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Volumn 6, Issue 12, 2011, Pages

Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANISOMYCIN; CALYCULIN A; CYTOKINE; INTERLEUKIN 1; MITOGEN ACTIVATED PROTEIN KINASE P38; MUTANT PROTEIN; PHOSPHATASE; PROTEIN TAB1; RANTES; SERINE; SORBITOL; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; UNCLASSIFIED DRUG; PRIMER DNA; SIGNAL PEPTIDE; TAB1 PROTEIN, MAPKKK ACTIVATOR, VERTEBRATE;

EID: 84055207523     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029256     Document Type: Article
Times cited : (19)

References (54)
  • 1
    • 66749134594 scopus 로고    scopus 로고
    • Targeting innate immunity protein kinase signalling in inflammation
    • Gaestel M, Kotlyarov A, Kracht M, (2009) Targeting innate immunity protein kinase signalling in inflammation. Nat Rev Drug Discov 8: 480-499.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 480-499
    • Gaestel, M.1    Kotlyarov, A.2    Kracht, M.3
  • 2
    • 33746111852 scopus 로고    scopus 로고
    • The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function
    • Wan YY, Chi H, Xie M, Schneider MD, Flavell RA, (2006) The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function. Nat Immunol 7: 851-858.
    • (2006) Nat Immunol , vol.7 , pp. 851-858
    • Wan, Y.Y.1    Chi, H.2    Xie, M.3    Schneider, M.D.4    Flavell, R.A.5
  • 3
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase TAK1 in innate and adaptive immune responses
    • Sato S, Sanjo H, Takeda K, Ninomiya-Tsuji J, Yamamoto M, et al. (2005) Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol 6: 1087-1095.
    • (2005) Nat Immunol , vol.6 , pp. 1087-1095
    • Sato, S.1    Sanjo, H.2    Takeda, K.3    Ninomiya-Tsuji, J.4    Yamamoto, M.5
  • 4
    • 0036150184 scopus 로고    scopus 로고
    • Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6
    • Mizukami J, Takaesu G, Akatsuka H, Sakurai H, Ninomiya-Tsuji J, et al. (2002) Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6. Mol Cell Biol 22: 992-1000.
    • (2002) Mol Cell Biol , vol.22 , pp. 992-1000
    • Mizukami, J.1    Takaesu, G.2    Akatsuka, H.3    Sakurai, H.4    Ninomiya-Tsuji, J.5
  • 5
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, et al. (1999) The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature 398: 252-256.
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5
  • 6
    • 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, (2005) 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) J Biol Chem , vol.280 , pp. 7359-7368
    • Singhirunnusorn, P.1    Suzuki, S.2    Kawasaki, N.3    Saiki, I.4    Sakurai, H.5
  • 7
    • 0029940355 scopus 로고    scopus 로고
    • TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction
    • Shibuya H, Yamaguchi K, Shirakabe K, Tonegawa A, Gotoh Y, et al. (1996) TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction. Science 272: 1179-1182.
    • (1996) Science , vol.272 , pp. 1179-1182
    • Shibuya, H.1    Yamaguchi, K.2    Shirakabe, K.3    Tonegawa, A.4    Gotoh, Y.5
  • 8
    • 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, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, et al. (2000) 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) Mol Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5
  • 11
    • 0035793610 scopus 로고    scopus 로고
    • The MAPK kinase kinase TAK1 plays a central role in coupling the interleukin-1 receptor to both transcriptional and RNA-targeted mechanisms of gene regulation
    • Holtmann H, Enninga J, Kalble S, Thiefes A, Dorrie A, et al. (2001) The MAPK kinase kinase TAK1 plays a central role in coupling the interleukin-1 receptor to both transcriptional and RNA-targeted mechanisms of gene regulation. J Biol Chem 276: 3508-3516.
