Functional Interplay between Acetylation and Methylation of the RelA Subunit of NF-κB

REFERENCES

• Chen, L. F., and W. C. Greene. 2004. Shaping the nuclear action of NF-κB. Nat. Rev. Mol. Cell Biol. 5:392–401.
   PubMed Web of Science ®Google Scholar
• Chen, L. F., Y. Mu, and W. C. Greene. 2002. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-κB. EMBO J. 21:6539–6548.
   PubMed Web of Science ®Google Scholar
• Chen, L. F., S. A. Williams, Y. Mu, H. Nakano, J. M. Duerr, L. Buckbinder, and W. C. Greene. 2005. NF-kappaB RelA phosphorylation regulates RelA acetylation. Mol. Cell. Biol. 25:7966–7975.
   PubMed Web of Science ®Google Scholar
• Cheung, P., C. D. Allis, and P. Sassone-Corsi. 2000. Signaling to chromatin through histone modifications. Cell 103:263–271.
   PubMed Web of Science ®Google Scholar
• Cheung, P., K. G. Tanner, W. L. Cheung, P. Sassone-Corsi, J. M. Denu, and C. D. Allis. 2000. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5:905–915.
   PubMed Web of Science ®Google Scholar
• Choi, K. C., M. G. Jung, Y. H. Lee, J. C. Yoon, S. H. Kwon, H. B. Kang, M. J. Kim, J. H. Cha, Y. J. Kim, W. J. Jun, J. M. Lee, and H. G. Yoon. 2009. Epigallocatechin-3-gallate, a histone acetyltransferase inhibitor, inhibits EBV-induced B lymphocyte transformation via suppression of RelA acetylation. Cancer Res. 69:583–592.
   PubMed Web of Science ®Google Scholar
• Chuikov, S., J. K. Kurash, J. R. Wilson, B. Xiao, N. Justin, G. S. Ivanov, K. McKinney, P. Tempst, C. Prives, S. J. Gamblin, N. A. Barlev, and D. Reinberg. 2004. Regulation of p53 activity through lysine methylation. Nature 432:353–360.
   PubMed Web of Science ®Google Scholar
• Couture, J. F., E. Collazo, G. Hauk, and R. C. Trievel. 2006. Structural basis for the methylation site specificity of SET7/9. Nat. Struct. Mol. Biol. 13:140–146.
   PubMed Web of Science ®Google Scholar
• Duran, A., M. T. Diaz-Meco, and J. Moscat. 2003. Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation. EMBO J. 22:3910–3918.
   PubMed Web of Science ®Google Scholar
• Fingerman, I. M., H. N. Du, and S. D. Briggs. 2008. Controlling histone methylation via trans-histone pathways. Epigenetics 3:237–242.
   PubMed Web of Science ®Google Scholar
• Fischle, W., Y. Wang, and C. D. Allis. 2003. Histone and chromatin cross-talk. Curr. Opin. Cell Biol. 15:172–183.
   PubMed Web of Science ®Google Scholar
• Ghosh, S., and M. Karin. 2002. Missing pieces in the NF-kappaB puzzle. Cell 109 (Suppl.):S81–S96.
   PubMed Web of Science ®Google Scholar
• Gringhuis, S. I., J. den Dunnen, M. Litjens, B. van Het Hof, Y. van Kooyk, and T. B. Geijtenbeek. 2007. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 26:605–616.
   PubMed Web of Science ®Google Scholar
• Hoberg, J. E., A. E. Popko, C. S. Ramsey, and M. W. Mayo. 2006. IkappaB kinase alpha-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300. Mol. Cell. Biol. 26:457–471.
   PubMed Web of Science ®Google Scholar
• Hoffmann, A., A. Levchenko, M. L. Scott, and D. Baltimore. 2002. The IkappaB-NF-kappaB signaling module: temporal control and selective gene activation. Science 298:1241–1245.
   PubMed Web of Science ®Google Scholar
• Huang, B., X. D. Yang, M. M. Zhou, K. Ozato, and L. F. Chen. 2009. Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA. Mol. Cell. Biol. 29:1375–1387.
   PubMed Web of Science ®Google Scholar
• Ishinaga, H., H. Jono, J. H. Lim, S. M. Kweon, H. Xu, U. H. Ha, T. Koga, C. Yan, X. H. Feng, L. F. Chen, and J. D. Li. 2007. TGF-beta induces p65 acetylation to enhance bacteria-induced NF-kappaB activation. EMBO J. 26:1150–1162.
   PubMed Web of Science ®Google Scholar
• Ito, K., C. E. Charron, and I. M. Adcock. 2007. Impact of protein acetylation in inflammatory lung diseases. Pharmacol. Ther. 116:249–265.
   PubMed Web of Science ®Google Scholar
• Ivanov, G. S., T. Ivanova, J. Kurash, A. Ivanov, S. Chuikov, F. Gizatullin, E. M. Herrera-Medina, F. Rauscher III, D. Reinberg, and N. A. Barlev. 2007. Methylation-acetylation interplay activates p53 in response to DNA damage. Mol. Cell. Biol. 27:6756–6769.
   PubMed Web of Science ®Google Scholar
• Jenuwein, T., and C. D. Allis. 2001. Translating the histone code. Science 293:1074–1080.
