메뉴 건너뛰기




Volumn 8, Issue 9, 2012, Pages

The p38/MK2-Driven Exchange between Tristetraprolin and HuR Regulates AU-Rich Element-Dependent Translation

Author keywords

[No Author keywords available]

Indexed keywords

HUR PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR;

EID: 84866951611     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002977     Document Type: Article
Times cited : (180)

References (77)
  • 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
    • 0024281428 scopus 로고
    • A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF
    • Kriegler M, Perez C, DeFay K, Albert I, Lu SD, (1988) A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell 53: 45-53.
    • (1988) Cell , vol.53 , pp. 45-53
    • Kriegler, M.1    Perez, C.2    DeFay, K.3    Albert, I.4    Lu, S.D.5
  • 3
    • 0028862973 scopus 로고
    • Human pro-tumor necrosis factor: molecular determinants of membrane translocation, sorting, and maturation
    • Utsumi T, Akimaru K, Kawabata Z, Levitan A, Tokunaga T, et al. (1995) Human pro-tumor necrosis factor: molecular determinants of membrane translocation, sorting, and maturation. Mol Cell Biol 15: 6398-6405.
    • (1995) Mol Cell Biol , vol.15 , pp. 6398-6405
    • Utsumi, T.1    Akimaru, K.2    Kawabata, Z.3    Levitan, A.4    Tokunaga, T.5
  • 4
    • 42149168460 scopus 로고    scopus 로고
    • A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo
    • Lieu ZZ, Lock JG, Hammond LA, La Gruta NL, Stow JL, et al. (2008) A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo. Proc Natl Acad Sci U S A 105: 3351-3356.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3351-3356
    • Lieu, Z.Z.1    Lock, J.G.2    Hammond, L.A.3    La Gruta, N.L.4    Stow, J.L.5
  • 5
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, et al. (1997) Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385: 733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5
  • 6
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases - MKs - two's company, three's a crowd
    • Gaestel M, (2006) MAPKAP kinases- MKs- two's company, three's a crowd. Nat Rev Mol Cell Biol 7: 120-130.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 120-130
    • Gaestel, M.1
  • 7
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee JC, Laydon JT, McDonnell PC, Gallagher TF, Kumar S, et al. (1994) A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 372: 739-746.
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1    Laydon, J.T.2    McDonnell, P.C.3    Gallagher, T.F.4    Kumar, S.5
  • 9
    • 0036479125 scopus 로고    scopus 로고
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels
    • Neininger A, Kontoyiannis D, Kotlyarov A, Winzen R, Eckert R, et al. (2002) MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels. J Biol Chem 277: 3065-3068.
    • (2002) J Biol Chem , vol.277 , pp. 3065-3068
    • Neininger, A.1    Kontoyiannis, D.2    Kotlyarov, A.3    Winzen, R.4    Eckert, R.5
  • 10
    • 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 TT, Cominelli F, Kollias G, (1999) 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) Immunity , vol.10 , pp. 387-398
    • Kontoyiannis, D.1    Pasparakis, M.2    Pizarro, T.T.3    Cominelli, F.4    Kollias, G.5
  • 11
    • 1642332899 scopus 로고    scopus 로고
    • MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding
    • Chrestensen CA, Schroeder MJ, Shabanowitz J, Hunt DF, Pelo JW, et al. (2004) MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding. J Biol Chem 279: 10176-10184.
    • (2004) J Biol Chem , vol.279 , pp. 10176-10184
    • Chrestensen, C.A.1    Schroeder, M.J.2    Shabanowitz, J.3    Hunt, D.F.4    Pelo, J.W.5
  • 12
    • 0037011121 scopus 로고    scopus 로고
    • Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs
    • Rousseau S, Morrice N, Peggie M, Campbell DG, Gaestel M, et al. (2002) Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs. Embo J 21: 6505-6514.
