메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

The Ubiquitin Ligase TRAF6 Negatively Regulates the JAK-STAT Signaling Pathway by Binding to STAT3 and Mediating Its Ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; ALPHA INTERFERON; C REACTIVE PROTEIN; JANUS KINASE 2; STAT3 PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 84869767938     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049567     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE Jr, Kerr IM, Stark GR, (1994) Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264: 1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 2
    • 0028349735 scopus 로고
    • Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Zhong Z, Wen Z, Darnell JE Jr, (1994) Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264: 95-98.
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell Jr., J.E.3
  • 3
    • 0032213273 scopus 로고    scopus 로고
    • Stat3 activation is responsible for IL-6-dependent T cell proliferation through preventing apoptosis: generation and characterization of T cell-specific Stat3-deficient mice
    • Takeda K, Kaisho T, Yoshida N, Takeda J, Kishimoto T, et al. (1998) Stat3 activation is responsible for IL-6-dependent T cell proliferation through preventing apoptosis: generation and characterization of T cell-specific Stat3-deficient mice. J Immunol 161: 4652-4660.
    • (1998) J Immunol , vol.161 , pp. 4652-4660
    • Takeda, K.1    Kaisho, T.2    Yoshida, N.3    Takeda, J.4    Kishimoto, T.5
  • 4
    • 79952207466 scopus 로고    scopus 로고
    • Novel role for STAT3 in transcriptional regulation of NK immune cell targeting receptor MICA on cancer cells
    • Bedel R, Thiery-Vuillemin A, Grandclement C, Balland J, Remy-Martin JP, et al. (2011) Novel role for STAT3 in transcriptional regulation of NK immune cell targeting receptor MICA on cancer cells. Cancer Res 71: 1615-1626.
    • (2011) Cancer Res , vol.71 , pp. 1615-1626
    • Bedel, R.1    Thiery-Vuillemin, A.2    Grandclement, C.3    Balland, J.4    Remy-Martin, J.P.5
  • 5
    • 0028922433 scopus 로고
    • A major role for the protein tyrosine kinase JAK1 in the JAK/STAT signal transduction pathway in response to interleukin-6
    • Guschin D, Rogers N, Briscoe J, Witthuhn B, Watling D, et al. (1995) A major role for the protein tyrosine kinase JAK1 in the JAK/STAT signal transduction pathway in response to interleukin-6. Embo J 14: 1421-1429.
    • (1995) Embo J , vol.14 , pp. 1421-1429
    • Guschin, D.1    Rogers, N.2    Briscoe, J.3    Witthuhn, B.4    Watling, D.5
  • 6
    • 62449283132 scopus 로고    scopus 로고
    • Sustained Src inhibition results in signal transducer and activator of transcription 3 (STAT3) activation and cancer cell survival via altered Janus-activated kinase-STAT3 binding
    • Sen B, Saigal B, Parikh N, Gallick G, Johnson FM, (2009) Sustained Src inhibition results in signal transducer and activator of transcription 3 (STAT3) activation and cancer cell survival via altered Janus-activated kinase-STAT3 binding. Cancer Res 69: 1958-1965.
    • (2009) Cancer Res , vol.69 , pp. 1958-1965
    • Sen, B.1    Saigal, B.2    Parikh, N.3    Gallick, G.4    Johnson, F.M.5
  • 7
    • 19444385692 scopus 로고    scopus 로고
    • Stat3 regulates genes common to both wound healing and cancer
    • Dauer DJ, Ferraro B, Song L, Yu B, Mora L, et al. (2005) Stat3 regulates genes common to both wound healing and cancer. Oncogene 24: 3397-3408.
    • (2005) Oncogene , vol.24 , pp. 3397-3408
    • Dauer, D.J.1    Ferraro, B.2    Song, L.3    Yu, B.4    Mora, L.5
  • 8
    • 69549116880 scopus 로고    scopus 로고
    • The E3 ligase TRAF6 regulates Akt ubiquitination and activation
    • Yang WL, Wang J, Chan CH, Lee SW, Campos AD, et al. (2009) The E3 ligase TRAF6 regulates Akt ubiquitination and activation. Science 325: 1134-1138.