    • (2001) J Biol Chem , vol.276 , pp. 3508-3516
    • Holtmann, H.1    Enninga, J.2    Kalble, S.3    Thiefes, A.4    Dorrie, A.5
  • 12
    • 1542314841 scopus 로고    scopus 로고
    • TAB3, a new binding partner of the protein kinase TAK1
    • Cheung PC, Nebreda AR, Cohen P, (2004) TAB3, a new binding partner of the protein kinase TAK1. Biochem J 378: 27-34.
    • (2004) Biochem J , vol.378 , pp. 27-34
    • Cheung, P.C.1    Nebreda, A.R.2    Cohen, P.3
  • 13
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, et al. (2001) TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412: 346-351.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5
  • 14
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • Kanayama A, Seth RB, Sun L, Ea CK, Hong M, et al. (2004) TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol Cell 15: 535-548.
    • (2004) Mol Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.K.4    Hong, M.5
  • 15
    • 33747794347 scopus 로고    scopus 로고
    • The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway
    • Thiefes A, Wolf A, Doerrie A, Grassl GA, Matsumoto K, et al. (2006) The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep 7: 838-844.
    • (2006) EMBO Rep , vol.7 , pp. 838-844
    • Thiefes, A.1    Wolf, A.2    Doerrie, A.3    Grassl, G.A.4    Matsumoto, K.5
  • 16
    • 0036402140 scopus 로고    scopus 로고
    • TAK1-TAB1 fusion protein: a novel constitutively active mitogen-activated protein kinase kinase kinase that stimulates AP-1 and NF-kappaB signaling pathways
    • Sakurai H, Nishi A, Sato N, Mizukami J, Miyoshi H, et al. (2002) TAK1-TAB1 fusion protein: a novel constitutively active mitogen-activated protein kinase kinase kinase that stimulates AP-1 and NF-kappaB signaling pathways. Biochem Biophys Res Commun 297: 1277-1281.
    • (2002) Biochem Biophys Res Commun , vol.297 , pp. 1277-1281
    • Sakurai, H.1    Nishi, A.2    Sato, N.3    Mizukami, J.4    Miyoshi, H.5
  • 17
    • 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, (2000) Phosphorylation-dependent activation of TAK1 mitogen-activated protein kinase kinase kinase by TAB1. FEBS Lett 474: 141-145.
    • (2000) FEBS Lett , vol.474 , pp. 141-145
    • Sakurai, H.1    Miyoshi, H.2    Mizukami, J.3    Sugita, T.4
  • 18
    • 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, (2000) TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop. J Biol Chem 275: 7359-7364.
    • (2000) J Biol Chem , vol.275 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 19
    • 0035968214 scopus 로고    scopus 로고
    • An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK
    • Ono K, Ohtomo T, Sato S, Sugamata Y, Suzuki M, et al. (2001) An evolutionarily conserved motif in the TAB1 C-terminal region is necessary for interaction with and activation of TAK1 MAPKKK. J Biol Chem 276: 24396-24400.
    • (2001) J Biol Chem , vol.276 , pp. 24396-24400
    • Ono, K.1    Ohtomo, T.2    Sato, S.3    Sugamata, Y.4    Suzuki, M.5
  • 20
    • 0242473165 scopus 로고    scopus 로고
    • Feedback control of the protein kinase TAK1 by SAPK2a/p38alpha
    • Cheung PC, Campbell DG, Nebreda AR, Cohen P, (2003) Feedback control of the protein kinase TAK1 by SAPK2a/p38alpha. EMBO J 22: 5793-5805.
    • (2003) EMBO J , vol.22 , pp. 5793-5805
    • Cheung, P.C.1    Campbell, D.G.2    Nebreda, A.R.3    Cohen, P.4
  • 21
    • 0037462658 scopus 로고    scopus 로고
    • TAB1beta (transforming growth factor-beta-activated protein kinase 1-binding protein 1beta), a novel splicing variant of TAB1 that interacts with p38alpha but not TAK1
    • Ge B, Xiong X, Jing Q, Mosley JL, Filose A, et al. (2003) TAB1beta (transforming growth factor-beta-activated protein kinase 1-binding protein 1beta), a novel splicing variant of TAB1 that interacts with p38alpha but not TAK1. J Biol Chem 278: 2286-2293.
