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Volumn 38, Issue 6, 2010, Pages 1632-1637

Molecular mechanisms of phosphorylation-regulated TTP (tristetraprolin) action and screening for further TTP-interacting proteins

Author keywords

mRNA stability; Phosphorylation; Protein protein interaction; Translation; Tristetraprolin (TTP); Yeast two hybrid screen

Indexed keywords

TRISTETRAPROLIN;

EID: 78649758708     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0381632     Document Type: Conference Paper
Times cited : (15)

References (43)
  • 1
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin
    • Carballo, E., Lai, W.S. and Blackshear, P.J. (1998) Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin. Science 281, 1001-1005 (Pubitemid 28399252)
    • (1998) Science , vol.281 , Issue.5379 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 2
    • 69249221371 scopus 로고    scopus 로고
    • TIS11 family proteins and their roles in posttranscriptional gene regulation
    • Baou, M., Jewell, A. and Murphy, J.J. (2009) TIS11 family proteins and their roles in posttranscriptional gene regulation. J. Biomed. Biotechnol. 2009, 634520
    • (2009) J. Biomed. Biotechnol. , vol.2009 , pp. 634520
    • Baou, M.1    Jewell, A.2    Murphy, J.J.3
  • 4
    • 45249098952 scopus 로고    scopus 로고
    • Control of mRNA decay by phosphorylation of tristetraprolin
    • Sandler, H. and Stoecklin, G. (2008) Control of mRNA decay by phosphorylation of tristetraprolin. Biochem. Soc. Trans. 36, 491-496
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 491-496
    • Sandler, H.1    Stoecklin, G.2
  • 5
    • 78049434471 scopus 로고    scopus 로고
    • MAPKAP kinases MK2 and MK3 in inflammation: Complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin
    • Ronkina, N., Menon, M.B., Schwermann, J., Tiedje, C., Hitti, E., Kotlyarov, A. and Gaestel, M. (2010) MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin. Biochem. Pharmacol. 80, 1915-1920
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1915-1920
    • Ronkina, N.1    Menon, M.B.2    Schwermann, J.3    Tiedje, C.4    Hitti, E.5    Kotlyarov, A.6    Gaestel, M.7
  • 6
    • 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, A.D., Radzioch, D., Clark, A.R., Blackshear, P.J., Kotlyarov, A. and Gaestel, M. (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    Radzioch, D.6    Clark, A.R.7    Blackshear, P.J.8    Kotlyarov, A.9    Gaestel, M.10
  • 7
    • 1942471656 scopus 로고    scopus 로고
    • MK2-induced tristetraprolin:14-3-3 Complexes prevent stress granule association and ARE-mRNA decay
    • DOI 10.1038/sj.emboj.7600163
    • Stoecklin, G., Stubbs, T., Kedersha, N., Wax, S., Rigby, W.F., Blackwell, T.K. and Anderson, P. (2004) MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 23, 1313-1324 (Pubitemid 38525003)
    • (2004) EMBO Journal , vol.23 , Issue.6 , pp. 1313-1324
    • Stoecklin, G.1    Stubbs, T.2    Kedersha, N.3    Wax, S.4    Rigby, W.F.C.5    Blackwell, T.K.6    Anderson, P.7
  • 8
    • 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
    • DOI 10.1128/MCB.21.9.6461-6469.2001
    • Mahtani, K.R., Brook, M., Dean, J.L.E., Sully, G., Saklatvala, J. and Clark, A.R. (2001) Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor α mRNA stability. Mol. Cell. Biol. 21, 6461-6469 (Pubitemid 32927414)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.19 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.E.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 9
    • 33644767306 scopus 로고    scopus 로고
    • Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways
    • Brook, M., Tchen, C.R., Santalucia, T., McIlrath, J., Arthur, J.S., Saklatvala, J. and Clark, A.R. (2006) Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways. Mol. Cell. Biol. 26, 2408-2418
