Post-transcriptional control of cytokine production (original) (raw)
Stoecklin, G. & Anderson, P. Posttranscriptional mechanisms regulating the inflammatory response. Adv. Immunol.89, 1–37 (2006). ArticleCASPubMed Google Scholar
Hamilton, T.A. et al. Chemokine and chemoattractant receptor expression: post-transcriptional regulation. J. Leukoc. Biol.82, 213–219 (2007). ArticleCASPubMed Google Scholar
Khabar, K.S. Rapid transit in the immune cells: the role of mRNA turnover regulation. J. Leukoc. Biol.81, 1335–1344 (2007). ArticleCASPubMed Google Scholar
Caput, D. et al. Identification of a common nucleotide sequence in the 3′-untranslated region of mRNA molecules specifying inflammatory mediators. Proc. Natl. Acad. Sci. USA83, 1670–1674 (1986). ArticleCASPubMedPubMed Central Google Scholar
Shaw, G. & Kamen, R. A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell46, 659–667 (1986). ArticleCASPubMed Google Scholar
Stoecklin, G. et al. Genome-wide analysis identifies interleukin-10 mRNA as target of tristetraprolin. J. Biol. Chem. published online 6 February 2008 (doi:10.1074/jbc.M709657200). ArticleCAS Google Scholar
Chen, C.Y.A. & Shyu, A.B. AU-rich elements: Characterization and importance in mRNA degradation. Trends Biochem. Sci.20, 465–470 (1995). ArticleCASPubMed Google Scholar
Chen, C.Y.A., Xu, N. & Shyu, A.B. mRNA decay mediated by two distinct AU-rich elements from c-fos and granulocyte-macrophage colony-stimulating factor transcripts: Different deadenylation kinetics and uncoupling from translation. Mol. Cell. Biol.15, 5777–5788 (1995). ArticleCASPubMedPubMed Central Google Scholar
Lagnado, C.A., Brown, C.Y. & Goodall, G.J. AUUUA is not sufficient to promote poly(A) shortening and degradation of an mRNA: the functional sequence within AU-rich elements may be UUAUUUA(U/A)(U/A). Mol. Cell. Biol.14, 7984–7995 (1994). CASPubMedPubMed Central Google Scholar
Zubiaga, A.M., Belasco, J.G. & Greenberg, M.E. The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation. Mol. Cell. Biol.15, 2219–2230 (1995). ArticleCASPubMedPubMed Central Google Scholar
Blackshear, P.J. et al. Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates. J. Biol. Chem.278, 19947–19955 (2003). ArticleCASPubMed Google Scholar
Worthington, M.T. et al. RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein. J. Biol. Chem.277, 48558–48564 (2002). ArticleCASPubMed Google Scholar
Lopez de Silanes, I. et al. Identification and functional outcome of mRNAs associated with RNA-binding protein TIA-1. Mol. Cell. Biol.25, 9520–9531 (2005). ArticleCASPubMedPubMed Central Google Scholar
Garnon, J. et al. Fragile X-related protein FXR1P regulates proinflammatory cytokine tumor necrosis factor expression at the post-transcriptional level. J. Biol. Chem.280, 5750–5763 (2005). ArticleCASPubMed Google Scholar
Mukhopadhyay, D., Houchen, C.W., Kennedy, S., Dieckgraefe, B.K. & Anant, S. Coupled mRNA stabilization and translational silencing of cyclooxygenase-2 by a novel RNA binding protein, CUGBP2. Mol. Cell11, 113–126 (2003). ArticleCASPubMed Google Scholar
Carballo, E., Lai, W.S. & Blackshear, P.J. Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin. Science281, 1001–1005 (1998). ArticleCASPubMed Google Scholar
Chou, C.F. et al. Tethering KSRP, a decay-promoting AU-rich element-binding protein, to mRNAs elicits mRNA decay. Mol. Cell. Biol.26, 3695–3706 (2006). ArticleCASPubMedPubMed Central Google Scholar
Gherzi, R. et al. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol. Cell14, 571–583 (2004). ArticleCASPubMed Google Scholar
Laroia, G., Cuesta, R., Brewer, G. & Schneider, R.J. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science284, 499–502 (1999). ArticleCASPubMed Google Scholar
