Inhibition of NF-κB Activity by IκBβ in Association with κB-Ras

REFERENCES

• Attar, R. M., Macdonald-Bravo H., Raventos-Suarez C., Durham S. K., and Bravo R.. 1998. Expression of constitutively active IκBβ in T cells of transgenic mice: persistent NF-κB activity is required for T-cell immune responses. Mol. Cell. Biol. 18:477–487.
   PubMedGoogle Scholar
• Baldwin, A. S. 1996. The NF-kappaB and IkappaB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649–683.
   PubMed Web of Science ®Google Scholar
• Bitko, V., and Barik S.. 1998. Persistent activation of RelA by respiratory syncytial virus involves protein kinase C, underphosphorylated IκBβ, and sequestration of protein phosphatase 2A by the viral phosphoprotein. J. Virol. 72:5610–5618.
   PubMedGoogle Scholar
• Blackwell, T. S., Stecenko A. A., and Christman J. W.. 2001. Dysregulated NF-kappaB activation in cystic fibrosis: evidence for a primary inflammatory disorder. Am. J. Physiol. 281:L69–L70.
   PubMed Web of Science ®Google Scholar
• Boguski, M. S., and McCormick F.. 1993. Proteins regulating ras and its relatives. Nature 366:643–654.
   PubMed Web of Science ®Google Scholar
• Bourne, H. R., Sanders D. A., and McCormick F.. 1990. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348:125–132.
   PubMed Web of Science ®Google Scholar
• Brummelkamp, T. R., Bernards R., and Agami R.. 2002. A system for stable expression of short interfering RNAs in mammalian cells. Science 296:550–553.
   PubMed Web of Science ®Google Scholar
• Chen, Y., Wu J., and Ghosh G.. 2003. κB-Ras binds to the unique insert within the ankyrin repeat domain of Ikappa Bbeta and regulates cytoplasmic retention of Ikappa Bbeta/NF-kappa B complexes. J. Biol. Chem. 278:23101–23106.
   PubMed Web of Science ®Google Scholar
• Claudio, E., Brown K., Park S., Wang H., and Siebenlist U.. 2002. BAFF-induced NEMO-independent processing of NF-kB2 in maturing B cells. Nat. Immunol. 3:958–965.
   PubMed Web of Science ®Google Scholar
• DeLuca, C., Petropoulos L., Zmeureanu D., and Hiscott J.. 1999. Nuclear IkappaBbeta maintains persistent NF-kappaB activation in HIV-1-infected myeloid cells. J. Biol. Chem. 274:13010–13016.
   PubMed Web of Science ®Google Scholar
• Elbashir, S. M., Harborth J., Lendeckel W., Yalcin A., Weber K., and Tuschl T.. 2001. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411:494–498.
   PubMed Web of Science ®Google Scholar
• Elbashir, S. M., Lendeckel W., and Tuschl T.. 2001. RNA interference is mediated by 21- and 22-nucleotide RNAs. Genes Dev. 15:188–200.
   PubMed Web of Science ®Google Scholar
• Erdman, R. A., Shellenberger K. E., Overmeyer J. H., and Maltese W. A.. 2000. Rab24 is an atypical member of the Rab GTPase family: deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells. J. Biol. Chem. 275:3848–3856.
   PubMedGoogle Scholar
• Fenwick, C., Na S.-Y., Voll R. E., Zhong H., Im S.-Y., Lee J. W., and Ghosh S.. 2000. A subclass of Ras proteins that regulate the degradation of IkappaB. Science 287:869–873.
   PubMed Web of Science ®Google Scholar
• Geisler, R., Bergmann A., Hiromi Y., and Nuesslein-Volhard C.. 1992. cactus, a gene involved in dorsoventral pattern formation of Drosophila, is related to the IkappaB gene family of vertebrates. Cell 71:613–621.
   PubMed Web of Science ®Google Scholar
• Ghosh, S., and Karin M.. 2002. Missing pieces in the NF-kappaB puzzle. Cell 109:S81–S96.
   PubMed Web of Science ®Google Scholar
• Ghosh, S., May M. J., and Kopp E. B.. 1998. NF-kappaB and Rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16:225–260.
   PubMed Web of Science ®Google Scholar
• Harhaj, E. W., Maggirwar S. B., Good L., and Sun S.-C.. 1996. CD28 mediates a potent costimulatory signal for rapid degradation of IκBβ which is associated with accelerated activation of various NF-κB/Rel heterodimers. Mol. Cell. Biol. 16:6736–6743.
   PubMedGoogle Scholar
• Hiscott, J., Kwon H., and Genin P.. 2001. Hostile takeovers: viral appropriation of the NF-kappaB pathway. J. Clin. Investig. 107:143–151.
   PubMed Web of Science ®Google Scholar
• Huxford, T., Malek S., and Ghosh G.. 2000. Preparation and crystallization of dynamic NF-kappa B · IkappaB complexes. J. Biol. Chem. 275:32800–32806.
   PubMedGoogle Scholar
• John, J., Sohmen R., Feuerstein J., Linke R., Wittinghofer A., and Goody R. S.. 1990. Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. Biochemistry 29:6058–6065.
   PubMedGoogle Scholar
• Johnson, D. R., Douglas I., Jahnke A., Ghosh S., and Pober J. S.. 1996. A sustained reduction in I-kappa-B-beta may contribute to persistent NF-kappa-B activation in human endothelial cells. J. Biol. Chem. 271:16317–16322.