    • (2002) Embo J , vol.21 , pp. 6505-6514
    • Rousseau, S.1    Morrice, N.2    Peggie, M.3    Campbell, D.G.4    Gaestel, M.5
  • 13
    • 29144491811 scopus 로고    scopus 로고
    • p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts
    • Briata P, Forcales SV, Ponassi M, Corte G, Chen CY, et al. (2005) p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts. Mol Cell 20: 891-903.
    • (2005) Mol Cell , vol.20 , pp. 891-903
    • Briata, P.1    Forcales, S.V.2    Ponassi, M.3    Corte, G.4    Chen, C.Y.5
  • 14
    • 0037436229 scopus 로고    scopus 로고
    • Affinity purification of ARE-binding proteins identifies poly(A)-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization
    • Bollig F, Winzen R, Gaestel M, Kostka S, Resch K, et al. (2003) Affinity purification of ARE-binding proteins identifies poly(A)-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization. Biochem Biophys Res Commun 301: 665-670.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 665-670
    • Bollig, F.1    Winzen, R.2    Gaestel, M.3    Kostka, S.4    Resch, K.5
  • 15
    • 1942471656 scopus 로고    scopus 로고
    • MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay
    • Stoecklin G, Stubbs T, Kedersha N, Wax S, Rigby WF, et al. (2004) MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. Embo J 23: 1313-1324.
    • (2004) Embo J , vol.23 , pp. 1313-1324
    • Stoecklin, G.1    Stubbs, T.2    Kedersha, N.3    Wax, S.4    Rigby, W.F.5
  • 16
    • 40949102111 scopus 로고    scopus 로고
    • Post-transcriptional control of cytokine production
    • Anderson P, (2008) Post-transcriptional control of cytokine production. Nat Immunol 9: 353-359.
    • (2008) Nat Immunol , vol.9 , pp. 353-359
    • Anderson, P.1
  • 17
    • 78751504841 scopus 로고    scopus 로고
    • Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment
    • Clement SL, Scheckel C, Stoecklin G, Lykke-Andersen J, (2011) Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol Cell Biol 31: 256-266.
    • (2011) Mol Cell Biol , vol.31 , pp. 256-266
    • Clement, S.L.1    Scheckel, C.2    Stoecklin, G.3    Lykke-Andersen, J.4
  • 18
    • 79960928455 scopus 로고    scopus 로고
    • Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin
    • Sandler H, Kreth J, Timmers HT, Stoecklin G, (2011) Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin. Nucleic Acids Res 39: 4373-4386.
    • (2011) Nucleic Acids Res , vol.39 , pp. 4373-4386
    • Sandler, H.1    Kreth, J.2    Timmers, H.T.3    Stoecklin, G.4
  • 19
    • 77956261147 scopus 로고    scopus 로고
    • MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment
    • Marchese FP, Aubareda A, Tudor C, Saklatvala J, Clark AR, et al. (2010) MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment. J Biol Chem 285: 27590-27600.
    • (2010) J Biol Chem , vol.285 , pp. 27590-27600
    • Marchese, F.P.1    Aubareda, A.2    Tudor, C.3    Saklatvala, J.4    Clark, A.R.5
  • 20
    • 0033555659 scopus 로고    scopus 로고
    • ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system
    • Ford LP, Watson J, Keene JD, Wilusz J, (1999) ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system. Genes Dev 13: 188-201.
    • (1999) Genes Dev , vol.13 , pp. 188-201
    • Ford, L.P.1    Watson, J.2    Keene, J.D.3    Wilusz, J.4
  • 21
    • 79960904961 scopus 로고    scopus 로고
    • UneCLIPsing HuR nuclear function
    • Srikantan S, Gorospe M, (2011) UneCLIPsing HuR nuclear function. Mol Cell 43: 319-321.
    • (2011) Mol Cell , vol.43 , pp. 319-321
    • Srikantan, S.1    Gorospe, M.2
  • 22
    • 0032985448 scopus 로고    scopus 로고
    • Binding of neuronal ELAV-like proteins to the uridine-rich sequence in the 3′-untranslated region of tumor necrosis factor-alpha messenger RNA
    • Sakai K, Kitagawa Y, Hirose G, (1999) Binding of neuronal ELAV-like proteins to the uridine-rich sequence in the 3′-untranslated region of tumor necrosis factor-alpha messenger RNA. FEBS Lett 446: 157-162.
