메뉴 건너뛰기




Volumn 192, Issue 4, 2014, Pages 1855-1861

Casein kinase 1γ1 inhibits the RIG-I/TLR signaling pathway through phosphorylating p65 and promoting its degradation

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; CASEIN KINASE I; CELL LINE; CULLIN PROTEINS; DEAD-BOX RNA HELICASES; ENZYME ACTIVATION; HEK293 CELLS; HUMANS; INTERFERON-BETA; PHOSPHORYLATION; RNA INTERFERENCE; RNA, SMALL INTERFERING; SENDAI VIRUS; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTORS; TRANSCRIPTION FACTOR RELA;

EID: 84894281723     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1302552     Document Type: Article
Times cited : (22)

References (33)
  • 1
    • 77956170809 scopus 로고    scopus 로고
    • RNA-based antiviral immunity
    • Ding, S. W. 2010. RNA-based antiviral immunity. Nat. Rev. Immunol. 10: 632-644.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 632-644
    • Ding, S.W.1
  • 2
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3
    • Seth, R. B., L. Sun, C. K. Ea, and Z. J. Chen. 2005. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3. Cell 122: 669-682.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 3
    • 58049217490 scopus 로고    scopus 로고
    • RNA recognition and signal transduction by RIG-I-like receptors
    • Yoneyama, M., and T. Fujita. 2009. RNA recognition and signal transduction by RIG-I-like receptors. Immunol. Rev. 227: 54-65.
    • (2009) Immunol. Rev. , vol.227 , pp. 54-65
    • Yoneyama, M.1    Fujita, T.2
  • 4
    • 79956314622 scopus 로고    scopus 로고
    • Immune signaling by RIG-I-like receptors
    • Loo, Y. M., and M. Gale, Jr. 2011. Immune signaling by RIG-I-like receptors. Immunity 34: 680-692.
    • (2011) Immunity , vol.34 , pp. 680-692
    • Loo, Y.M.1    Gale Jr., M.2
  • 5
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: Remarkable progress and outstanding questions
    • Hayden, M. S., and S. Ghosh. 2012. NF-κB, 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
  • 6
    • 79952591283 scopus 로고    scopus 로고
    • The measles virus v protein binds to p65 (RelA) to suppress NF-κB activity
    • Schuhmann, K. M., C. K. Pfaller, and K. K. Conzelmann. 2011. The measles virus V protein binds to p65 (RelA) to suppress NF-κB activity. J. Virol. 85: 3162-3171.
    • (2011) J. Virol. , vol.85 , pp. 3162-3171
    • Schuhmann, K.M.1    Pfaller, C.K.2    Conzelmann, K.K.3
  • 10
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • Knippschild, U., A. Gocht, S. Wolff, N. Huber, J. Löhler, and M. Stöter. 2005. The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. Cell. Signal. 17: 675-689.
    • (2005) Cell. Signal. , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Löhler, J.5    Stöter, M.6
  • 11
    • 28644444440 scopus 로고    scopus 로고
    • Casein kinase 1 g couples Wnt receptor activation to cytoplasmic signal transduction
    • Davidson, G., W. Wu, J. Shen, J. Bilic, U. Fenger, P. Stannek, A. Glinka, and C. Niehrs. 2005. Casein kinase 1 g couples Wnt receptor activation to cytoplasmic signal transduction. Nature 438: 867-872.
    • (2005) Nature , vol.438 , pp. 867-872
    • Davidson, G.1    Wu, W.2    Shen, J.3    Bilic, J.4    Fenger, U.5    Stannek, P.6    Glinka, A.7    Niehrs, C.8
  • 13
    • 78951493072 scopus 로고    scopus 로고
    • Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic shuttling of mammalian translation initiation factor eIF6
    • Biswas, A., S. Mukherjee, S. Das, D. Shields, C. W. Chow, and U. Maitra. 2011. Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic shuttling of mammalian translation initiation factor eIF6. J. Biol. Chem. 286: 3129-3138.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3129-3138
    • Biswas, A.1    Mukherjee, S.2    Das, S.3    Shields, D.4    Chow, C.W.5    Maitra, U.6
  • 14
    • 17144457602 scopus 로고    scopus 로고
    • Interaction of casein kinase 1 delta (CK1d) with post-Golgi structures, microtubules and the spindle apparatus
    • Behrend, L., M. Stöter, M. Kurth, G. Rutter, J. Heukeshoven, W. Deppert, and U. Knippschild. 2000. Interaction of casein kinase 1 delta (CK1d) with post-Golgi structures, microtubules and the spindle apparatus. Eur. J. Cell Biol. 79: 240-251.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 240-251
    • Behrend, L.1    Stöter, M.2    Kurth, M.3    Rutter, G.4    Heukeshoven, J.5    Deppert, W.6    Knippschild, U.7
  • 15
    • 84869748782 scopus 로고    scopus 로고
    • Ndfip1 negatively regulates RIG-Idependent immune signaling by enhancing E3 ligase Smurf1-mediated MAVS degradation
    • Wang, Y. T., X. M. Tong, and X. Ye. 2012. Ndfip1 negatively regulates RIG-Idependent immune signaling by enhancing E3 ligase Smurf1-mediated MAVS degradation. J. Immunol. 189: 5304-5313.
    • (2012) J. Immunol. , vol.189 , pp. 5304-5313
    • Wang, Y.T.1    Tong, X.M.2    Ye, X.3
  • 16
    • 84867264050 scopus 로고    scopus 로고
    • Tetraspanin 6 (TSPAN6) negatively regulates retinoic acid-inducible gene I-like receptor-mediated immune signaling in a ubiquitination-dependent manner