   PubMedGoogle Scholar
• Karin, M., and Ben-Neriah Y.. 2000. Phosphorylation meets ubiquitination: the control of NF-kappaB activity. Annu. Rev. Immunol. 18:621–663.
   PubMed Web of Science ®Google Scholar
• Kidd, S. 1992. Characterization of the Drosophila cactus locus and analysis of interactions between cactus and dorsal proteins. Cell 71:623–635.
   PubMed Web of Science ®Google Scholar
• Malek, S., Chen Y., Huxford T., and Ghosh G.. 2001. IkappaBbeta, but not IkappaBalpha, functions as a classical cytoplasmic inhibitor of NF-kappaB dimers by masking both NF-kappaB nuclear localization sequences in resting cells. J. Biol. Chem. 276:45225–45235.
   PubMed Web of Science ®Google Scholar
• Malek, S., Huang D. B., Huxford T., Ghosh S., and Ghosh G.. 2003. X-ray crystal structure of an Ikappa Bbeta/NF-kappa B p65 homodimer complex. J. Biol. Chem. 278:23094–23100.
   PubMedGoogle Scholar
• Montaner, S., Perona R., Saniger L., and Lacal J. C.. 1998. Multiple signalling pathways lead to the activation of the nuclear factor kappaB by the Rho family of GTPases. J. Biol. Chem. 273:12779–12785.
   PubMedGoogle Scholar
• Nobes, C. D., Lauritzen I., Mattei M.-G., Paris S., Hall A., and Chardin P.. 1998. A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion. J. Cell Biol. 141:187–197.
   PubMed Web of Science ®Google Scholar
• Palmer, G. H., Machado J., Fernandez P., Heussler V., Perinat T., and Dobbelaere D. A. E.. 1997. Parasite-mediated nuclear factor kappaB regulation in lymphoproliferation caused by Theileria parva infection. Proc. Natl. Acad. Sci. USA 94:12527–12532.
   PubMedGoogle Scholar
• Perona, R., Montaner S., Saniger L., Sanchez-Perez I., Bravo R., and Lacal J. C.. 1997. Activation of the nuclear factor-kappa-B by Rho, CDC42, and Rac-1 proteins. Genes Dev. 11:463–475.
   PubMed Web of Science ®Google Scholar
• Schmidt, C., Peng B., Li Z., Sclabas G. M., Fujioka S., Niu J., Schmidt-Supprian M., Evans D. B., Abbruzzese J. L., and Chiao P. J.. 2003. Mechanisms of proinflammatory cytokine-induced biphasic NF-kappaB activation. Mol. Cell 12:1287–1300.
   PubMed Web of Science ®Google Scholar
• Senftleben, U., Cao Y., Xiao G., Greten F. R., Krahn G., Bonizzi G., Chen Y., Hu Y., Fong A., Sun S.-C., and Karin M.. 2001. Activation by IKKalpha of a second, evolutionary conserved, NF-kappaB signaling pathway. Science 293:1495–1499.
   PubMed Web of Science ®Google Scholar
• Stecenko, A. A., King G., Torii K., Breyer R. M., Dworski R., Blackwell T. S., Christman J. W., and Brigham K. L.. 2001. Dysregulated cytokine production in human cystic fibrosis bronchial epithelial cells. Inflammation 25:145–155.
   PubMed Web of Science ®Google Scholar
• Tam, W. F., and Sen R.. 2001. IkappaB family members function by different mechanisms. J. Biol. Chem. 276:7701–7704.
   PubMedGoogle Scholar
• Thompson, J. E., Phillips R. J., Erdjument-Bromage H., Tempst P., and Ghosh S.. 1995. I-kappa-B-beta regulates the persistent response in a biphasic activation of NF-kappa-B. Cell 80:573–582.
   PubMed Web of Science ®Google Scholar
• Tran, K., Merika M., and Thanos D.. 1997. Distinct functional properties of IκBα and IκBβ. Mol. Cell. Biol. 17:5386–5399.
   PubMedGoogle Scholar
• Tucker, J., Sczakiel G., Feuerstein J., John J., Goody R. S., and Wittinghofer A.. 1986. Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site. EMBO J. 5:1351–1358.
   PubMedGoogle Scholar
• Verma, I. M., Stevenson K., Schwarz E. W., Van Antwerp D., and Miyamoto S.. 1995. Rel/NF-kappa-B/I-kappa-B family: intimate tales of association and dissociation. Genes Dev. 9:2723–2735.
   PubMed Web of Science ®Google Scholar
• Vetter, I. R., and Wittinghofer A.. 2001. The guanine nucleotide-binding switch in three dimensions. Science 294:1299–1304.
   PubMed Web of Science ®Google Scholar
• Xiao, G., Harhaj E. W., and Sun S.-C.. 2001. NF-kappaB-inducing kinase regulates the processing of NF-kappaB2 p100. Mol. Cell 7:401–409.
   PubMed Web of Science ®Google Scholar
• Zhou, X.-Y., Yashiro-Ohtani Y., Nakahira M., Park W. R., Abe R., Hamaoka T., Naramura M., Gu H., and Fujiwara H.. 2002. Molecular mechanism underlying differential contribution of CD28 versus non-CD28 costimulatory molecules to IL-2 promoter activation. J. Immunol. 168:3847–3854.
   PubMed Web of Science ®Google Scholar