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Volumn 5, Issue , 2015, Pages

Polyubiquitination of Transforming Growth Factor β-activated Kinase 1 (TAK1) at Lysine 562 Residue Regulates TLR4-mediated JNK and p38 MAPK Activation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; I KAPPA B KINASE; LYSINE; MAP KINASE KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN; STRESS ACTIVATED PROTEIN KINASE; TAB1 PROTEIN, HUMAN; TOLL LIKE RECEPTOR 4; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 84937686124     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep12300     Document Type: Article
Times cited : (49)

References (45)
  • 1
    • 0029551805 scopus 로고
    • Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction
    • Yamaguchi, K. et al. Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction. Science 270, 2008-2011 (1995).
    • (1995) Science , vol.270 , pp. 2008-2011
    • Yamaguchi, K.1
  • 2
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim, J. H. et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 19, 2668-2681 (2005).
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1
  • 3
    • 84880847105 scopus 로고    scopus 로고
    • Cell type-specific function of TAK1 in innate immune signaling
    • Ajibade, A. A., Wang, H. Y. & Wang, R. F. Cell type-specific function of TAK1 in innate immune signaling. Trends Immunol 34, 307-316 (2013).
    • (2013) Trends Immunol , vol.34 , pp. 307-316
    • Ajibade, A.A.1    Wang, H.Y.2    Wang, R.F.3
  • 4
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase TAK1 in innate and adaptive immune responses
    • Sato, S. et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol 6, 1087-1095 (2005).
    • (2005) Nat Immunol , vol.6 , pp. 1087-1095
    • Sato, S.1
  • 5
    • 84856301921 scopus 로고    scopus 로고
    • TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1+ CD11b+ neutrophils
    • Ajibade, A. A. et al. TAK1 negatively regulates NF-kappaB and p38 MAP kinase activation in Gr-1+ CD11b+ neutrophils. Immunity 36, 43-54 (2012).
    • (2012) Immunity , vol.36 , pp. 43-54
    • Ajibade, A.A.1
  • 6
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S. & Takeda, K. Toll-like receptor signalling. Nat Rev Immunol 4, 499-511 (2004).
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 8
    • 74049136127 scopus 로고    scopus 로고
    • Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines
    • Tseng, P. H. et al. Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines. Nat Immunol 11, 70-75 (2010).
    • (2010) Nat Immunol , vol.11 , pp. 70-75
    • Tseng, P.H.1
  • 9
    • 15844431960 scopus 로고    scopus 로고
    • A novel kinase cascade mediated by mitogen-activated protein kinase kinase 6 and MKK3
    • Moriguchi, T. et al. A novel kinase cascade mediated by mitogen-activated protein kinase kinase 6 and MKK3. J Biol Chem 271, 13675-13679 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 13675-13679
    • Moriguchi, T.1
  • 10
    • 0030968634 scopus 로고    scopus 로고
    • TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-jun N-terminal kinase
    • Shirakabe, K. et al. TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase. J Biol Chem 272, 8141-8144 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 8141-8144
    • Shirakabe, K.1
  • 11
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang, C. et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412, 346-351 (2001).
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1
  • 12
    • 0033537866 scopus 로고    scopus 로고
    • Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation
    • Sakurai, H., Miyoshi, H., Toriumi, W. & Sugita, T. Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation. J Biol Chem 274, 10641-10648 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 10641-10648
    • Sakurai, H.1    Miyoshi, H.2    Toriumi, W.3    Sugita, T.4
  • 13
    • 0029940355 scopus 로고    scopus 로고
    • TAB1: An activator of the TAK1 MAPKKK in TGF-beta signal transduction
    • Shibuya, H. et al. TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction. Science 272, 1179-1182 (1996).
    • (1996) Science , vol.272 , pp. 1179-1182
    • Shibuya, H.1
  • 14
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu, G. et al. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 5, 649-658 (2000).