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2408-2418
    • Brook, M.1    Tchen, C.R.2    Santalucia, T.3    McIlrath, J.4    Arthur, J.S.5    Saklatvala, J.6    Clark, A.R.7
  • 10
    • 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., Milarski, K., Askew, R., Marusic, S., Lin, L.L., Gaestel, M. and Telliez, J.B. (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    Milarski, K.6    Askew, R.7    Marusic, S.8    Lin, L.L.9    Gaestel, M.10    Telliez, J.B.11
  • 11
    • 77956261147 scopus 로고    scopus 로고
    • MAPKAP kinase 2 blocks tristetraprolin-directed mRNA decay by inhibiting CAF1 deadenylase recruitment
    • Marchese, F.P., Aubareda, A., Tudor, C., Saklatvala, J., Clark, A.R. and Dean, J.L. (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    Dean, J.L.6
  • 12
    • 77949716572 scopus 로고    scopus 로고
    • Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85
    • Kedar, V.P., Darby, M.K., Williams, J.G. and Blackshear, P.J. (2010) Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85. PLoS ONE 5, e9588
    • (2010) PLoS ONE , vol.5
    • Kedar, V.P.1    Darby, M.K.2    Williams, J.G.3    Blackshear, P.J.4
  • 14
    • 0037124067 scopus 로고    scopus 로고
    • Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms
    • Johnson, B.A., Stehn, J.R., Yaffe, M.B. and Blackwell, T.K. (2002) Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanismsJBiolChem. 277, 18029-18036
    • (2002) JBiolChem , vol.277 , pp. 18029-18036
    • Johnson, B.A.1    Stehn, J.R.2    Yaffe, M.B.3    Blackwell, T.K.4
  • 15
    • 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-α mRNA
    • Sun, L., Stoecklin, G., Van Way, S., Hinkovska-Galcheva, V., Guo, R.F., Anderson, P. and Shanley, T.P. (2007) Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-α 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    Anderson, P.6    Shanley, T.P.7
  • 16
    • 32944473015 scopus 로고    scopus 로고
    • Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis
    • DOI 10.1042/BJ20051316
    • Cao, H., Deterding, L.J., Venable, J.D., Kennington, E.A., Yates, 3rd, J.R., Tomer, K.B. and Blackshear, P.J. (2006) Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis. Biochem. J. 394, 285-297 (Pubitemid 43259679)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 285-297
    • Cao, H.1    Deterding, L.J.2    Venable, J.D.3    Kennington, E.A.4    Yates III, J.R.5    Tomer, K.B.6    Blackshear, P.J.7
  • 17
    • 0037376557 scopus 로고    scopus 로고
    • Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-α mRNA and serve as a substrate for mitogen-activated protein kinases
    • Cao, H., Dzineku, F. and Blackshear, P.J. (2003) Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-α mRNA and serve as a substrate for mitogen-activated protein kinases. Arch. Biochem. Biophys. 412, 106-120
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 106-120
    • Cao, H.1    Dzineku, F.2    Blackshear, P.J.3
  • 18
    • 0029016832 scopus 로고
    • Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro
    • Taylor, G.A., Thompson, M.J., Lai, W.S. and Blackshear, P.J. (1995) Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro. J. Biol. Chem. 270, 13341-13347
    • (1995) J. Biol. Chem. , vol.270 , pp. 13341-13347
    • Taylor, G.A.1    Thompson, M.J.2    Lai, W.S.3    Blackshear, P.J.4
  • 20
    • 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
    • DOI 10.1101/gad.1282305
    • Lykke-Andersen, J. and 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 (Pubitemid 40189298)
    • (2005) Genes and Development , vol.19 , Issue.3 , pp. 351-361
    • Lykke-Andersen, J.1    Wagner, E.2
  • 21
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • DOI 10.1101/gr.2122004