    • (1999) FEBS Lett , vol.446 , pp. 157-162
    • Sakai, K.1    Kitagawa, Y.2    Hirose, G.3
  • 23
    • 0034746363 scopus 로고    scopus 로고
    • The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR
    • Dean JL, Wait R, Mahtani KR, Sully G, Clark AR, et al. (2001) The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR. Mol Cell Biol 21: 721-730.
    • (2001) Mol Cell Biol , vol.21 , pp. 721-730
    • Dean, J.L.1    Wait, R.2    Mahtani, K.R.3    Sully, G.4    Clark, A.R.5
  • 25
    • 33645824941 scopus 로고    scopus 로고
    • Translational control of cytochrome c by RNA-binding proteins TIA-1 and HuR
    • Kawai T, Lal A, Yang X, Galban S, Mazan-Mamczarz K, et al. (2006) Translational control of cytochrome c by RNA-binding proteins TIA-1 and HuR. Mol Cell Biol 26: 3295-3307.
    • (2006) Mol Cell Biol , vol.26 , pp. 3295-3307
    • Kawai, T.1    Lal, A.2    Yang, X.3    Galban, S.4    Mazan-Mamczarz, K.5
  • 26
    • 84855465218 scopus 로고    scopus 로고
    • Myeloid cell expression of the RNA-binding protein HuR protects mice from pathologic inflammation and colorectal carcinogenesis
    • Yiakouvaki A, Dimitriou M, Karakasiliotis I, Eftychi C, Theocharis S, et al. (2012) Myeloid cell expression of the RNA-binding protein HuR protects mice from pathologic inflammation and colorectal carcinogenesis. J Clin Invest 122: 48-61.
    • (2012) J Clin Invest , vol.122 , pp. 48-61
    • Yiakouvaki, A.1    Dimitriou, M.2    Karakasiliotis, I.3    Eftychi, C.4    Theocharis, S.5
  • 28
    • 16044369031 scopus 로고    scopus 로고
    • A pathogenetic role for TNF alpha in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency
    • Taylor GA, Carballo E, Lee DM, Lai WS, Thompson MJ, et al. (1996) A pathogenetic role for TNF alpha in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency. Immunity 4: 445-454.
    • (1996) Immunity , vol.4 , pp. 445-454
    • Taylor, G.A.1    Carballo, E.2    Lee, D.M.3    Lai, W.S.4    Thompson, M.J.5
  • 29
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E, Lai WS, Blackshear PJ, (1998) Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 281: 1001-1005.
    • (1998) Science , vol.281 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 30
    • 33644753147 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element
    • Hitti E, Iakovleva T, Brook M, Deppenmeier S, Gruber AD, et al. (2006) Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. Mol Cell Biol 26: 2399-2407.
    • (2006) Mol Cell Biol , vol.26 , pp. 2399-2407
    • Hitti, E.1    Iakovleva, T.2    Brook, M.3    Deppenmeier, S.4    Gruber, A.D.5
  • 31
    • 79954585486 scopus 로고    scopus 로고
    • Stress induced gene expression: a direct role for MAPKAP kinases in transcriptional activation of immediate early genes
    • Ronkina N, Menon MB, Schwermann J, Arthur JS, Legault H, et al. (2011) Stress induced gene expression: a direct role for MAPKAP kinases in transcriptional activation of immediate early genes. Nucleic Acids Res 39: 2503-2518.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2503-2518
    • Ronkina, N.1    Menon, M.B.2    Schwermann, J.3    Arthur, J.S.4    Legault, H.5
  • 32
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • Ronkina N, Kotlyarov A, Dittrich-Breiholz O, Kracht M, Hitti E, et al. (2007) The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK. Mol Cell Biol 27: 170-181.