    • (2003) J Biol Chem , vol.278 , pp. 2286-2293
    • Ge, B.1    Xiong, X.2    Jing, Q.3    Mosley, J.L.4    Filose, A.5
  • 22
    • 33646576174 scopus 로고    scopus 로고
    • Determinants that control the specific interactions between TAB1 and p38alpha
    • Zhou H, Zheng M, Chen J, Xie C, Kolatkar AR, et al. (2006) Determinants that control the specific interactions between TAB1 and p38alpha. Mol Cell Biol 26: 3824-3834.
    • (2006) Mol Cell Biol , vol.26 , pp. 3824-3834
    • Zhou, H.1    Zheng, M.2    Chen, J.3    Xie, C.4    Kolatkar, A.R.5
  • 23
    • 33748743740 scopus 로고    scopus 로고
    • Multiple activation mechanisms of p38alpha mitogen-activated protein kinase
    • Kang YJ, Seit-Nebi A, Davis RJ, Han J, (2006) Multiple activation mechanisms of p38alpha mitogen-activated protein kinase. J Biol Chem 281: 26225-26234.
    • (2006) J Biol Chem , vol.281 , pp. 26225-26234
    • Kang, Y.J.1    Seit-Nebi, A.2    Davis, R.J.3    Han, J.4
  • 24
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha
    • Ge B, Gram H, Di Padova F, Huang B, New L, et al. (2002) MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha. Science 295: 1291-1294.
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1    Gram, H.2    Di Padova, F.3    Huang, B.4    New, L.5
  • 26
    • 38949115893 scopus 로고    scopus 로고
    • Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex
    • Mendoza H, Campbell DG, Burness K, Hastie J, Ronkina N, et al. (2008) Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex. Biochem J 409: 711-722.
    • (2008) Biochem J , vol.409 , pp. 711-722
    • Mendoza, H.1    Campbell, D.G.2    Burness, K.3    Hastie, J.4    Ronkina, N.5
  • 27
    • 0035937111 scopus 로고    scopus 로고
    • Regulation of the TAK1 signaling pathway by protein phosphatase 2C
    • Hanada M, Ninomiya-Tsuji J, Komaki K, Ohnishi M, Katsura K, et al. (2001) Regulation of the TAK1 signaling pathway by protein phosphatase 2C. J Biol Chem 276: 5753-5759.
    • (2001) J Biol Chem , vol.276 , pp. 5753-5759
    • Hanada, M.1    Ninomiya-Tsuji, J.2    Komaki, K.3    Ohnishi, M.4    Katsura, K.5
  • 28
    • 33845994781 scopus 로고    scopus 로고
    • Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway
    • Kajino T, Ren H, Iemura S, Natsume T, Stefansson B, et al. (2006) Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway. J Biol Chem 281: 39891-39896.
    • (2006) J Biol Chem , vol.281 , pp. 39891-39896
    • Kajino, T.1    Ren, H.2    Iemura, S.3    Natsume, T.4    Stefansson, B.5
  • 29
    • 59649116320 scopus 로고    scopus 로고
    • Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point
    • Liu Q, Busby JC, Molkentin JD, (2009) Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point. Nat Cell Biol 11: 154-161.
