , pp. 108-112
    • Barbie, D.A.1
  • 21
    • 80755126865 scopus 로고    scopus 로고
    • Mapping a dynamic innate immunity protein interaction network regulating type I interferon production
    • Li S, Wang L, Berman M, Kong Y-Y, Dorf ME (2011) Mapping a dynamic innate immunity protein interaction network regulating type I interferon production. Immunity 35:426-440.
    • (2011) Immunity , vol.35 , pp. 426-440
    • Li, S.1    Wang, L.2    Berman, M.3    Kong, Y.-Y.4    Dorf, M.E.5
  • 23
    • 80052534056 scopus 로고    scopus 로고
    • Functional dissection of the TBK1 molecular network
    • Goncalves A, et al. (2011) Functional dissection of the TBK1 molecular network. PLoS One 6:e23971.
    • (2011) PLoS One , vol.6
    • Goncalves, A.1
  • 24
    • 8544230698 scopus 로고    scopus 로고
    • A novel ubiquitin-like domain in IκB kinase β is required for functional activity of the kinase
    • DOI 10.1074/jbc.M408579200
    • May MJ, Larsen SE, Shim JH, Madge LA, Ghosh S (2004) A novel ubiquitin-like domain in IeκB kinase β is required for functional activity of the kinase. J Biol Chem 279: 45528-45539. (Pubitemid 39491539)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 45528-45539
    • May, M.J.1    Larsen, S.E.2    Shim, J.H.3    Madge, L.A.4    Ghosh, S.5
  • 25
    • 79955481873 scopus 로고    scopus 로고
    • Crystal structure of inhibitor of κB kinase β
    • Xu G, et al. (2011) Crystal structure of inhibitor of κB kinase β. Nature 472:325-330.
    • (2011) Nature , vol.472 , pp. 325-330
    • Xu, G.1
  • 27
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: A further update
    • Bain J, et al. (2007) The selectivity of protein kinase inhibitors: A further update. Biochem J 408:297-315.
    • (2007) Biochem J , vol.408 , pp. 297-315
    • Bain, J.1
  • 28
    • 0000127673 scopus 로고
    • 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng J, et al. (1993) 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr D Biol Crystallogr 49:362-365.
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , pp. 362-365
    • Zheng, J.1
  • 29
    • 34547930163 scopus 로고    scopus 로고
    • Interferon regulatory factor 3 is regulated by a dual phosphorylation- dependent switch
    • DOI 10.1074/jbc.M703019200
    • Panne D, McWhirter SM, Maniatis T, Harrison SC (2007) Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch. J Biol Chem 282:22816-22822. (Pubitemid 47267373)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22816-22822
    • Panne, D.1    McWhirter, S.M.2    Maniatis, T.3    Harrison, S.C.4
  • 30
    • 49149114140 scopus 로고    scopus 로고
    • The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response
    • Soulat D, et al. (2008) The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response. EMBO J 27:2135-2146.
    • (2008) EMBO J , vol.27 , pp. 2135-2146
    • Soulat, D.1
  • 31
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase
    • DOI 10.1016/S0014-5793(96)01370-1, PII S0014579396013701
    • Alessi DR, Caudwell FB, Andjelkovic M, Hemmings BA, Cohen P (1996) Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett 399:333-338. (Pubitemid 26426877)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    Andjelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 34
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: A common mechanism of kinase autophosphorylation?
    • DOI 10.1016/j.tibs.2007.06.004, PII S0968000407001478
    • Oliver AW, Knapp S, Pearl LH (2007) Activation segment exchange: A common mechanism of kinase autophosphorylation? Trends Biochem Sci 32:351-356. (Pubitemid 47126856)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.8 , pp. 351-356
    • Oliver, A.W.1    Knapp, S.2    Pearl, L.H.3
  • 35
    • 59949105249 scopus 로고    scopus 로고
    • Crystal structure of domain-swapped STE20 OSR1 kinase domain
    • Lee S-J, Cobb MH, Goldsmith EJ (2009) Crystal structure of domain-swapped STE20 OSR1 kinase domain. Protein Sci 18:304-313.
    • (2009) Protein Sci , vol.18 , pp. 304-313
    • Lee, S.-J.1    Cobb, M.H.2    Goldsmith, E.J.3
  • 36
    • 33750443289 scopus 로고    scopus 로고
    • IeκB kinase complexes: Gateways to NF-κB activation and transcription
    • Scheidereit C (2006) IeκB kinase complexes: Gateways to NF-κB activation and transcription. Oncogene 25:6685-6705.
    • (2006) Oncogene , vol.25 , pp. 6685-6705
    • Scheidereit, C.1
  • 37
    • 34548611290 scopus 로고    scopus 로고
    • PKA-I Holoenzyme Structure Reveals a Mechanism for cAMP-Dependent Activation
    • DOI 10.1016/j.cell.2007.07.018, PII S0092867407009555
    • Kim C, Cheng CY, Saldanha SA, Taylor SS (2007) PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation. Cell 130:1032-1043. (Pubitemid 47410267)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1032-1043
    • Kim, C.1    Cheng, C.Y.2    Saldanha, S.A.3    Taylor, S.S.4
  • 38
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • DOI 10.1038/nrm1527
    • Wong W, Scott JD (2004) AKAP signalling complexes: Focal points in space and time. Nat Rev Mol Cell Biol 5:959-970. (Pubitemid 39611533)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.12 , pp. 959-970
    • Wong, W.1    Scott, J.D.2


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