    • (2007) Mol Cell Biol , vol.27 , pp. 170-181
    • Ronkina, N.1    Kotlyarov, A.2    Dittrich-Breiholz, O.3    Kracht, M.4    Hitti, E.5
  • 34
    • 43549083894 scopus 로고    scopus 로고
    • MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-relevance in a mouse model of Parkinson's disease
    • Thomas T, Timmer M, Cesnulevicius K, Hitti E, Kotlyarov A, et al. (2008) MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-relevance in a mouse model of Parkinson's disease. J Neurochem 105: 2039-2052.
    • (2008) J Neurochem , vol.105 , pp. 2039-2052
    • Thomas, T.1    Timmer, M.2    Cesnulevicius, K.3    Hitti, E.4    Kotlyarov, A.5
  • 36
    • 0041832111 scopus 로고    scopus 로고
    • Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes
    • Lerner RS, Seiser RM, Zheng T, Lager PJ, Reedy MC, et al. (2003) Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes. RNA 9: 1123-1137.
    • (2003) RNA , vol.9 , pp. 1123-1137
    • Lerner, R.S.1    Seiser, R.M.2    Zheng, T.3    Lager, P.J.4    Reedy, M.C.5
  • 37
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
    • Pyhtila B, Zheng T, Lager PJ, Keene JD, Reedy MC, et al. (2008) Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum. RNA 14: 445-453.
    • (2008) RNA , vol.14 , pp. 445-453
    • Pyhtila, B.1    Zheng, T.2    Lager, P.J.3    Keene, J.D.4    Reedy, M.C.5
  • 38
    • 84857253794 scopus 로고    scopus 로고
    • Primary role for endoplasmic reticulum-bound ribosomes in cellular translation identified by ribosome profiling
    • Reid DW, Nicchitta CV, (2012) Primary role for endoplasmic reticulum-bound ribosomes in cellular translation identified by ribosome profiling. J Biol Chem 287: 5518-5527.
    • (2012) J Biol Chem , vol.287 , pp. 5518-5527
    • Reid, D.W.1    Nicchitta, C.V.2
  • 39
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M, Clifton AD, Lucocq LM, Alessi DR, (1998) Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. Embo J 17: 4426-4441.
    • (1998) Embo J , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 40
    • 0034254553 scopus 로고    scopus 로고
    • TIA-1 is a translational silencer that selectively regulates the expression of TNF-alpha
    • Piecyk M, Wax S, Beck AR, Kedersha N, Gupta M, et al. (2000) TIA-1 is a translational silencer that selectively regulates the expression of TNF-alpha. Embo J 19: 4154-4163.
    • (2000) Embo J , vol.19 , pp. 4154-4163
    • Piecyk, M.1    Wax, S.2    Beck, A.R.3    Kedersha, N.4    Gupta, M.5
  • 41
    • 20044388720 scopus 로고    scopus 로고
    • Involvement of microRNA in AU-rich element-mediated mRNA instability
    • Jing Q, Huang S, Guth S, Zarubin T, Motoyama A, et al. (2005) Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell 120: 623-634.
    • (2005) Cell , vol.120 , pp. 623-634
    • Jing, Q.1    Huang, S.2    Guth, S.3    Zarubin, T.4    Motoyama, A.5
  • 42
    • 36749026906 scopus 로고    scopus 로고
    • Switching from repression to activation: microRNAs can up-regulate translation
    • Vasudevan S, Tong Y, Steitz JA, (2007) Switching from repression to activation: microRNAs can up-regulate translation. Science 318: 1931-1934.
    • (2007) Science , vol.318 , pp. 1931-1934
    • Vasudevan, S.1    Tong, Y.2    Steitz, J.A.3
  • 43
    • 33947262696 scopus 로고    scopus 로고
    • AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2
    • Vasudevan S, Steitz JA, (2007) AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2. Cell 128: 1105-1118.