Lu, J.Y., Bergman, N., Sadri, N. & Schneider, R.J. Assembly of AUF1 with eIF4G-poly(A) binding protein complex suggests a translation function in AU-rich mRNA decay. RNA12, 883–893 (2006). ArticleCASPubMedPubMed Central Google Scholar
Lu, J.Y., Sadri, N. & Schneider, R.J. Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs. Genes Dev.20, 3174–3184 (2006). ArticleCASPubMedPubMed Central Google Scholar
Sarkar, B., Xi, Q., He, C. & Schneider, R.J. Selective degradation of AU-rich mRNAs promoted by the p37 AUF1 protein isoform. Mol. Cell. Biol.23, 6685–6693 (2003). ArticleCASPubMedPubMed Central Google Scholar
Fan, X.C. & Steitz, J.A. Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J.17, 3448–3460 (1998). ArticleCASPubMedPubMed Central Google Scholar
Peng, S.S., Chen, C.Y., Xu, N. & Shyu, A.B. RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J.17, 3461–3470 (1998). ArticleCASPubMedPubMed Central Google Scholar
Galban, S. et al. RNA-binding proteins HuR and PTB promote the translation of hypoxia-inducible factor-1α. Mol. Cell Biol.28, 93–107 (2007). ArticlePubMedPubMed CentralCAS Google Scholar
Katsanou, V. et al. HuR as a negative posttranscriptional modulator in inflammation. Mol. Cell19, 777–789 (2005). ArticleCASPubMed Google Scholar
Sureban, S.M. et al. Functional antagonism between RNA binding proteins HuR and CUGBP2 determines the fate of COX-2 mRNA translation. Gastroenterology132, 1055–1065 (2007). ArticleCASPubMed Google Scholar
Linker, K. et al. 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 (2005). ArticleCASPubMedPubMed Central Google Scholar
David, P.S., Tanveer, R. & Port, J.D. FRET-detectable interactions between the ARE binding proteins, HuR and p37AUF1. RNA13, 1453–1468 (2007). ArticleCASPubMedPubMed Central Google Scholar
Pan, Y.X., Chen, H. & Kilberg, M.S. Interaction of RNA-binding proteins HuR and AUF1 with the human ATF3 mRNA 3′-untranslated region regulates its amino acid limitation-induced stabilization. J. Biol. Chem.280, 34609–34616 (2005). ArticleCASPubMed Google Scholar
Yamasaki, S., Stoecklin, G., Kedersha, N., Simarro, M. & Anderson, P. T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs. J. Biol. Chem.282, 30070–30077 (2007). ArticleCASPubMed Google Scholar
Rothe, F., Gueydan, C., Bellefroid, E., Huez, G. & Kruys, V. Identification of FUSE-binding proteins as interacting partners of TIA proteins. Biochem. Biophys. Res. Commun.343, 57–68 (2006). ArticleCASPubMed Google Scholar
Liao, B., Hu, Y. & Brewer, G. Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation. Nat. Struct. Mol. Biol.14, 511–518 (2007). ArticleCASPubMed Google Scholar
Chrestensen, C.A. et al. 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). ArticleCASPubMed Google Scholar
Stoecklin, G., Stubbs, T., Kedersha, N., Blackwell, T.K. & Anderson, P. MK2-induced tristetraprolin:14–3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J.23, 1313–1324 (2004). ArticleCASPubMedPubMed Central Google Scholar
Sun, L. et al. 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). ArticleCASPubMed Google Scholar
Schmidlin, M. et al. The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B. EMBO J.23, 4760–4769 (2004). ArticleCASPubMedPubMed Central Google Scholar
Benjamin, D., Schmidlin, M., Min, L., Gross, B. & Moroni, C. BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites. Mol. Cell. Biol.26, 9497–9507 (2006). ArticleCASPubMedPubMed Central Google Scholar
Gherzi, R. et al. The RNA-binding protein KSRP promotes decay of β-catenin mRNA and is inactivated by PI3K-AKT signaling. PLoS Biol.5, e5 (2006). ArticlePubMedPubMed CentralCAS Google Scholar
