Functional Analysis of KSRP Interaction with the AU-Rich Element of Interleukin-8 and Identification of Inflammatory mRNA Targets

REFERENCES

• Bakheet, T., B. R. Williams, and K. S. Khabar. 2006. ARED 3.0: the large and diverse AU-rich transcriptome. Nucleic Acids Res. 34:D111–D114.
   PubMed Web of Science ®Google Scholar
• Ben-Levy, R., S. Hooper, R. Wilson, H. F. Paterson, and C. J. Marshall. 1998. Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr. Biol. 8:1049–1057.
   PubMed Web of Science ®Google Scholar
• Briata, P., S. V. Forcales, M. Ponassi, G. Corte, C. Y. Chen, M. Karin, P. L. Puri, and R. Gherzi. 2005. p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts. Mol. Cell 20:891–903.
   PubMed Web of Science ®Google Scholar
• Brook, M., C. R. Tchen, T. Santalucia, J. McIlrath, J. S. Arthur, J. Saklatvala, and A. R. Clark. 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.
   PubMed Web of Science ®Google Scholar
• Brooks, S. A., J. E. Connolly, and W. F. 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Chen, C. Y., R. Gherzi, S. E. Ong, E. L. Chan, R. Raijmakers, G. J. Pruijn, G. Stoecklin, C. Moroni, M. Mann, and M. Karin. 2001. AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 107:451–464.
   PubMed Web of Science ®Google Scholar
• Chen, C. Y., and A. B. Shyu. 1995. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 20:465–470.
   PubMed Web of Science ®Google Scholar
• Chou, C. F., A. Mulky, S. Maitra, W. J. Lin, R. Gherzi, J. Kappes, and C. Y. Chen. 2006. Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay. Mol. Cell. Biol. 26:3695–3706.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Chung, H. J., J. Liu, M. Dundr, Z. Nie, S. Sanford, and D. Levens. 2006. FBPs are calibrated molecular tools to adjust gene expression. Mol. Cell. Biol. 26:6584–6597.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Dong, S., C. Li, D. Zenklusen, R. H. Singer, A. Jacobson, and F. He. 2007. YRA1 autoregulation requires nuclear export and cytoplasmic Edc3p-mediated degradation of its pre-mRNA. Mol. Cell 25:559–573.
   PubMedGoogle Scholar
• Engel, K., A. Kotlyarov, and M. Gaestel. 1998. Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J. 17:3363–3371.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Gaestel, M. 2006. MAPKAP kinases—MKs—two's company, three's a crowd. Nat. Rev. Mol. Cell Biol. 7:120–130.
   PubMed Web of Science ®Google Scholar
• Garneau, N. L., J. Wilusz, and C. J. Wilusz. 2007. The highways and byways of mRNA decay. Nat. Rev. Mol. Cell Biol. 8:113–126.
   PubMed Web of Science ®Google Scholar
• Gherzi, R., K. Y. Lee, P. Briata, D. Wegmuller, C. Moroni, M. Karin, and C. Y. Chen. 2004. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol. Cell 14:571–583.
   PubMed Web of Science ®Google Scholar
• Gherzi, R., M. Trabucchi, M. Ponassi, T. Ruggiero, G. Corte, C. Moroni, C. Y. Chen, K. S. Khabar, J. S. Andersen, and P. Briata. 2006. The RNA-binding protein KSRP promotes decay of beta-catenin mRNA and is inactivated by PI3K-AKT signaling. PLoS Biol. 5:e5.
   PubMed Web of Science ®Google Scholar
• Gowrishankar, G., R. Winzen, F. Bollig, B. Ghebremedhin, N. Redich, B. Ritter, K. Resch, M. Kracht, and H. Holtmann. 2005. Inhibition of mRNA deadenylation and degradation by ultraviolet light. Biol. Chem. 386:1287–1293.
   PubMedGoogle Scholar
• Gowrishankar, G., R. Winzen, O. Dittrich-Breiholz, N. Redich, M. Kracht, and H. Holtmann. 2006. Inhibition of mRNA deadenylation and degradation by different types of cell stress. Biol. Chem. 387:323–327.
   PubMed Web of Science ®Google Scholar
• Green, J., K. S. Khabar, B. C. Koo, B. R. Williams, and S. J. Polyak. 2006. Stability of CXCL-8 and related AU-rich mRNAs in the context of hepatitis C virus replication in vitro. J. Infect. Dis. 193:802–811.
   PubMedGoogle Scholar
• Gu, W., F. Pan, H. Zhang, G. J. Bassell, and R. H. Singer. 2002. A predominantly nuclear protein affecting cytoplasmic localization of beta-actin mRNA in fibroblasts and neurons. J. Cell Biol. 156:41–51.
   PubMedGoogle Scholar
• Hitti, E., T. Iakovleva, M. Brook, S. Deppenmeier, A. D. Gruber, D. Radzioch, A. R. Clark, P. J. Blackshear, A. Kotlyarov, and M. Gaestel. 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.
   PubMed Web of Science ®Google Scholar
• Hoffmann, E., O. Dittrich-Breiholz, H. Holtmann, and M. Kracht. 2002. Multiple control of interleukin-8 gene expression. J. Leukoc. Biol. 72:847–855.