    • (2009) Science , vol.325 , pp. 1134-1138
    • Yang, W.L.1    Wang, J.2    Chan, C.H.3    Lee, S.W.4    Campos, A.D.5
  • 9
    • 65049086930 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation
    • Wicovsky A, Henkler F, Salzmann S, Scheurich P, Kneitz C, et al. (2009) Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation. Oncogene 28: 1769-1781.
    • (2009) Oncogene , vol.28 , pp. 1769-1781
    • Wicovsky, A.1    Henkler, F.2    Salzmann, S.3    Scheurich, P.4    Kneitz, C.5
  • 10
    • 33947506490 scopus 로고    scopus 로고
    • Specificity of TRAF3 in its negative regulation of the noncanonical NF-kappa B pathway
    • He JQ, Saha SK, Kang JR, Zarnegar B, Cheng G, (2007) Specificity of TRAF3 in its negative regulation of the noncanonical NF-kappa B pathway. J Biol Chem 282: 3688-3694.
    • (2007) J Biol Chem , vol.282 , pp. 3688-3694
    • He, J.Q.1    Saha, S.K.2    Kang, J.R.3    Zarnegar, B.4    Cheng, G.5
  • 11
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida T, Mizushima S, Azuma S, Kobayashi N, Tojo T, et al. (1996) Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J Biol Chem 271: 28745-28748.
    • (1996) J Biol Chem , vol.271 , pp. 28745-28748
    • Ishida, T.1    Mizushima, S.2    Azuma, S.3    Kobayashi, N.4    Tojo, T.5
  • 12
    • 31344463886 scopus 로고    scopus 로고
    • Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling
    • Wang Y, Tang Y, Teng L, Wu Y, Zhao X, et al. (2006) Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling. Nat Immunol 7: 139-147.
    • (2006) Nat Immunol , vol.7 , pp. 139-147
    • Wang, Y.1    Tang, Y.2    Teng, L.3    Wu, Y.4    Zhao, X.5
  • 13
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • Martin MU, Wesche H, (2002) Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim Biophys Acta 1592: 265-280.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 14
    • 79951852219 scopus 로고    scopus 로고
    • Mutational analysis of TRAF6 reveals a conserved functional role of the RING dimerization interface and a potentially necessary but insufficient role of RING-dependent TRAF6 polyubiquitination towards NF-kappaB activation
    • Megas C, Hatzivassiliou EG, Yin Q, Marinopoulou E, Hadweh P, et al. (2011) Mutational analysis of TRAF6 reveals a conserved functional role of the RING dimerization interface and a potentially necessary but insufficient role of RING-dependent TRAF6 polyubiquitination towards NF-kappaB activation. Cell Signal 23: 772-777.
    • (2011) Cell Signal , vol.23 , pp. 772-777
    • Megas, C.1    Hatzivassiliou, E.G.2    Yin, Q.3    Marinopoulou, E.4    Hadweh, P.5
  • 15
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai T, Sato S, Ishii KJ, Coban C, Hemmi H, et al. (2004) Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nat Immunol 5: 1061-1068.
    • (2004) Nat Immunol , vol.5 , pp. 1061-1068
    • Kawai, T.1    Sato, S.2    Ishii, K.J.3    Coban, C.4    Hemmi, H.5
  • 16
    • 0033561039 scopus 로고    scopus 로고
    • TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling
    • Lomaga MA, Yeh WC, Sarosi I, Duncan GS, Furlonger C, et al. (1999) TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev 13: 1015-1024.