    • Lehner, B. and Sanderson, C.M. (2004) A protein interaction framework for human mRNA degradation. Genome Res. 14, 1315-1323 (Pubitemid 39029228)
    • (2004) Genome Research , vol.14 , Issue.7 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 23
    • 0034610333 scopus 로고    scopus 로고
    • A new screen for protein interactions reveals that the Saccharomyces cerevisiae high mobility group proteins Nhp6A/B are involved in the regulation of the GAL1 promoter
    • Laser, H., Bongards, C., Schuller, J., Heck, S., Johnsson, N. and Lehming, N. (2000) A new screen for protein interactions reveals that the Saccharomyces cerevisiae high mobility group proteins Nhp6A/B are involved in the regulation of the GAL1 promoter. Proc. Natl. Acad. Sci. U.S.A. 97, 13732-13737
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13732-13737
    • Laser, H.1    Bongards, C.2    Schuller, J.3    Heck, S.4    Johnsson, N.5    Lehming, N.6
  • 24
    • 34447130876 scopus 로고    scopus 로고
    • Yeast split-ubiquitin-based cytosolic screening system to detect interactions between transcriptionally active proteins
    • DOI 10.2144/000112455
    • Mockli, N., Deplazes, A., Hassa, P.O., Zhang, Z., Peter, M., Hottiger, M.O., Stagljar, I. and Auerbach, D. (2007) Yeast split-ubiquitin-based cytosolic screening system to detect interactions between transcriptionally active proteins. BioTechniques 42, 725-730 (Pubitemid 47035979)
    • (2007) BioTechniques , vol.42 , Issue.6 , pp. 725-730
    • Mockli, N.1    Deplazes, A.2    Hassa, P.O.3    Zhang, Z.4    Peter, M.5    Hottiger, M.O.6    Stagljar, I.7    Auerbach, D.8
  • 25
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar, I., Korostensky, C., Johnsson, N. and te Heesen, S. (1998) A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. U.S.A. 95, 5187-5192
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    Te Heesen, S.4
  • 26
    • 0032803068 scopus 로고    scopus 로고
    • Probing the molecular environment of membrane proteins in vivo
    • Wittke, S., Lewke, N., Muller, S. and Johnsson, N. (1999) Probing the molecular environment of membrane proteins in vivo. Mol. Biol. Cell 10, 2519-2530 (Pubitemid 29393507)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.8 , pp. 2519-2530
    • Wittke, S.1    Lewke, N.2    Muller, S.3    Johnsson, N.4
  • 27
    • 41849128212 scopus 로고    scopus 로고
    • An optimized split-ubiquitin cDNA-library screening system to identify novel interactors of the human Frizzled 1 receptor
    • DOI 10.1093/nar/gkm1163
    • Dirnberger, D., Messerschmid, M. and Baumeister, R. (2008) An optimized split-ubiquitin cDNA-library screening system to identify novel interactors of the human Frizzled 1 receptor. Nucleic Acids Res. 36, e37 (Pubitemid 351494254)
    • (2008) Nucleic Acids Research , vol.36 , Issue.6
    • Dirnberger, D.1    Messerschmid, M.2    Baumeister, R.3
  • 29
    • 36248962036 scopus 로고    scopus 로고
    • Proteins involved in sterol synthesis interact with Ste20 and regulate cell polarity
    • DOI 10.1242/jcs.009860
    • Tiedje, C., Holland, D.G., Just, U. and Hofken, T. (2007) Proteins involved in sterol synthesis interact with Ste20 and regulate cell polarity. J. Cell Sci. 120, 3613-3624 (Pubitemid 350120953)
    • (2007) Journal of Cell Science , vol.120 , Issue.20 , pp. 3613-3624
    • Tiedje, C.1    Holland, D.G.2    Just, U.3    Hofken, T.4
  • 31
    • 3042780219 scopus 로고    scopus 로고
    • A tethered catalysis, two-hybrid system to identify protein-protein interactions requiring post-translational modifications
    • Guo, D., Hazbun, T.R., Xu, X.J., Ng, S.L., Fields, S. and Kuo, M.H. (2004) A tethered catalysis, two-hybrid system to identify protein-protein interactions requiring post-translational modifications. Nat. Biotechnol. 22, 888-892