    • (2007) Cell , vol.128 , pp. 1105-1118
    • Vasudevan, S.1    Steitz, J.A.2
  • 44
    • 48249114811 scopus 로고    scopus 로고
    • Phosphorylation of Argonaute 2 at serine-387 facilitates its localization to processing bodies
    • Zeng Y, Sankala H, Zhang X, Graves PR, (2008) Phosphorylation of Argonaute 2 at serine-387 facilitates its localization to processing bodies. Biochem J 413: 429-436.
    • (2008) Biochem J , vol.413 , pp. 429-436
    • Zeng, Y.1    Sankala, H.2    Zhang, X.3    Graves, P.R.4
  • 45
    • 32944473015 scopus 로고    scopus 로고
    • Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis
    • Cao H, Deterding LJ, Venable JD, Kennington EA, Yates JR 3rd, et al. (2006) Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis. Biochem J 394: 285-297.
    • (2006) Biochem J , vol.394 , pp. 285-297
    • Cao, H.1    Deterding, L.J.2    Venable, J.D.3    Kennington, E.A.4    Yates III, J.R.5
  • 46
    • 1242337338 scopus 로고    scopus 로고
    • Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1)
    • Sully G, Dean JLE, Wait R, Rawlinson L, Santalucia T, et al. (2004) Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1). Biochem J 377: 629-639.
    • (2004) Biochem J , vol.377 , pp. 629-639
    • Sully, G.1    Dean, J.L.E.2    Wait, R.3    Rawlinson, L.4    Santalucia, T.5
  • 47
    • 68949161769 scopus 로고    scopus 로고
    • p38 Mitogen-activated protein kinase- and HuR-dependent stabilization of p21(Cip1) mRNA mediates the G(1)/S checkpoint
    • Lafarga V, Cuadrado A, Lopez de Silanes I, Bengoechea R, Fernandez-Capetillo O, et al. (2009) p38 Mitogen-activated protein kinase- and HuR-dependent stabilization of p21(Cip1) mRNA mediates the G(1)/S checkpoint. Mol Cell Biol 29: 4341-4351.
    • (2009) Mol Cell Biol , vol.29 , pp. 4341-4351
    • Lafarga, V.1    Cuadrado, A.2    Lopez de Silanes, I.3    Bengoechea, R.4    Fernandez-Capetillo, O.5
  • 50
    • 34547235597 scopus 로고    scopus 로고
    • The RNA-binding protein HuR promotes cell migration and cell invasion by stabilizing the beta-actin mRNA in a U-rich-element-dependent manner
    • Dormoy-Raclet V, Menard I, Clair E, Kurban G, Mazroui R, et al. (2007) The RNA-binding protein HuR promotes cell migration and cell invasion by stabilizing the beta-actin mRNA in a U-rich-element-dependent manner. Mol Cell Biol 27: 5365-5380.
    • (2007) Mol Cell Biol , vol.27 , pp. 5365-5380
    • Dormoy-Raclet, V.1    Menard, I.2    Clair, E.3    Kurban, G.4    Mazroui, R.5
  • 51
    • 3543003469 scopus 로고    scopus 로고
    • The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself
    • Tchen CR, Brook M, Saklatvala J, Clark AR, (2004) The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself. J Biol Chem 279: 32393-32400.
    • (2004) J Biol Chem , vol.279 , pp. 32393-32400
    • Tchen, C.R.1    Brook, M.2    Saklatvala, J.3    Clark, A.R.4
  • 52
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG, (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136: 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 53
    • 13244298460 scopus 로고    scopus 로고
    • Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1
    • Lykke-Andersen J, Wagner E, (2005) Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev 19: 351-361.
    • (2005) Genes Dev , vol.19 , pp. 351-361
    • Lykke-Andersen, J.1    Wagner, E.2
  • 55
    • 77949716572 scopus 로고    scopus 로고
    • Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85
    • Kedar VP, Darby MK, Williams JG, Blackshear PJ, (2010) Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85. PLoS ONE 5: e9588 doi:10.1371/journal.pone.0009588.