    • (1999) Genes Dev , vol.13 , pp. 1015-1024
    • Lomaga, M.A.1    Yeh, W.C.2    Sarosi, I.3    Duncan, G.S.4    Furlonger, C.5
  • 17
    • 84855287537 scopus 로고    scopus 로고
    • CUEDC2 (CUE domain-containing 2) and SOCS3 (suppressors of cytokine signaling 3) cooperate to negatively regulate Janus kinase 1/signal transducers and activators of transcription 3 signaling
    • Zhang WN, Wang L, Wang Q, Luo X, Fang DF, et al. (2012) CUEDC2 (CUE domain-containing 2) and SOCS3 (suppressors of cytokine signaling 3) cooperate to negatively regulate Janus kinase 1/signal transducers and activators of transcription 3 signaling. J Biol Chem 287: 382-392.
    • (2012) J Biol Chem , vol.287 , pp. 382-392
    • Zhang, W.N.1    Wang, L.2    Wang, Q.3    Luo, X.4    Fang, D.F.5
  • 18
    • 70349568369 scopus 로고    scopus 로고
    • Green tea catechins inhibit angiogenesis through suppression of STAT3 activation
    • Leong H, Mathur PS, Greene GL, (2009) Green tea catechins inhibit angiogenesis through suppression of STAT3 activation. Breast Cancer Res Treat 117: 505-515.
    • (2009) Breast Cancer Res Treat , vol.117 , pp. 505-515
    • Leong, H.1    Mathur, P.S.2    Greene, G.L.3
  • 19
    • 0034329453 scopus 로고    scopus 로고
    • The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3
    • Rodel B, Tavassoli K, Karsunky H, Schmidt T, Bachmann M, et al. (2000) The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3. Embo J 19: 5845-5855.
    • (2000) Embo J , vol.19 , pp. 5845-5855
    • Rodel, B.1    Tavassoli, K.2    Karsunky, H.3    Schmidt, T.4    Bachmann, M.5
  • 20
    • 39449123058 scopus 로고    scopus 로고
    • Crif1 is a novel transcriptional coactivator of STAT3
    • Kwon MC, Koo BK, Moon JS, Kim YY, Park KC, et al. (2008) Crif1 is a novel transcriptional coactivator of STAT3. Embo J 27: 642-653.
    • (2008) Embo J , vol.27 , pp. 642-653
    • Kwon, M.C.1    Koo, B.K.2    Moon, J.S.3    Kim, Y.Y.4    Park, K.C.5
  • 21
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung CD, Liao J, Liu B, Rao X, Jay P, et al. (1997) Specific inhibition of Stat3 signal transduction by PIAS3. Science 278: 1803-1805.
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5
  • 22
    • 67949110955 scopus 로고    scopus 로고
    • Nuclear protein IkappaB-zeta inhibits the activity of STAT3
    • Wu Z, Zhang X, Yang J, Wu G, Zhang Y, et al. (2009) Nuclear protein IkappaB-zeta inhibits the activity of STAT3. Biochem Biophys Res Commun 387: 348-352.
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 348-352
    • Wu, Z.1    Zhang, X.2    Yang, J.3    Wu, G.4    Zhang, Y.5
  • 23
    • 77954634242 scopus 로고    scopus 로고
    • The scaffold protein TANK/I-TRAF inhibits NF-kappaB activation by recruiting polo-like kinase 1
    • Zhang W, Wang J, Zhang Y, Yuan Y, Guan W, et al. (2010) The scaffold protein TANK/I-TRAF inhibits NF-kappaB activation by recruiting polo-like kinase 1. Mol Biol Cell 21: 2500-2513.
    • (2010) Mol Biol Cell , vol.21 , pp. 2500-2513
    • Zhang, W.1    Wang, J.2    Zhang, Y.3    Yuan, Y.4    Guan, W.5
  • 25
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia ZP, Sun L, Chen X, Pineda G, Jiang X, et al. (2009) Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 461: 114-119.