    • Wang, Y. T., X. M. Tong, E. S. Omoregie, W. J. Liu, S. D. Meng, and X. Ye. 2012. Tetraspanin 6 (TSPAN6) negatively regulates retinoic acid-inducible gene I-like receptor-mediated immune signaling in a ubiquitination-dependent manner. J. Biol. Chem. 287: 34626-34634.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34626-34634
    • Wang, Y.T.1    Tong, X.M.2    Omoregie, E.S.3    Liu, W.J.4    Meng, S.D.5    Ye, X.6
  • 18
    • 0033662144 scopus 로고    scopus 로고
    • Cell-cycle regulation in immunity, tolerance and autoimmunity
    • Balomenos, D., and C. Martínez-A. 2000. Cell-cycle regulation in immunity, tolerance and autoimmunity. Immunol. Today 21: 551-555.
    • (2000) Immunol. Today , vol.21 , pp. 551-555
    • Balomenos, D.1    Martínez-A, C.2
  • 19
    • 84873444909 scopus 로고    scopus 로고
    • Perturbation of cell cycle regulation triggers plant immune response via activation of disease resistance genes
    • Bao, Z., H. Yang, and J. Hua. 2013. Perturbation of cell cycle regulation triggers plant immune response via activation of disease resistance genes. Proc. Natl. Acad. Sci. USA 110: 2407-2412.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2407-2412
    • Bao, Z.1    Yang, H.2    Hua, J.3
  • 20
    • 9644262497 scopus 로고    scopus 로고
    • Phosphorylation of serine 468 by GSK-3β negatively regulates basal p65 NF-κB activity
    • Buss, H., A. Dörrie, M. L. Schmitz, R. Frank, M. Livingstone, K. Resch, and M. Kracht. 2004. Phosphorylation of serine 468 by GSK-3β negatively regulates basal p65 NF-κB activity. J. Biol. Chem. 279: 49571-49574.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49571-49574
    • Buss, H.1    Dörrie, A.2    Schmitz, M.L.3    Frank, R.4    Livingstone, M.5    Resch, K.6    Kracht, M.7
  • 21
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai, H., H. Chiba, H. Miyoshi, T. Sugita, and W. Toriumi. 1999. IκB kinases phosphorylate NF-κB 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
  • 22
    • 0141703513 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway
    • Sakurai, H., S. Suzuki, N. Kawasaki, H. Nakano, T. Okazaki, A. Chino, T. Doi, and I. Saiki. 2003. Tumor necrosis factor-α-induced IKK phosphorylation of NF-κB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway. J. Biol. Chem. 278: 36916-36923.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36916-36923
    • Sakurai, H.1    Suzuki, S.2    Kawasaki, N.3    Nakano, H.4    Okazaki, T.5    Chino, A.6    Doi, T.7    Saiki, I.8
  • 23
    • 80051673744 scopus 로고    scopus 로고
    • Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1
    • Meng, Z., L. Capalbo, D. M. Glover, and W. G. Dunphy. 2011. Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1. Mol. Biol. Cell 22: 2834-2847.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2834-2847
    • Meng, Z.1    Capalbo, L.2    Glover, D.M.3    Dunphy, W.G.4
  • 24
    • 17844386319 scopus 로고    scopus 로고
    • IKKα limits macrophage NF-κB activation and contributes to the resolution of inflammation
    • Lawrence, T., M. Bebien, G. Y. Liu, V. Nizet, and M. Karin. 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
  • 26
    • 48249149162 scopus 로고    scopus 로고
    • RIG-I mediates the coinduction of tumor necrosis factor and type I interferon elicited by myxoma virus in primary human macrophages
    • Wang, F., X. J. Gao, J. W. Barrett, Q. Shao, E. Bartee, M. R. Mohamed, M. Rahman, S. Werden, T. Irvine, J. X. Cao, et al. 2008. RIG-I mediates the coinduction of tumor necrosis factor and type I interferon elicited by myxoma virus in primary human macrophages. PLoS Pathog. 4: e1000099.
    • (2008) PLoS Pathog. , vol.4
    • Wang, F.1    Gao, X.J.2    Barrett, J.W.3    Shao, Q.4    Bartee, E.5    Mohamed, M.R.6    Rahman, M.7    Werden, S.8    Irvine, T.9    Cao, J.X.10
  • 29
    • 78650665171 scopus 로고    scopus 로고
    • Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response
    • Sun, Z. G., H. W. Ren, Y. Liu, J. L. Teeling, and J. Gu. 2011. Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response. J. Virol. 85: 1036-1047.
    • (2011) J. Virol. , vol.85 , pp. 1036-1047
    • Sun, Z.G.1    Ren, H.W.2    Liu, Y.3    Teeling, J.L.4    Gu, J.5
  • 30
    • 65649141586 scopus 로고    scopus 로고
    • Pathogen recognition in the innate immune response
    • Kumar, H., T. Kawai, and S. Akira. 2009. Pathogen recognition in the innate immune response. Biochem. J. 420: 1-16.
    • (2009) Biochem. J. , vol.420 , pp. 1-16
    • Kumar, H.1    Kawai, T.2    Akira, S.3
  • 31
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri, T., J. W. Yu, P. Datta, J. Wu, and E. S. Alnemri. 2009. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458: 509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 33
    • 80052969639 scopus 로고    scopus 로고
    • The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
    • Zhang, Z., B. Yuan, M. Bao, N. Lu, T. Kim, and Y. J. Liu. 2011. The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells. Nat. Immunol. 12: 959-965.
    • (2011) Nat. Immunol. , vol.12 , pp. 959-965
    • Zhang, Z.1    Yuan, B.2    Bao, M.3    Lu, N.4    Kim, T.5    Liu, Y.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.