    • (2010) PLoS ONE , vol.5
    • Kedar, V.P.1    Darby, M.K.2    Williams, J.G.3    Blackshear, P.J.4
  • 56
    • 33947495156 scopus 로고    scopus 로고
    • Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA
    • Sun L, Stoecklin G, Van Way S, Hinkovska-Galcheva V, Guo RF, et al. (2007) Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA. J Biol Chem 282: 3766-3777.
    • (2007) J Biol Chem , vol.282 , pp. 3766-3777
    • Sun, L.1    Stoecklin, G.2    van Way, S.3    Hinkovska-Galcheva, V.4    Guo, R.F.5
  • 57
    • 84863116439 scopus 로고    scopus 로고
    • AU-rich-element-dependent translation repression requires the cooperation of tristetraprolin and RCK/P54
    • Qi MY, Wang ZZ, Zhang Z, Shao Q, Zeng A, et al. (2012) AU-rich-element-dependent translation repression requires the cooperation of tristetraprolin and RCK/P54. Mol Cell Biol 32: 913-928.
    • (2012) Mol Cell Biol , vol.32 , pp. 913-928
    • Qi, M.Y.1    Wang, Z.Z.2    Zhang, Z.3    Shao, Q.4    Zeng, A.5
  • 58
    • 33745159015 scopus 로고    scopus 로고
    • Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation
    • Weston A, Sommerville J, (2006) Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation. Nucleic Acids Res 34: 3082-3094.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3082-3094
    • Weston, A.1    Sommerville, J.2
  • 59
    • 84856855006 scopus 로고    scopus 로고
    • Cullin 4B is recruited to tristetraprolin-containing messenger ribonucleoproteins and regulates TNF-alpha mRNA polysome loading
    • Pfeiffer JR, Brooks SA, (2012) Cullin 4B is recruited to tristetraprolin-containing messenger ribonucleoproteins and regulates TNF-alpha mRNA polysome loading. J Immunol 188: 1828-1839.
    • (2012) J Immunol , vol.188 , pp. 1828-1839
    • Pfeiffer, J.R.1    Brooks, S.A.2
  • 60
    • 80055086748 scopus 로고    scopus 로고
    • Novel phosphorylation-dependent ubiquitination of tristetraprolin by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (MEKK1) and tumor necrosis factor receptor-associated factor 2 (TRAF2)
    • Schichl YM, Resch U, Lemberger CE, Stichlberger D, de Martin R, (2011) Novel phosphorylation-dependent ubiquitination of tristetraprolin by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1 (MEKK1) and tumor necrosis factor receptor-associated factor 2 (TRAF2). J Biol Chem 286: 38466-38477.
    • (2011) J Biol Chem , vol.286 , pp. 38466-38477
    • Schichl, Y.M.1    Resch, U.2    Lemberger, C.E.3    Stichlberger, D.4    de Martin, R.5
  • 61
    • 79956089534 scopus 로고    scopus 로고
    • miR-346 controls release of TNF-alpha protein and stability of its mRNA in rheumatoid arthritis via tristetraprolin stabilization
    • Semaan N, Frenzel L, Alsaleh G, Suffert G, Gottenberg JE, et al. (2011) miR-346 controls release of TNF-alpha protein and stability of its mRNA in rheumatoid arthritis via tristetraprolin stabilization. PLoS ONE 6: e19827 doi:10.1371/journal.pone.0019827.
    • (2011) PLoS ONE , vol.6
    • Semaan, N.1    Frenzel, L.2    Alsaleh, G.3    Suffert, G.4    Gottenberg, J.E.5
  • 62
    • 84865179916 scopus 로고    scopus 로고
    • Tristetraprolin-driven regulatory circuit controls quality and timing of mRNA decay in inflammation
    • Kratochvill F, Machacek C, Vogl C, Ebner F, Sedlyarov V, et al. (2011) Tristetraprolin-driven regulatory circuit controls quality and timing of mRNA decay in inflammation. Mol Syst Biol 7: 560.