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3    Pineda, G.4    Jiang, X.5
  • 26
    • 67349242723 scopus 로고    scopus 로고
    • E2 interaction and dimerization in the crystal structure of TRAF6
    • Yin Q, Lin SC, Lamothe B, Lu M, Lo YC, et al. (2009) E2 interaction and dimerization in the crystal structure of TRAF6. Nat Struct Mol Biol 16: 658-666.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 658-666
    • Yin, Q.1    Lin, S.C.2    Lamothe, B.3    Lu, M.4    Lo, Y.C.5
  • 27
    • 33947721445 scopus 로고    scopus 로고
    • Structure, interactions, and dynamics of the RING domain from human TRAF6
    • Mercier P, Lewis MJ, Hau DD, Saltibus LF, Xiao W, et al. (2007) Structure, interactions, and dynamics of the RING domain from human TRAF6. Protein Sci 16: 602-614.
    • (2007) Protein Sci , vol.16 , pp. 602-614
    • Mercier, P.1    Lewis, M.J.2    Hau, D.D.3    Saltibus, L.F.4    Xiao, W.5
  • 28
    • 0030000589 scopus 로고    scopus 로고
    • STAT3 participates in transcriptional activation of the C-reactive protein gene by interleukin-6
    • Zhang D, Sun M, Samols D, Kushner I, (1996) STAT3 participates in transcriptional activation of the C-reactive protein gene by interleukin-6. J Biol Chem 271: 9503-9509.
    • (1996) J Biol Chem , vol.271 , pp. 9503-9509
    • Zhang, D.1    Sun, M.2    Samols, D.3    Kushner, I.4
  • 29
    • 0345826123 scopus 로고    scopus 로고
    • Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism
    • Yoshida Y, Kumar A, Koyama Y, Peng H, Arman A, et al. (2004) Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism. J Biol Chem 279: 1768-1776.
    • (2004) J Biol Chem , vol.279 , pp. 1768-1776
    • Yoshida, Y.1    Kumar, A.2    Koyama, Y.3    Peng, H.4    Arman, A.5
  • 30
    • 67649988989 scopus 로고    scopus 로고
    • Mitochondrial STAT3 supports Ras-dependent oncogenic transformation
    • Gough DJ, Corlett A, Schlessinger K, Wegrzyn J, Larner AC, et al. (2009) Mitochondrial STAT3 supports Ras-dependent oncogenic transformation. Science 324: 1713-1716.
    • (2009) Science , vol.324 , pp. 1713-1716
    • Gough, D.J.1    Corlett, A.2    Schlessinger, K.3    Wegrzyn, J.4    Larner, A.C.5
  • 31
    • 65549114590 scopus 로고    scopus 로고
    • ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells
    • Hawthorne VS, Huang WC, Neal CL, Tseng LM, Hung MC, et al. (2009) ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. Mol Cancer Res 7: 592-600.
    • (2009) Mol Cancer Res , vol.7 , pp. 592-600
    • Hawthorne, V.S.1    Huang, W.C.2    Neal, C.L.3    Tseng, L.M.4    Hung, M.C.5
  • 32
    • 67449123326 scopus 로고    scopus 로고
    • Acetylation and activation of STAT3 mediated by nuclear translocation of CD44
    • Lee JL, Wang MJ, Chen JY, (2009) Acetylation and activation of STAT3 mediated by nuclear translocation of CD44. J Cell Biol 185: 949-957.
    • (2009) J Cell Biol , vol.185 , pp. 949-957
    • Lee, J.L.1    Wang, M.J.2    Chen, J.Y.3
  • 33
    • 79952538100 scopus 로고    scopus 로고
    • Lysine methylation of promoter-bound transcription factors and relevance to cancer
    • Stark GR, Wang Y, Lu T, (2011) Lysine methylation of promoter-bound transcription factors and relevance to cancer. Cell Res 21: 375-380.
    • (2011) Cell Res , vol.21 , pp. 375-380
    • Stark, G.R.1    Wang, Y.2    Lu, T.3
  • 34
    • 10644271682 scopus 로고    scopus 로고
    • TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3
    • Perry E, Tsruya R, Levitsky P, Pomp O, Taller M, et al. (2004) TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3. Oncogene 23: 8908-8919.