He, C. & Schneider, R. 14–3-3sigma is a p37 AUF1-binding protein that facilitates AUF1 transport and AU-rich mRNA decay. EMBO J.25, 3823–3831 (2006). ArticleCASPubMedPubMed Central Google Scholar
Pyronnet, S. et al. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J.18, 270–279 (1999). ArticleCASPubMedPubMed Central Google Scholar
Waskiewicz, A.J. et al. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol. Cell. Biol.19, 1871–1880 (1999). ArticleCASPubMedPubMed Central Google Scholar
Buxade, M. et al. The Mnks are novel components in the control of TNFα biosynthesis and phosphorylate and regulate hnRNP A1. Immunity23, 177–189 (2005). ArticleCASPubMed Google Scholar
Shen, Z.J., Esnault, S. & Malter, J.S. The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils. Nat. Immunol.6, 1280–1287 (2005). ArticleCASPubMed Google Scholar
Esnault, S. et al. A critical role for Pin1 in allergic pulmonary eosinophilia in rats. J. Allergy Clin. Immunol.120, 1082–1088 (2007). ArticleCASPubMed Google Scholar
Greenwald, R.J., Freeman, G.J. & Sharpe, A.H. The B7 family revisited. Annu. Rev. Immunol.23, 515–548 (2005). ArticlePubMedCAS Google Scholar
Sharpe, A.H., Wherry, E.J., Ahmed, R. & Freeman, G.J. The function of programmed cell death 1 and its ligands in regulating autoimmunity and infection. Nat. Immunol.8, 239–245 (2007). ArticleCASPubMed Google Scholar
Lindstein, T., June, C.H., Ledbetter, J.A., Stella, G. & Thompson, C.B. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science244, 339–343 (1989). ArticleCASPubMed Google Scholar
Sanchez-Lockhart, M. & Miller, J. Engagement of CD28 outside of the immunological synapse results in up-regulation of IL-2 mRNA stability but not IL-2 transcription. J. Immunol.176, 4778–4784 (2006). ArticleCASPubMed Google Scholar
Mestas, J., Crampton, S.P., Hori, T. & Hughes, C.C. Endothelial cell co-stimulation through OX40 augments and prolongs T cell cytokine synthesis by stabilization of cytokine mRNA. Int. Immunol.17, 737–747 (2005). ArticleCASPubMed Google Scholar
Wang, J.G. et al. LFA-1-dependent HuR nuclear export and cytokine mRNA stabilization in T cell activation. J. Immunol.176, 2105–2113 (2006). ArticleCASPubMed Google Scholar
Stoecklin, G., Lu, M., Rattenbacher, B. & Moroni, C. A constitutive decay element promotes tumor necrosis factor α mRNA degradation via an AU-rich element-independent pathway. Mol. Cell. Biol.23, 3506–3515 (2003). ArticleCASPubMedPubMed Central Google Scholar
Brown, C.Y., Lagnado, C.A. & Goodall, G.J. A cytokine mRNA-destabilizing element that is structurally and functionally distinct from A+U-rich elements. Proc. Natl. Acad. Sci. USA93, 13721–13725 (1996). ArticleCASPubMedPubMed Central Google Scholar
Shim, J. & Lim, H. J, R.Y. & Karin, M. Nuclear export of NF90 is required for interleukin-2 mRNA stabilization. Mol. Cell10, 1331–1344 (2002). ArticleCASPubMed Google Scholar
Chen, C.Y. et al. Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation. Genes Dev.14, 1236–1248 (2000). ArticleCASPubMedPubMed Central Google Scholar
Jing, Q. et al. Involvement of microRNA in AU-rich element-mediated mRNA instability. Cell120, 623–634 (2005). ArticleCASPubMed Google Scholar
Pillai, R.S., Artus, C.G. & Filipowicz, W. Tethering of human Ago proteins to mRNA mimics the miRNA-mediated repression of protein synthesis. RNA10, 1518–1525 (2004). ArticleCASPubMedPubMed Central Google Scholar
Vasudevan, S., Tong, Y. & Steitz, J.A. Switching from repression to activation: microRNAs can up-regulate translation. Science318, 1931–1934 (2007). ArticleCASPubMed Google Scholar