    • (2000) Mol Cell , vol.5 , pp. 649-658
    • Takaesu, G.1
  • 15
    • 0037214344 scopus 로고    scopus 로고
    • The TAK1-NLK mitogen-activated protein kinase cascade functions in the wnt-5a/Ca(2+) pathway to antagonize wnt/beta-catenin signaling
    • Ishitani, T. et al. The TAK1-NLK mitogen-activated protein kinase cascade functions in the Wnt-5a/Ca(2+) pathway to antagonize Wnt/beta-catenin signaling. Mol Cell Biol 23, 131-139 (2003).
    • (2003) Mol Cell Biol , vol.23 , pp. 131-139
    • Ishitani, T.1
  • 16
    • 14844295421 scopus 로고    scopus 로고
    • Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-beta-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2
    • Singhirunnusorn, P., Suzuki, S., Kawasaki, N., Saiki, I. & Sakurai, H. Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-beta-activated kinase 1 (TAK1) in a signaling complex containing TAK1-binding protein TAB1 and TAB2. J Biol Chem 280, 7359-7368 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 7359-7368
    • Singhirunnusorn, P.1    Suzuki, S.2    Kawasaki, N.3    Saiki, I.4    Sakurai, H.5
  • 17
    • 77955497476 scopus 로고    scopus 로고
    • Autoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular process
    • Scholz, R. et al. Autoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular process. J Biol Chem 285, 25753-25766 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 25753-25766
    • Scholz, R.1
  • 18
    • 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
  • 19
    • 0034629146 scopus 로고    scopus 로고
    • TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop
    • Kishimoto, K., Matsumoto, K. & Ninomiya-Tsuji, J. TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop. J Biol Chem 275, 7359-7364 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 20
    • 15744392220 scopus 로고    scopus 로고
    • Prostaglandin E2 enhances osteoclastic differentiation of precursor cells through protein kinase A-dependent phosphorylation of TAK1
    • Kobayashi, Y. et al. Prostaglandin E2 enhances osteoclastic differentiation of precursor cells through protein kinase A-dependent phosphorylation of TAK1. J Biol Chem 280, 11395-11403 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 11395-11403
    • Kobayashi, Y.1
  • 21
    • 84906880166 scopus 로고    scopus 로고
    • TGF-beta-activated kinase 1 (TAK1) activation requires phosphorylation of serine 412 by protein kinase A catalytic subunit alpha (PKACalpha) and protein kinase X (PRKX)
    • Ouyang, C. et al. TGF-beta-activated kinase 1 (TAK1) Activation Requires Phosphorylation of Serine 412 by Protein Kinase A Catalytic Subunit alpha (PKACalpha) and Protein Kinase X (PRKX). J Biol Chem 289, 24226-24237 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 24226-24237
    • Ouyang, C.1
  • 22
    • 82755190610 scopus 로고    scopus 로고
    • Tripartite motif 8 (TRIM8) modulates TNFalpha- and IL-1beta-triggered NF-kappaB activation by targeting TAK1 for K63-linked polyubiquitination
    • Li, Q. et al. Tripartite motif 8 (TRIM8) modulates TNFalpha- and IL-1beta-triggered NF-kappaB activation by targeting TAK1 for K63-linked polyubiquitination. Proc Natl Acad Sci U S A 108, 19341-19346 (2011).
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 19341-19346
    • Li, Q.1
  • 23
    • 34250368115 scopus 로고    scopus 로고
    • Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase tak1 and prevents abnormal T cell responses
    • Reiley, W. W. et al. Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses. J Exp Med 204, 1475-1485 (2007).
    • (2007) J Exp Med , vol.204 , pp. 1475-1485
    • Reiley, W.W.1
  • 24
    • 80052691620 scopus 로고    scopus 로고
    • USP4 targets TAK1 to downregulate TNFalpha-induced NF-kappaB activation
    • Fan, Y. H. et al. USP4 targets TAK1 to downregulate TNFalpha-induced NF-kappaB activation. Cell Death Differ 18, 1547-1560 (2011).