   PubMed Web of Science ®Google Scholar
• Holtmann, H., R. Winzen, P. Holland, S. Eickemeier, E. Hoffmann, D. Wallach, N. L. Malinin, J. A. Cooper, K. Resch, and M. Kracht. 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.
   PubMed Web of Science ®Google Scholar
• Hornstein, E., H. Harel, G. Levy, and O. Meyuhas. 1999. Overexpression of poly(A)-binding protein down-regulates the translation or the abundance of its own mRNA. FEBS Lett. 457:209–213.
   PubMedGoogle Scholar
• Huttelmaier, S., D. Zenklusen, M. Lederer, J. Dictenberg, M. Lorenz, X. Meng, G. J. Bassell, J. Condeelis, and R. H. Singer. 2005. Spatial regulation of beta-actin translation by Src-dependent phosphorylation of ZBP1. Nature 438:512–515.
   PubMed Web of Science ®Google Scholar
• Junttila, M. R., S. Saarinen, T. Schmidt, J. Kast, and J. Westermarck. 2005. Single-step Strep-tag purification for the isolation and identification of protein complexes from mammalian cells. Proteomics 5:1199–1203.
   PubMed Web of Science ®Google Scholar
• Kolev, N. G., and P. W. Huber. 2003. VgRBP71 stimulates cleavage at a polyadenylation signal in Vg1 mRNA, resulting in the removal of a cis-acting element that represses translation. Mol. Cell 11:745–755.
   PubMedGoogle Scholar
• Lai, W. S., E. Carballo, J. M. Thorn, E. A. Kennington, and P. J. Blackshear. 2000. Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA. J. Biol. Chem. 275:17827–17837.
   PubMed Web of Science ®Google Scholar
• Linker, K., A. Pautz, M. Fechir, T. Hubrich, J. Greeve, and H. Kleinert. 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Mahtani, K. R., M. Brook, J. L. 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.
   PubMed Web of Science ®Google Scholar
• Min, H., C. W. Turck, J. M. Nikolic, and D. L. Black. 1997. A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer. Genes Dev. 11:1023–1036.
   PubMedGoogle Scholar
• Rehbein, M., K. Wege, F. Buck, M. Schweizer, D. Richter, and S. Kindler. 2002. Molecular characterization of MARTA1, a protein interacting with the dendritic targeting element of MAP2 mRNAs. J. Neurochem. 82:1039–1046.
   PubMedGoogle Scholar
• Ruggiero, T., M. Trabucchi, M. Ponassi, G. Corte, C. Y. Chen, L. al-Haj, K. S. Khabar, P. Briata, and R. Gherzi. 2007. Identification of a set of KSRP target transcripts upregulated by PI3K-AKT signaling. BMC Mol. Biol. 8:28.
   PubMedGoogle Scholar
• Rydziel, S., A. M. Delany, and E. Canalis. 2004. AU-rich elements in the collagenase 3 mRNA mediate stabilization of the transcript by cortisol in osteoblasts. J. Biol. Chem. 279:5397–5404.
   PubMed Web of Science ®Google Scholar
• Shaw, G., and R. Kamen. 1986. A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46:659–667.
   PubMed Web of Science ®Google Scholar
• Snee, M., G. J. Kidd, T. P. Munro, and R. Smith. 2002. RNA trafficking and stabilization elements associate with multiple brain proteins. J. Cell Sci. 115:4661–4669.
   PubMedGoogle Scholar
• Stoecklin, G., T. Mayo, and P. Anderson. 2006. ARE-mRNA degradation requires the 5′-3′ decay pathway. EMBO Rep. 7:72–77.
   PubMed Web of Science ®Google Scholar
• Stoecklin, G., T. Stubbs, N. Kedersha, S. Wax, W. F. Rigby, T. K. Blackwell, and P. Anderson. 2004. MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 23:1313–1324.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Winzen, R., G. Gowrishankar, F. Bollig, N. Redich, K. Resch, and H. Holtmann. 2004. Distinct domains of AU-rich elements exert different functions in mRNA destabilization and stabilization by p38 mitogen-activated protein kinase or HuR. Mol. Cell. Biol. 24:4835–4847.
   PubMedGoogle Scholar
• Winzen, R., S. Kafert, B. Preiss, H. A. Mylius-Spencker, K. Resch, and H. Holtmann. 1996. Interaction between the mRNA of the 55-kDa tumor necrosis factor receptor and cellular proteins. Possible involvement in post-transcriptional regulation of receptor expression. J. Biol. Chem. 271:13461–13467.
   PubMedGoogle Scholar
• Winzen, R., M. Kracht, B. Ritter, A. Wilhelm, C. Y. Chen, A. B. Shyu, M. Muller, M. Gaestel, K. Resch, and H. Holtmann. 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.
   PubMed Web of Science ®Google Scholar
• Yu, J. Y., S. L. DeRuiter, and D. L. Turner. 2002. RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells. Proc. Natl. Acad. Sci. USA 99:6047–6052.
   PubMed Web of Science ®Google Scholar