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Article

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

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Pages 2399-2407 | Received 26 Aug 2005, Accepted 22 Dec 2005, Published online: 27 Mar 2023

REFERENCES

  • Bakheet, T., M. Frevel, B. R. Williams, W. Greer, and K. S. Khabar. 2001. ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins. Nucleic Acids Res. 29:246–254.
  • Bakheet, T., B. R. Williams, and K. S. Khabar. 2003. ARED 2.0: an update of AU-rich element mRNA database. Nucleic Acids Res. 31:421–423.
  • Blasi, E., D. Radzioch, L. Merletti, and L. Varesio. 1989. Generation of macrophage cell line from fresh bone marrow cells with a myc/raf recombinant retrovirus. Cancer Biochem. Biophys. 10:303–317.
  • Bollig, F., R. Winzen, M. Gaestel, S. Kostka, K. Resch, and H. Holtmann. 2003. Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization. Biochem. Biophys. Res. Commun. 301:665–670.
  • Brook, M., G. Sully, A. R. Clark, and J. Saklatvala. 2000. Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett. 483:57–61.
  • Brooks, S. A., J. E. Connolly, and W. F. C. Rigby. 2004. The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. J. Immunol. 172:7263–7271.
  • Buxade, M., J. L. Parra, S. Rousseau, N. Shapiro, R. Marquez, N. Morrice, J. Bain, E. Espel, and C. G. Proud. 2005. The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1. Immunity 23:177–189.
  • Cao, H., L. J. Deterding, J. D. Venable, E. A. Kennington, J. R. Yates III, K. B. Tomer, and P. J. Blackshear. 2006. Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis. Biochem. J. 394:285–297.
  • Cao, H., J. S. Tuttle, and P. J. Blackshear. 2004. Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein. J. Biol. Chem. 279:21489–21499.
  • Carballo, E., H. Cao, W. S. Lai, E. A. Kennington, D. Campbell, and P. J. Blackshear. 2001. Decreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathway. J. Biol. Chem. 276:42580–42587.
  • Carrick, D., W. Lai, and P. Blackshear. 2004. The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis. Arthritis Res. Ther. 6:248–264.
  • Chrestensen, C. A., M. J. Schroeder, J. Shabanowitz, D. F. Hunt, J. W. Pelo, M. T. Worthington, and T. W. Sturgill. 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.
  • Clark, A. R., J. L. Dean, and J. Saklatvala. 2003. Post-transcriptional regulation of gene expression by mitogen-activated protein kinase p38. FEBS Lett. 546:37–44.
  • Dean, J. L., G. Sully, A. R. Clark, and J. Saklatvala. 2004. The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation. Cell Signal. 16:1113–1121.
  • Fechir, M., K. Linker, A. Pautz, T. Hubrich, U. Forstermann, F. Rodriguez-Pascual, and H. Kleinert. 2005. Tristetraprolin regulates the expression of the human inducible nitric-oxide synthase gene. Mol. Pharmacol. 67:2148–2161.
  • Frevel, M. A., T. Bakheet, A. M. Silva, J. G. Hissong, K. S. Khabar, and B. R. Williams. 2003. p38 mitogen-activated protein kinase-dependent and -independent signaling of mRNA stability of AU-rich element-containing transcripts. Mol. Cell. Biol. 23:425–436.
  • Jing, Q., S. Huang, S. Guth, T. Zarubin, A. Motoyama, J. Chen, F. Di Padova, S. C. Lin, H. Gram, and J. Han. 2005. Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell 120:623–634.
  • Karlsson, J. O., K. Ostwald, C. Kabjorn, and M. Andersson. 1994. A method for protein assay in Laemmli buffer. Anal. Biochem. 219:144–146.
  • Kedersha, N., and P. Anderson. 2002. Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 30:963–969.
  • Kotlyarov, A., A. Neininger, C. Schubert, R. Eckert, C. Birchmeier, H. Volk, and M. Gaestel. 1999. MAPKAP kinase 2 is essential for LPS-induced TNF-alpha biosynthesis. Nat. Cell Biol. 1:94–97.
  • Kotlyarov, A., Y. Yannoni, S. Fritz, K. Laass, J.-B. Telliez, D. Pitman, L.-L. Lin, and M. Gaestel. 2002. Distinct cellular functions of MK2. Mol. Cell. Biol. 22:4827–4835.
  • Lai, W. S., E. A. Kennington, and P. J. Blackshear. 2003. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol. Cell. Biol. 23:3798–3812.
  • Laroia, G., R. Cuesta, G. Brewer, and R. J. Schneider. 1999. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284:499–502.
  • Laroia, G., B. Sarkar, and R. J. Schneider. 2002. Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs. Proc. Natl. Acad. Sci. USA 99:1842–1846.
  • Lu, J.-Y., and R. J. Schneider. 2004. Tissue distribution of AU-rich mRNA-binding proteins involved in regulation of mRNA decay. J. Biol. Chem. 279:12974–12979.
  • Lykke-Andersen, J., and E. Wagner. 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.
  • Mahtani, K. R., M. Brook, J. L. E. Dean, G. Sully, J. Saklatvala, and A. R. Clark. 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.
  • Neininger, A., D. Kontoyiannis, A. Kotlyarov, R. Winzen, R. Eckert, H.-D. Volk, H. Holtmann, G. Kollias, and M. Gaestel. 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.
  • Rousseau, S., N. Morrice, M. Peggie, D. G. Campbell, M. Gaestel, and P. Cohen. 2002. Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs. EMBO J. 21:6505–6514.
  • Saklatvala, J. 2004. The p38 MAP kinase pathway as a therapeutic target in inflammatory disease. Curr. Opin. Pharmacol. 4:372–377.
  • Saklatvala, J., J. Dean, and A. Clark. 2003. Control of the expression of inflammatory response genes. Biochem. Soc. Symp. 70:95–106.
  • Stoecklin, G., T. Stubbs, N. Kedersha, S. Wax, W. F. Rigby, T. K. Blackwell, and P. Anderson. 2004. MK2-induced tristetraprolin:14-13-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 23:1313–1324.
  • Taylor, G., E. Carballo, D. Lee, W. Lai, M. Thompson, D. Patel, D. Schenkman, G. Gilkeson, H. Broxmeyer, B. Haynes, and P. Blackshear. 1996. A pathogenetic role for TNF alpha in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency. Immunity 4:445–454.
  • Tchen, C. R., M. Brook, J. Saklatvala, and A. R. Clark. 2004. The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself. J. Biol. Chem. 279:32393–32400.
  • Zhu, W., M. A. Brauchle, F. Di Padova, H. Gram, L. New, K. Ono, J. S. Downey, and J. Han. 2001. Gene suppression by tristetraprolin and release by the p38 pathway. Am. J. Physiol. Lung Cell Mol. Physiol. 281:L499–L508.

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