   PubMed Web of Science ®Google Scholar
• Kurash, J. K., H. Lei, Q. Shen, W. L. Marston, B. W. Granda, H. Fan, D. Wall, E. Li, and F. Gaudet. 2008. Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo. Mol. Cell 29:392–400.
   PubMedGoogle Scholar
• Lee, H., A. Herrmann, J. H. Deng, M. Kujawski, G. Niu, Z. Li, S. Forman, R. Jove, D. M. Pardoll, and H. Yu. 2009. Persistently activated Stat3 maintains constitutive NF-kappaB activity in tumors. Cancer Cell 15:283–293.
   PubMed Web of Science ®Google Scholar
• Lo, W. S., L. Duggan, N. C. Emre, R. Belotserkovskya, W. S. Lane, R. Shiekhattar, and S. L. Berger. 2001. Snf1—a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293:1142–1146.
   PubMed Web of Science ®Google Scholar
• Lo, W. S., R. C. Trievel, J. R. Rojas, L. Duggan, J. Y. Hsu, C. D. Allis, R. Marmorstein, and S. L. Berger. 2000. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell 5:917–926.
   PubMed Web of Science ®Google Scholar
• MacKerell, A. D. J., D. Bashford, M. Bellott, R. L. Dunbrack, Jr., J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher III, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiórkiewicz-Kuczera, D. Yin, and M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102:3586–3616.
   PubMed Web of Science ®Google Scholar
• Natoli, G., and S. Chiocca. 2008. Nuclear ubiquitin ligases, NF-kappaB degradation, and the control of inflammation. Sci. Signal. 1:pe1.
   PubMedGoogle Scholar
• Nishioka, K., S. Chuikov, K. Sarma, H. Erdjument-Bromage, C. D. Allis, P. Tempst, and D. Reinberg. 2002. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:479–489.
   PubMed Web of Science ®Google Scholar
• Perkins, N. D. 2007. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 8:49–62.
   PubMed Web of Science ®Google Scholar
• Perkins, N. D. 2006. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 25:6717–6730.
   PubMed Web of Science ®Google Scholar
• Phillips, J. C., R. Braun, W. Wang, J. Gumbart, E. Tajkhorshid, E. Villa, C. Chipot, R. D. Skeel, L. Kale, and K. Schulten. 2005. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26:1781–1802.
   PubMed Web of Science ®Google Scholar
• Pruitt, K., R. L. Zinn, J. E. Ohm, K. M. McGarvey, S. H. Kang, D. N. Watkins, J. G. Herman, and S. B. Baylin. 2006. Inhibition of SIRT1 reactivates silenced cancer genes without loss of promoter DNA hypermethylation. PLoS Genet. 2:e40.
   PubMed Web of Science ®Google Scholar
• Sakurai, H., H. Chiba, H. Miyoshi, T. Sugita, and W. Toriumi. 1999. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J. Biol. Chem. 274:30353–30356.
   PubMed Web of Science ®Google Scholar
• Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368–379.
   PubMed Web of Science ®Google Scholar
• Shi, Y., and J. R. Whetstine. 2007. Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25:1–14.
   PubMed Web of Science ®Google Scholar
• Sims, R. J., III, and D. Reinberg. 2008. Is there a code embedded in proteins that is based on post-translational modifications? Nat. Rev. Mol. Cell Biol. 9:815–820.
   PubMed Web of Science ®Google Scholar
• Subramanian, K., D. Jia, P. Kapoor-Vazirani, D. R. Powell, R. E. Collins, D. Sharma, J. Peng, X. Cheng, and P. M. Vertino. 2008. Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase. Mol. Cell 30:336–347.
   PubMed Web of Science ®Google Scholar
• Suganuma, T., and J. L. Workman. 2008. Crosstalk among histone modifications. Cell 135:604–607.
   PubMed Web of Science ®Google Scholar
• Wang, D., S. D. Westerheide, J. L. Hanson, and A. S. Baldwin, Jr. 2000. Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J. Biol. Chem. 275:32592–32597.
   PubMed Web of Science ®Google Scholar
• Yang, S. R., J. Wright, M. Bauter, K. Seweryniak, A. Kode, and I. Rahman. 2007. Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging. Am. J. Physiol. Lung Cell. Mol. Physiol. 292:L567–L576.
   PubMed Web of Science ®Google Scholar
• Yang, X. D., B. Huang, M. Li, A. Lamb, N. L. Kelleher, and L. F. Chen. 2009. Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit. EMBO J. 28:1055–1066.
   PubMed Web of Science ®Google Scholar
• Yang, X. D., A. Lamb, and L. F. Chen. 2009. Methylation, a new epigenetic mark for protein stability. Epigenetics 4:429–433.
   PubMed Web of Science ®Google Scholar
• Yang, X. J., and E. Seto. 2008. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31:449–461.
   PubMed Web of Science ®Google Scholar
• Yeung, F., J. E. Hoberg, C. S. Ramsey, M. D. Keller, D. R. Jones, R. A. Frye, and M. W. Mayo. 2004. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23:2369–2380.
   PubMed Web of Science ®Google Scholar
• Zhang, K., and S. Y. Dent. 2005. Histone modifying enzymes and cancer: going beyond histones. J. Cell. Biochem. 96:1137–1148.
   PubMed Web of Science ®Google Scholar