    • (2011) Cell Death Differ , vol.18 , pp. 1547-1560
    • Fan, Y.H.1
  • 25
    • 77950367657 scopus 로고    scopus 로고
    • Two mechanistically and temporally distinct NF-kappaB activation pathways in IL-1 signaling
    • Yamazaki, K. et al. Two mechanistically and temporally distinct NF-kappaB activation pathways in IL-1 signaling. Sci Signal 2, ra66 (2009).
    • (2009) Sci Signal , vol.2 , pp. ra66
    • Yamazaki, K.1
  • 26
    • 79151482586 scopus 로고    scopus 로고
    • TAK1 lys-158 but not lys-209 is required for IL-1beta-induced lys63-linked TAK1 polyubiquitination and IKK/NF-kappaB activation
    • Fan, Y., Yu, Y., Mao, R., Zhang, H. & Yang, J. TAK1 Lys-158 but not Lys-209 is required for IL-1beta-induced Lys63-linked TAK1 polyubiquitination and IKK/NF-kappaB activation. Cell Signal 23, 660-665 (2011).
    • (2011) Cell Signal , vol.23 , pp. 660-665
    • Fan, Y.1    Yu, Y.2    Mao, R.3    Zhang, H.4    Yang, J.5
  • 27
    • 77957783934 scopus 로고    scopus 로고
    • TAK1 lysine 158 is required for TGF-beta-induced TRAF6-mediated smad-independent IKK/NF-kappaB and JNK/AP-1 activation
    • Mao, R. et al. TAK1 lysine 158 is required for TGF-beta-induced TRAF6-mediated Smad-independent IKK/NF-kappaB and JNK/AP-1 activation. Cell Signal 23, 222-227 (2011).
    • (2011) Cell Signal , vol.23 , pp. 222-227
    • Mao, R.1
  • 28
    • 77949316183 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation
    • Fan, Y. et al. Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor alpha- and interleukin-1beta-induced IKK/NF-kappaB and JNK/AP-1 activation. J Biol Chem 285, 5347-5360 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 5347-5360
    • Fan, Y.1
  • 29
    • 84882413848 scopus 로고    scopus 로고
    • Helicobacter pylori activates NF-kappaB by inducing ubc13-mediated ubiquitination of lysine 158 of TAK1
    • Lamb, A., Chen, J., Blanke, S. R. & Chen, L. F. Helicobacter pylori activates NF-kappaB by inducing Ubc13-mediated ubiquitination of lysine 158 of TAK1. J Cell Biochem 114, 2284-2292 (2013).
    • (2013) J Cell Biochem , vol.114 , pp. 2284-2292
    • Lamb, A.1    Chen, J.2    Blanke, S.R.3    Chen, L.F.4
  • 30
    • 53349164136 scopus 로고    scopus 로고
    • The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner
    • Sorrentino, A. et al. The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat Cell Biol 10, 1199-1207 (2008).
    • (2008) Nat Cell Biol , vol.10 , pp. 1199-1207
    • Sorrentino, A.1
  • 31
    • 84855292725 scopus 로고    scopus 로고
    • Polyubiquitination of transforming growth factor beta (TGFbeta)-associated kinase 1 mediates nuclear factorkappaB activation in response to different inflammatory stimuli
    • Hamidi, A. et al. Polyubiquitination of transforming growth factor beta (TGFbeta)-associated kinase 1 mediates nuclear factorkappaB activation in response to different inflammatory stimuli. J Biol Chem 287, 123-133 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 123-133
    • Hamidi, A.1
  • 32
    • 84859973888 scopus 로고    scopus 로고
    • Lys48-linked TAK1 polyubiquitination at lysine-72 downregulates TNFalpha-induced NF-kappaB activation via mediating TAK1 degradation
    • Fan, Y. et al. Lys48-linked TAK1 polyubiquitination at lysine-72 downregulates TNFalpha-induced NF-kappaB activation via mediating TAK1 degradation. Cell Signal 24, 1381-1389 (2012).
    • (2012) Cell Signal , vol.24 , pp. 1381-1389
    • Fan, Y.1
  • 33
    • 84867103151 scopus 로고    scopus 로고
    • Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues
    • Wagner, S. A. et al. Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Mol Cell Proteomics 11, 1578-1585 (2012).