    • (2009) Nat Cell Biol , vol.11 , pp. 154-161
    • Liu, Q.1    Busby, J.C.2    Molkentin, J.D.3
  • 30
    • 33746215065 scopus 로고    scopus 로고
    • Small interfering RNAs generated by recombinant dicer induce inflammatory gene expression independent from the TAK1-NFkappaB-MAPK signaling pathways
    • Kettner-Buhrow D, Dittrich-Breiholz O, Schneider H, Wolter S, Resch K, et al. (2006) Small interfering RNAs generated by recombinant dicer induce inflammatory gene expression independent from the TAK1-NFkappaB-MAPK signaling pathways. Biochem Biophys Res Commun 347: 566-573.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 566-573
    • Kettner-Buhrow, D.1    Dittrich-Breiholz, O.2    Schneider, H.3    Wolter, S.4    Resch, K.5
  • 31
    • 0037422858 scopus 로고    scopus 로고
    • TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway
    • Takaesu G, Surabhi RM, Park KJ, Ninomiya-Tsuji J, Matsumoto K, et al. (2003) TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway. J Mol Biol 326: 105-115.
    • (2003) J Mol Biol , vol.326 , pp. 105-115
    • Takaesu, G.1    Surabhi, R.M.2    Park, K.J.3    Ninomiya-Tsuji, J.4    Matsumoto, K.5
  • 32
    • 33745851830 scopus 로고    scopus 로고
    • TAK1 is a master regulator of epidermal homeostasis involving skin inflammation and apoptosis
    • Omori E, Matsumoto K, Sanjo H, Sato S, Akira S, et al. (2006) TAK1 is a master regulator of epidermal homeostasis involving skin inflammation and apoptosis. J Biol Chem 281: 19610-19617.
    • (2006) J Biol Chem , vol.281 , pp. 19610-19617
    • Omori, E.1    Matsumoto, K.2    Sanjo, H.3    Sato, S.4    Akira, S.5
  • 33
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim JH, Xiao C, Paschal AE, Bailey ST, Rao P, et al. (2005) TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 19: 2668-2681.
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1    Xiao, C.2    Paschal, A.E.3    Bailey, S.T.4    Rao, P.5
  • 34
    • 57749122042 scopus 로고    scopus 로고
    • TAK1-binding protein 1, TAB1, mediates osmotic stress-induced TAK1 activation but is dispensable for TAK1-mediated cytokine signaling
    • Inagaki M, Omori E, Kim JY, Komatsu Y, Scott G, et al. (2008) TAK1-binding protein 1, TAB1, mediates osmotic stress-induced TAK1 activation but is dispensable for TAK1-mediated cytokine signaling. J Biol Chem 283: 33080-33086.
    • (2008) J Biol Chem , vol.283 , pp. 33080-33086
    • Inagaki, M.1    Omori, E.2    Kim, J.Y.3    Komatsu, Y.4    Scott, G.5
  • 35
    • 0037809234 scopus 로고    scopus 로고
    • Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon)
    • Li MG, Katsura K, Nomiyama H, Komaki K, Ninomiya-Tsuji J, et al. (2003) Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). J Biol Chem 278: 12013-12021.
    • (2003) J Biol Chem , vol.278 , pp. 12013-12021
    • Li, M.G.1    Katsura, K.2    Nomiyama, H.3    Komaki, K.4    Ninomiya-Tsuji, J.5
  • 36
    • 62449265216 scopus 로고    scopus 로고
    • The PP2C Alphabet Is a Negative Regulator of Stress-Activated Protein Kinase Signaling in Drosophila
    • Baril C, Sahmi M, Ashton-Beaucage D, Stronach B, Therrien M, (2009) The PP2C Alphabet Is a Negative Regulator of Stress-Activated Protein Kinase Signaling in Drosophila. Genetics 181: 567-579.
    • (2009) Genetics , vol.181 , pp. 567-579
    • Baril, C.1    Sahmi, M.2    Ashton-Beaucage, D.3    Stronach, B.4    Therrien, M.5
  • 37
    • 33646829136 scopus 로고    scopus 로고
    • TAB-1 modulates intracellular localization of p38 MAP kinase and downstream signaling
    • Lu G, Kang YJ, Han J, Herschman HR, Stefani E, et al. (2006) TAB-1 modulates intracellular localization of p38 MAP kinase and downstream signaling. J Biol Chem 281: 6087-6095.