    • (2011) Mol Syst Biol , vol.7 , pp. 560
    • Kratochvill, F.1    Machacek, C.2    Vogl, C.3    Ebner, F.4    Sedlyarov, V.5
  • 64
    • 24044436193 scopus 로고    scopus 로고
    • Functionally independent AU-rich sequence motifs regulate KC (CXCL1) mRNA
    • Novotny M, Datta S, Biswas R, Hamilton T, (2005) Functionally independent AU-rich sequence motifs regulate KC (CXCL1) mRNA. J Biol Chem 280: 30166-30174.
    • (2005) J Biol Chem , vol.280 , pp. 30166-30174
    • Novotny, M.1    Datta, S.2    Biswas, R.3    Hamilton, T.4
  • 65
    • 79960929333 scopus 로고    scopus 로고
    • Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR
    • Lebedeva S, Jens M, Theil K, Schwanhausser B, Selbach M, et al. (2011) Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR. Mol Cell 43: 340-352.
    • (2011) Mol Cell , vol.43 , pp. 340-352
    • Lebedeva, S.1    Jens, M.2    Theil, K.3    Schwanhausser, B.4    Selbach, M.5
  • 66
    • 79960918737 scopus 로고    scopus 로고
    • Integrative regulatory mapping indicates that the RNA-binding protein HuR couples pre-mRNA processing and mRNA stability
    • Mukherjee N, Corcoran DL, Nusbaum JD, Reid DW, Georgiev S, et al. (2011) Integrative regulatory mapping indicates that the RNA-binding protein HuR couples pre-mRNA processing and mRNA stability. Mol Cell 43: 327-339.
    • (2011) Mol Cell , vol.43 , pp. 327-339
    • Mukherjee, N.1    Corcoran, D.L.2    Nusbaum, J.D.3    Reid, D.W.4    Georgiev, S.5
  • 67
    • 80555135917 scopus 로고    scopus 로고
    • Regulation of primary response genes
    • Fowler T, Sen R, Roy AL, (2011) Regulation of primary response genes. Mol Cell 44: 348-360.
    • (2011) Mol Cell , vol.44 , pp. 348-360
    • Fowler, T.1    Sen, R.2    Roy, A.L.3
  • 68
    • 34548810305 scopus 로고    scopus 로고
    • Analysis of turnover and translation regulatory RNA-binding protein expression through binding to cognate mRNAs
    • Pullmann R Jr, Kim HH, Abdelmohsen K, Lal A, Martindale JL, et al. (2007) Analysis of turnover and translation regulatory RNA-binding protein expression through binding to cognate mRNAs. Mol Cell Biol 27: 6265-6278.
    • (2007) Mol Cell Biol , vol.27 , pp. 6265-6278
    • Pullmann Jr., R.1    Kim, H.H.2    Abdelmohsen, K.3    Lal, A.4    Martindale, J.L.5
  • 69
    • 84857340173 scopus 로고    scopus 로고
    • Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins
    • Kedar VP, Zucconi BE, Wilson GM, Blackshear PJ, (2012) Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins. J Biol Chem 287: 5459-5471.
    • (2012) J Biol Chem , vol.287 , pp. 5459-5471
    • Kedar, V.P.1    Zucconi, B.E.2    Wilson, G.M.3    Blackshear, P.J.4
  • 70
    • 0035864364 scopus 로고    scopus 로고
    • Polymorphism in the 3′-untranslated region of TNFalpha mRNA impairs binding of the post-transcriptional regulatory protein HuR to TNFalpha mRNA
    • Di Marco S, Hel Z, Lachance C, Furneaux H, Radzioch D, (2001) Polymorphism in the 3′-untranslated region of TNFalpha mRNA impairs binding of the post-transcriptional regulatory protein HuR to TNFalpha mRNA. Nucleic Acids Res 29: 863-871.
    • (2001) Nucleic Acids Res , vol.29 , pp. 863-871
    • Di Marco, S.1    Hel, Z.2    Lachance, C.3    Furneaux, H.4    Radzioch, D.5
  • 71
    • 33744973775 scopus 로고    scopus 로고
    • Relief of microRNA-mediated translational repression in human cells subjected to stress
    • Bhattacharyya SN, Habermacher R, Martine U, Closs EI, Filipowicz W, (2006) Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125: 1111-1124.