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1578-1585
    • Wagner, S.A.1
  • 34
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • Adhikari, A., Xu, M. & Chen, Z. J. Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 26, 3214-3226 (2007).
    • (2007) Oncogene , vol.26 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 35
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • Hunter, T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell 28, 730-738 (2007).
    • (2007) Mol Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 36
    • 0034595826 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1
    • Sakurai, H., Miyoshi, H., Mizukami, J. & Sugita, T. Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1. FEBS Lett 474, 141-145 (2000).
    • (2000) FEBS Lett , vol.474 , pp. 141-145
    • Sakurai, H.1    Miyoshi, H.2    Mizukami, J.3    Sugita, T.4
  • 37
    • 0033103805 scopus 로고    scopus 로고
    • Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: Implications for joint and gut-associated immunopathologies
    • Kontoyiannis, D., Pasparakis, M., Pizarro, T. T., Cominelli, F. & Kollias, G. Impaired on/off regulation of TNF biosynthesis in mice lacking TNF AU-rich elements: implications for joint and gut-associated immunopathologies. Immunity 10, 387-398 (1999).
    • (1999) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 38
    • 0035794225 scopus 로고    scopus 로고
    • Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factoralpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts
    • Rutault, K., Hazzalin, C. A. & Mahadevan, L. C. Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factoralpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts. J Biol Chem 276, 6666-6674 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 6666-6674
    • Rutault, K.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 39
    • 69949154245 scopus 로고    scopus 로고
    • Zcchc11-dependent uridylation of microRNA directs cytokine expression
    • Jones, M. R. et al. Zcchc11-dependent uridylation of microRNA directs cytokine expression. Nat Cell Biol 11, 1157-1163 (2009).
    • (2009) Nat Cell Biol , vol.11 , pp. 1157-1163
    • Jones, M.R.1
  • 40
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated immune responses
    • Liew, F. Y., Xu, D., Brint, E. K. & O'Neill, L. A. Negative regulation of toll-like receptor-mediated immune responses. Nat Rev Immunol 5, 446-458 (2005).
    • (2005) Nat Rev Immunol , vol.5 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 41
    • 0036779446 scopus 로고    scopus 로고
    • Toll-like receptor signaling and regulation of cytokine gene expression in the immune system
    • 72 passim
    • Ozato, K., Tsujimura, H. & Tamura, T. Toll-like receptor signaling and regulation of cytokine gene expression in the immune system. Biotechniques Suppl, 66-68, 70, 72 passim (2002).
    • (2002) Biotechniques Suppl , vol.66-68 , pp. 70
    • Ozato, K.1    Tsujimura, H.2    Tamura, T.3
  • 42
    • 1542615083 scopus 로고    scopus 로고
    • P53 pathway in renal cell carcinoma is repressed by a dominant mechanism
    • Gurova, K. V., Hill, J. E., Razorenova, O. V., Chumakov, P. M. & Gudkov, A. V. p53 pathway in renal cell carcinoma is repressed by a dominant mechanism. Cancer Res 64, 1951-1958 (2004).
    • (2004) Cancer Res , vol.64 , pp. 1951-1958
    • Gurova, K.V.1    Hill, J.E.2    Razorenova, O.V.3    Chumakov, P.M.4    Gudkov, A.V.5
  • 43
    • 30544451546 scopus 로고    scopus 로고
    • Specificity in toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6
    • Hacker, H. et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 439, 204-207 (2006).
    • (2006) Nature , vol.439 , pp. 204-207
    • Hacker, H.1
  • 44
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H. & Freitas, M. A. MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9, 1548-1555 (2009).
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 45
    • 77954356041 scopus 로고    scopus 로고
    • Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry
    • Xu, H., Hsu, P. H., Zhang, L., Tsai, M. D. & Freitas, M. A. Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry. J Proteome Res 9, 3384-3393 (2010).
    • (2010) J Proteome Res , vol.9 , pp. 3384-3393
    • Xu, H.1    Hsu, P.H.2    Zhang, L.3    Tsai, M.D.4    Freitas, M.A.5


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