O'Connell, R.M., Taganov, K.D., Boldin, M.P., Cheng, G. & Baltimore, D. MicroRNA-155 is induced during the macrophage inflammatory response. Proc. Natl. Acad. Sci. USA104, 1604–1609 (2007). ArticleCASPubMedPubMed Central Google Scholar
Leung, A.K., Calabrese, J.M. & Sharp, P.A. Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules. Proc. Natl. Acad. Sci. USA103, 18125–18130 (2006). ArticleCASPubMedPubMed Central Google Scholar
Liu, J. et al. A role for the P-body component GW182 in microRNA function. Nat. Cell Biol.7, 1161–1166 (2005). ArticleCAS Google Scholar
Liu, J., Valencia-Sanchez, M.A., Hannon, G.J. & Parker, R. MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nat. Cell Biol.7, 719–723 (2005). ArticleCASPubMedPubMed Central Google Scholar
Anderson, P. & Kedersha, N. Stress granules: the Tao of RNA triage. Trends Biochem. Sci. published online 19 February 2008 (doi:10.1016/j.tibs.2007.12.003). ArticleCASPubMed Google Scholar
Parker, R. & Sheth, U. P bodies and the control of mRNA translation and degradation. Mol. Cell25, 635–646 (2007). ArticleCASPubMed Google Scholar
Kedersha, N. et al. Stress granules and processing bodies are dynamically liked sites of mRNP remodeling. J. Cell Biol.169, 871–884 (2005). ArticleCASPubMedPubMed Central Google Scholar
Franks, T.M. & Lykke-Andersen, J. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev.21, 719–735 (2007). ArticleCASPubMedPubMed Central Google Scholar
Stoecklin, G. & Anderson, P. In a tight spot: ARE-mRNAs at processing bodies. Genes Dev.21, 627–631 (2007). ArticleCASPubMed Google Scholar
Bhattacharyya, S.N., Habermacher, R., Martine, U., Closs, E.I. & Filipowicz, W. Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell125, 1111–1124 (2006). ArticleCASPubMed Google Scholar
Scheu, S. et al. Activation of the integrated stress response during T helper cell differentiation. Nat. Immunol.7, 644–651 (2006). ArticleCASPubMed Google Scholar
Vinuesa, C.G. et al. A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity. Nature435, 452–458 (2005). ArticleCASPubMed Google Scholar
Yu, D. et al. Roquin represses autoimmunity by limiting inducible T-cell co-stimulator mRNA. Nature450, 299–303 (2007). ArticleCASPubMed Google Scholar
Munn, D.H. et al. GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase. Immunity22, 633–642 (2005). ArticleCASPubMed Google Scholar
MacKenzie, C.R., Heseler, K., Muller, A. & Daubener, W. Role of indoleamine 2,3-dioxygenase in antimicrobial defence and immuno-regulation: tryptophan depletion versus production of toxic kynurenines. Curr. Drug Metab.8, 237–244 (2007). ArticleCASPubMed Google Scholar
Sedlmayr, P. Indoleamine 2,3-dioxygenase in materno-fetal interaction. Curr. Drug Metab.8, 205–208 (2007). ArticleCASPubMed Google Scholar
Gaestel, M., Mengel, A., Bothe, U. & Asadullah, K. Protein kinases as small molecule inhibitor targets in inflammation. Curr. Med. Chem.14, 2214–2234 (2007). ArticleCASPubMed Google Scholar
Schett, G., Zwerina, J. & Firestein, G. The p38 mitogen activated protein kinase (MAPK) pathway in rheumatoid arthritis. Ann. Rheum. Dis., published online 7 September 2007 (doi:10.1136/ard.2007.074278). ArticlePubMedCAS Google Scholar
Johansen, C. et al. Protein expression of TNF-α in psoriatic skin is regulated at a posttranscriptional level by MAPK-activated protein kinase 2. J. Immunol.176, 1431–1438 (2006). ArticleCASPubMed Google Scholar
Hegen, M., Gaestel, M., Nickerson-Nutter, C.L., Lin, L.L. & Telliez, J.B. MAPKAP kinase 2-deficient mice are resistant to collagen-induced arthritis. J. Immunol.177, 1913–1917 (2006). ArticleCASPubMed Google Scholar