    • (2006) J Biol Chem , vol.281 , pp. 6087-6095
    • Lu, G.1    Kang, Y.J.2    Han, J.3    Herschman, H.R.4    Stefani, E.5
  • 38
    • 64849108653 scopus 로고    scopus 로고
    • p38 is Active in vitro and in vivo when Monophosphorylated on Thr180
    • Askari N, Beenstock J, Livnah O, Engelberg D, (2009) p38 is Active in vitro and in vivo when Monophosphorylated on Thr180. Biochemistry 48: 2497-2504.
    • (2009) Biochemistry , vol.48 , pp. 2497-2504
    • Askari, N.1    Beenstock, J.2    Livnah, O.3    Engelberg, D.4
  • 39
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • Ben Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ, (1998) Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr Biol 8: 1049-1057.
    • (1998) Curr Biol , vol.8 , pp. 1049-1057
    • Ben Levy, R.1    Hooper, S.2    Wilson, R.3    Paterson, H.F.4    Marshall, C.J.5
  • 40
    • 33846370205 scopus 로고    scopus 로고
    • TAB1 modulates IL-1alpha mediated cytokine secretion but is dispensable for TAK1 activation
    • Bertelsen M, Sanfridson A, (2007) TAB1 modulates IL-1alpha mediated cytokine secretion but is dispensable for TAK1 activation. Cell Signal 19: 646-657.
    • (2007) Cell Signal , vol.19 , pp. 646-657
    • Bertelsen, M.1    Sanfridson, A.2
  • 41
    • 0036893097 scopus 로고    scopus 로고
    • Regulation of RANTES promoter activation in alveolar epithelial cells after cytokine stimulation
    • 10.1152/ajplung.00162.2002 [doi];00162.2002 [pii]
    • Casola A, Henderson A, Liu T, Garofalo RP, Brasier AR, (2002) Regulation of RANTES promoter activation in alveolar epithelial cells after cytokine stimulation. Am J Physiol Lung Cell Mol Physiol 283: L1280-L1290 10.1152/ajplung.00162.2002 [doi];00162.2002 [pii].
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.283
    • Casola, A.1    Henderson, A.2    Liu, T.3    Garofalo, R.P.4    Brasier, A.R.5
  • 43
    • 38949115893 scopus 로고    scopus 로고
    • Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex
    • Mendoza H, Campbell DG, Burness K, Hastie J, Ronkina N, et al. (2008) Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex. Biochem J 409: 711-722.
    • (2008) Biochem J , vol.409 , pp. 711-722
    • Mendoza, H.1    Campbell, D.G.2    Burness, K.3    Hastie, J.4    Ronkina, N.5
  • 44
    • 0032526988 scopus 로고    scopus 로고
    • Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation
    • Engel K, Kotlyarov A, Gaestel M, (1998) Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J 17: 3363-3371.
    • (1998) EMBO J , vol.17 , pp. 3363-3371
    • Engel, K.1    Kotlyarov, A.2    Gaestel, M.3
  • 45
    • 34249799878 scopus 로고    scopus 로고
    • XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization
    • Lu M, Lin SC, Huang Y, Kang YJ, Rich R, et al. (2007) XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization. Mol Cell 26: 689-702.
    • (2007) Mol Cell , vol.26 , pp. 689-702
    • Lu, M.1    Lin, S.C.2    Huang, Y.3    Kang, Y.J.4    Rich, R.5
  • 46
    • 28144449928 scopus 로고    scopus 로고
    • Structural basis for the interaction of TAK1 kinase with its activating protein TAB1
    • Brown K, Vial SC, Dedi N, Long JM, Dunster NJ, et al. (2005) Structural basis for the interaction of TAK1 kinase with its activating protein TAB1. J Mol Biol 354: 1013-1020.