    • (2004) Nat. Biotechnol. , vol.22 , pp. 888-892
    • Guo, D.1    Hazbun, T.R.2    Xu, X.J.3    Ng, S.L.4    Fields, S.5    Kuo, M.H.6
  • 32
    • 0028802599 scopus 로고
    • The yeast tribrid system: Genetic detection of trans-phosphorylated ITAM-SH2 interactions
    • Osborne, M.A., Dalton, S. and Kochan, J.P. (1995) The yeast tribrid system: genetic detection of trans-phosphorylated ITAM-SH2 interactions. Biotechnology 13, 1474-1478
    • (1995) Biotechnology , vol.13 , pp. 1474-1478
    • Osborne, M.A.1    Dalton, S.2    Kochan, J.P.3
  • 34
    • 24144499990 scopus 로고    scopus 로고
    • Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR
    • DOI 10.1093/nar/gki797
    • Linker, K., Pautz, A., Fechir, M., Hubrich, T., Greeve, J. and Kleinert, H. (2005) Involvement of KSRP in the post-transcriptional regulation of human iNOS expression: complex interplay of KSRP with TTP and HuR. Nucleic Acids Res. 33, 4813-4827 (Pubitemid 41418881)
    • (2005) Nucleic Acids Research , vol.33 , Issue.15 , pp. 4813-4827
    • Linker, K.1    Pautz, A.2    Fechir, M.3    Hubrich, T.4    Greeve, J.5    Kleinert, H.6
  • 35
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • DOI 10.1016/j.molcel.2005.10.031, PII S1097276505017260
    • Fenger-Gron, M., Fillman, C., Norrild, B. and Lykke-Andersen, J. (2005) Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 20, 905-915 (Pubitemid 41814879)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 905-915
    • Fenger-Gron, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 36
    • 20044388720 scopus 로고    scopus 로고
    • Involvement of MicroRNA in AU-Rich Element-Mediated mRNA Instability
    • DOI 10.1016/j.cell.2004.12.038
    • Jing, Q., Huang, S., Guth, S., Zarubin, T., Motoyama, A., Chen, J., Di Padova, F., Lin, S.C., Gram, H. and Han, J. (2005) Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell 120, 623-634 (Pubitemid 40343075)
    • (2005) Cell , vol.120 , Issue.5 , pp. 623-634
    • Jing, Q.1    Huang, S.2    Guth, S.3    Zarubin, T.4    Motoyama, A.5    Chen, J.6    Di Padova, F.7    Lin, S.-C.8    Gram, H.9    Han, J.10
  • 37
    • 41949103837 scopus 로고    scopus 로고
    • p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein
    • Chen, G., Guo, X., Lv, F., Xu, Y. and Gao, G. (2008) p72 DEAD box RNA helicase is required for optimal function of the zinc-finger antiviral protein. Proc. Natl. Acad. Sci. U.S.A. 105, 4352-4357
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4352-4357
    • Chen, G.1    Guo, X.2    Lv, F.3    Xu, Y.4    Gao, G.5
  • 38
    • 0842332176 scopus 로고    scopus 로고
    • Direct association of tristetraprolin with the nucleoporin CAN/Nup214Biochem
    • Carman, J.A. and Nadler, S.G. (2004) Direct association of tristetraprolin with the nucleoporin CAN/Nup214Biochem. Biophys. Res. Commun. 315, 445-449
    • (2004) Biophys. Res. Commun. , vol.315 , pp. 445-449
    • Carman, J.A.1    Nadler, S.G.2
  • 41
    • 0036510607 scopus 로고    scopus 로고
    • HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences
    • Dintilhac, A. and Bernues, J. (2002) HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. J. Biol. Chem. 277, 7021-7028
    • (2002) J. Biol. Chem. , vol.277 , pp. 7021-7028
    • Dintilhac, A.1    Bernues, J.2
  • 43
    • 0028875318 scopus 로고
    • Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif
    • Engel, K., Schultz, H., Martin, F., Kotlyarov, A., Plath, K., Hahn, M., Heinemann, U. and Gaestel, M. (1995) Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif. J. Biol. Chem. 270, 27213-27221
    • (1995) J. Biol. Chem. , vol.270 , pp. 27213-27221
    • Engel, K.1    Schultz, H.2    Martin, F.3    Kotlyarov, A.4    Plath, K.5    Hahn, M.6    Heinemann, U.7    Gaestel, M.8


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