Ding, C. Drug evaluation: VX-702, a MAP kinase inhibitor for rheumatoid arthritis and acute coronary syndrome. Curr. Opin. Investig. Drugs7, 1020–1025 (2006). CASPubMed Google Scholar
Schreiber, S. et al. Oral p38 mitogen-activated protein kinase inhibition with BIRB 796 for active Crohn's disease: a randomized, double-blind, placebo-controlled trial. Clin. Gastroenterol. Hepatol.4, 325–334 (2006). ArticleCASPubMed Google Scholar
Esnault, S., Shen, Z.J., Whitesel, E. & Malter, J.S. The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes. J. Immunol.177, 6999–7006 (2006). ArticleCASPubMed Google Scholar
Chen, Y.L. et al. Differential regulation of ARE-mediated TNFα and IL-1β mRNA stability by lipopolysaccharide in RAW264.7 cells. Biochem. Biophys. Res. Commun.346, 160–168 (2006). ArticleCASPubMed Google Scholar
Bufler, P., Gamboni-Robertson, F., Azam, T., Kim, S.H. & Dinarello, C.A. Interleukin-1 homologues IL-1F7b and IL-18 contain functional mRNA instability elements within the coding region responsive to lipopolysaccharide. Biochem. J.381, 503–510 (2004). ArticleCASPubMedPubMed Central Google Scholar
Ogilvie, R.L. et al. Tristetraprolin down-regulates IL-2 gene expression through AU-rich element-mediated mRNA decay. J. Immunol.174, 953–961 (2005). ArticleCASPubMed Google Scholar
Shi, L., Godfrey, W., Lin, J., Zhao, G. & Kao, P. NF90 regulates inducible IL-2 gene expression in T cells. J. Exp. Med.204, 971–977 (2007). ArticleCASPubMedPubMed Central Google Scholar
Stoecklin, G., Ming, X.F., Looser, R. & Moroni, C. Somatic mRNA turnover mutants implicate tristetraprolin in the interleukin-3 mRNA degradation pathway. Mol. Cell. Biol.20, 3753–3763 (2000). ArticleCASPubMedPubMed Central Google Scholar
Yarovinsky, T.O., Butler, N.S., Monick, M.M. & Hunninghake, G.W. Early exposure to IL-4 stabilizes IL-4 mRNA in CD4+ T cells via RNA-binding protein HuR. J. Immunol.177, 4426–4435 (2006). ArticleCASPubMed Google Scholar
Neininger, A. et al. 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). ArticleCASPubMed Google Scholar
Paschoud, S. et al. Destabilization of interleukin-6 mRNA requires a putative RNA stem-loop structure, an AU-rich element, and the RNA-binding protein AUF1. Mol. Cell. Biol.26, 8228–8241 (2006). ArticleCASPubMedPubMed Central Google Scholar
Winzen, R. et al. 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). ArticleCASPubMedPubMed Central Google Scholar
Bamba, S. et al. Regulation of IL-11 expression in intestinal myofibroblasts: role of c-Jun AP-1- and MAPK-dependent pathways. Am. J. Physiol. Gastrointest. Liver Physiol.285, G529–G538 (2003). ArticleCASPubMed Google Scholar
Carballo, E., Lai, W.S. & Blackshear, P.J. Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony-stimulating factor messenger RNA deadenylation and stability. Blood95, 1891–1899 (2000). ArticleCASPubMed Google Scholar
Grosset, C. et al. In vivo studies of translational repression mediated by the granulocyte-macrophage colony-stimulating factor AU-rich element. J. Biol. Chem.279, 13354–13362 (2004). ArticleCASPubMed Google Scholar
Putland, R.A. et al. RNA destabilization by the granulocyte colony-stimulating factor stem-loop destabilizing element involves a single stem-loop that promotes deadenylation. Mol. Cell. Biol.22, 1664–1673 (2002). ArticleCASPubMedPubMed Central Google Scholar
Whittemore, L.A. & Maniatis, T. Postinduction turnoff of β-interferon gene expression. Mol. Cell. Biol.10, 1329–1337 (1990). CASPubMedPubMed Central Google Scholar
Mavropoulos, A., Sully, G., Cope, A.P. & Clark, A.R. Stabilization of IFN-γ mRNA by MAPK p38 in IL-12- and IL-18-stimulated human NK cells. Blood105, 282–288 (2005). ArticleCASPubMed Google Scholar