    • (2004) Oncogene , vol.23 , pp. 8908-8919
    • Perry, E.1    Tsruya, R.2    Levitsky, P.3    Pomp, O.4    Taller, M.5
  • 35
    • 0028937707 scopus 로고
    • Spacing of palindromic half sites as a determinant of selective STAT (signal transducers and activators of transcription) DNA binding and transcriptional activity
    • Seidel HM, Milocco LH, Lamb P, Darnell JE Jr, Stein RB, et al. (1995) Spacing of palindromic half sites as a determinant of selective STAT (signal transducers and activators of transcription) DNA binding and transcriptional activity. Proc Natl Acad Sci U S A 92: 3041-3045.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3041-3045
    • Seidel, H.M.1    Milocco, L.H.2    Lamb, P.3    Darnell Jr., J.E.4    Stein, R.B.5
  • 36
    • 0036256644 scopus 로고    scopus 로고
    • What does Stat3 do?
    • Levy DE, Lee CK, (2002) What does Stat3 do? J Clin Invest 109: 1143-1148.
    • (2002) J Clin Invest , vol.109 , pp. 1143-1148
    • Levy, D.E.1    Lee, C.K.2
  • 37
    • 79952724023 scopus 로고    scopus 로고
    • Suppression of signal transducer and activator of transcription 3 activation by butein inhibits growth of human hepatocellular carcinoma in vivo
    • Rajendran P, Ong TH, Chen L, Li F, Shanmugam MK, et al. (2011) Suppression of signal transducer and activator of transcription 3 activation by butein inhibits growth of human hepatocellular carcinoma in vivo. Clin Cancer Res 17: 1425-1439.
    • (2011) Clin Cancer Res , vol.17 , pp. 1425-1439
    • Rajendran, P.1    Ong, T.H.2    Chen, L.3    Li, F.4    Shanmugam, M.K.5
  • 38
    • 77949281908 scopus 로고    scopus 로고
    • [Advances of the correlation between JAK-STAT3 signaling pathway and the biological behavior of non-small cell lung cancer]
    • Yu Y, Wang Z, (2010) [Advances of the correlation between JAK-STAT3 signaling pathway and the biological behavior of non-small cell lung cancer]. Zhongguo Fei Ai Za Zhi 13: 160-164.
    • (2010) Zhongguo Fei Ai Za Zhi , vol.13 , pp. 160-164
    • Yu, Y.1    Wang, Z.2
  • 39
    • 78650274037 scopus 로고    scopus 로고
    • Stat3 as a therapeutic target for the treatment of psoriasis: a clinical feasibility study with STA-21, a Stat3 inhibitor
    • Miyoshi K, Takaishi M, Nakajima K, Ikeda M, Kanda T, et al. (2011) Stat3 as a therapeutic target for the treatment of psoriasis: a clinical feasibility study with STA-21, a Stat3 inhibitor. J Invest Dermatol 131: 108-117.
    • (2011) J Invest Dermatol , vol.131 , pp. 108-117
    • Miyoshi, K.1    Takaishi, M.2    Nakajima, K.3    Ikeda, M.4    Kanda, T.5
  • 40
    • 63249104202 scopus 로고    scopus 로고
    • Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination
    • Xu K, Shimelis H, Linn DE, Jiang R, Yang X, et al. (2009) Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination. Cancer Cell 15: 270-282.
    • (2009) Cancer Cell , vol.15 , pp. 270-282
    • Xu, K.1    Shimelis, H.2    Linn, D.E.3    Jiang, R.4    Yang, X.5
  • 41
  • 42
    • 79959531020 scopus 로고    scopus 로고
    • Regulation of RANKL-induced osteoclastogenesis by TGF-beta through molecular interaction between Smad3 and Traf6
    • Yasui T, Kadono Y, Nakamura M, Oshima Y, Matsumoto T, et al. (2011) Regulation of RANKL-induced osteoclastogenesis by TGF-beta through molecular interaction between Smad3 and Traf6. J Bone Miner Res 26: 1447-1456.
    • (2011) J Bone Miner Res , vol.26 , pp. 1447-1456
    • Yasui, T.1    Kadono, Y.2    Nakamura, M.3    Oshima, Y.4    Matsumoto, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.