    • (2005) J Mol Biol , vol.354 , pp. 1013-1020
    • Brown, K.1    Vial, S.C.2    Dedi, N.3    Long, J.M.4    Dunster, N.J.5
  • 47
    • 0032585625 scopus 로고    scopus 로고
    • Nuclear import: a tale of two sites
    • Dingwall C, Laskey RA, (1998) Nuclear import: a tale of two sites. Curr Biol 8: R922-R924.
    • (1998) Curr Biol , vol.8
    • Dingwall, C.1    Laskey, R.A.2
  • 48
    • 52049108218 scopus 로고    scopus 로고
    • Identification and characterization of a general nuclear translocation signal in signaling proteins
    • Chuderland D, Konson A, Seger R, (2008) Identification and characterization of a general nuclear translocation signal in signaling proteins. Mol Cell 31: 850-861.
    • (2008) Mol Cell , vol.31 , pp. 850-861
    • Chuderland, D.1    Konson, A.2    Seger, R.3
  • 49
    • 23044483249 scopus 로고    scopus 로고
    • Simultaneous blockade of NFkappaB, JNK, and p38 MAPK by a kinase-inactive mutant of the protein kinase TAK1 sensitizes cells to apoptosis and affects a distinct spectrum of tumor necrosis target genes
    • Thiefes A, Wolter S, Mushinski JF, Hoffmann E, Dittrich-Breiholz O, et al. (2005) Simultaneous blockade of NFkappaB, JNK, and p38 MAPK by a kinase-inactive mutant of the protein kinase TAK1 sensitizes cells to apoptosis and affects a distinct spectrum of tumor necrosis target genes. J Biol Chem 280: 27728-27741.
    • (2005) J Biol Chem , vol.280 , pp. 27728-27741
    • Thiefes, A.1    Wolter, S.2    Mushinski, J.F.3    Hoffmann, E.4    Dittrich-Breiholz, O.5
  • 50
    • 0032823313 scopus 로고    scopus 로고
    • Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways
    • Holtmann H, Winzen R, Holland P, Eickemeier S, Hoffmann E, et al. (1999) Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways. Mol Cell Biol 19: 6742-6753.
    • (1999) Mol Cell Biol , vol.19 , pp. 6742-6753
    • Holtmann, H.1    Winzen, R.2    Holland, P.3    Eickemeier, S.4    Hoffmann, E.5
  • 51
    • 0033568608 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism
    • Winzen R, Kracht M, Ritter B, Wilhelm A, Chen CY, et al. (1999) The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism. EMBO J 18: 4969-4980.
    • (1999) EMBO J , vol.18 , pp. 4969-4980
    • Winzen, R.1    Kracht, M.2    Ritter, B.3    Wilhelm, A.4    Chen, C.Y.5
  • 52
    • 0033729426 scopus 로고    scopus 로고
    • Generation of deletion and point mutations with one primer in a single cloning step
    • Makarova O, Kamberov E, Margolis B, (2000) Generation of deletion and point mutations with one primer in a single cloning step. Biotechniques 29: 970-972.
    • (2000) Biotechniques , vol.29 , pp. 970-972
    • Makarova, O.1    Kamberov, E.2    Margolis, B.3
  • 53
    • 15744393216 scopus 로고    scopus 로고
    • MEK1-dependent delayed expression of Fos-related antigen-1 counteracts c-Fos and p65 NF-kappaB-mediated interleukin-8 transcription in response to cytokines or growth factors
    • Hoffmann E, Thiefes A, Buhrow D, Dittrich-Breiholz O, Schneider H, et al. (2005) MEK1-dependent delayed expression of Fos-related antigen-1 counteracts c-Fos and p65 NF-kappaB-mediated interleukin-8 transcription in response to cytokines or growth factors. J Biol Chem 280: 9706-9718.
    • (2005) J Biol Chem , vol.280 , pp. 9706-9718
    • Hoffmann, E.1    Thiefes, A.2    Buhrow, D.3    Dittrich-Breiholz, O.4    Schneider, H.5


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