    • (2006) Cell , vol.125 , pp. 1111-1124
    • Bhattacharyya, S.N.1    Habermacher, R.2    Martine, U.3    Closs, E.I.4    Filipowicz, W.5
  • 72
    • 0032431026 scopus 로고    scopus 로고
    • HNS, a nuclear-cytoplasmic shuttling sequence in HuR
    • Fan XC, Steitz JA, (1998) HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proc Natl Acad Sci U S A 95: 15293-15298.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15293-15298
    • Fan, X.C.1    Steitz, J.A.2
  • 73
    • 42149150455 scopus 로고    scopus 로고
    • Posttranslational modification of the AU-rich element binding protein HuR by protein kinase Cdelta elicits angiotensin II-induced stabilization and nuclear export of cyclooxygenase 2 mRNA
    • Doller A, Akool el S, Huwiler A, Muller R, Radeke HH, et al. (2008) Posttranslational modification of the AU-rich element binding protein HuR by protein kinase Cdelta elicits angiotensin II-induced stabilization and nuclear export of cyclooxygenase 2 mRNA. Mol Cell Biol 28: 2608-2625.
    • (2008) Mol Cell Biol , vol.28 , pp. 2608-2625
    • Doller, A.1    Akool el, S.2    Huwiler, A.3    Muller, R.4    Radeke, H.H.5
  • 74
    • 0141640857 scopus 로고    scopus 로고
    • Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2
    • Tran H, Maurer F, Nagamine Y, (2003) Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2. Mol Cell Biol 23: 7177-7188.
    • (2003) Mol Cell Biol , vol.23 , pp. 7177-7188
    • Tran, H.1    Maurer, F.2    Nagamine, Y.3
  • 75
    • 79960027929 scopus 로고    scopus 로고
    • Distinct functions of the mitogen-activated protein kinase-activated protein (MAPKAP) kinases MK2 and MK3: MK2 mediates lipopolysaccharide-induced signal transducers and activators of transcription 3 (STAT3) activation by preventing negative regulatory effects of MK3
    • Ehlting C, Ronkina N, Bohmer O, Albrecht U, Bode KA, et al. (2011) Distinct functions of the mitogen-activated protein kinase-activated protein (MAPKAP) kinases MK2 and MK3: MK2 mediates lipopolysaccharide-induced signal transducers and activators of transcription 3 (STAT3) activation by preventing negative regulatory effects of MK3. J Biol Chem 286: 24113-24124.
    • (2011) J Biol Chem , vol.286 , pp. 24113-24124
    • Ehlting, C.1    Ronkina, N.2    Bohmer, O.3    Albrecht, U.4    Bode, K.A.5
  • 76
    • 36849054438 scopus 로고    scopus 로고
    • Functional Analysis of KSRP Interaction with the AU-Rich Element of Interleukin-8 and Identification of Inflammatory mRNA Targets
    • Winzen R, Thakur BK, Dittrich-Breiholz O, Shah M, Redich N, et al. (2007) Functional Analysis of KSRP Interaction with the AU-Rich Element of Interleukin-8 and Identification of Inflammatory mRNA Targets. Mol Cell Biol 27: 8388-8400.
    • (2007) Mol Cell Biol , vol.27 , pp. 8388-8400
    • Winzen, R.1    Thakur, B.K.2    Dittrich-Breiholz, O.3    Shah, M.4    Redich, N.5
  • 77
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-Activated Protein Kinase p38 Controls the Expression and Posttranslational Modification of Tristetraprolin, a Regulator of Tumor Necrosis Factor Alpha mRNA Stability
    • Mahtani KR, Brook M, Dean JL, Sully G, Saklatvala J, et al. (2001) Mitogen-Activated Protein Kinase p38 Controls the Expression and Posttranslational Modification of Tristetraprolin, a Regulator of Tumor Necrosis Factor Alpha mRNA Stability. Mol Cell Biol 21: 6461-6469.
    • (2001) Mol Cell Biol , vol.21 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.