Regulation of the Forkhead Transcription Factor AFX by Ral-Dependent Phosphorylation of Threonines 447 and 451

REFERENCES

• Borkhardt, A., R. Repp, O. A. Haas, T. Leis, J. Harbott, J. Kreuder, J. Hammermann, T. Henn, and F. Lampert. 1997. Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemias with a t(X;11)(q13;q23). Oncogene 14:195–202.
   PubMed Web of Science ®Google Scholar
• Bos, J. L.. 1998. All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral. EMBO J. 17:6776–6782.
   PubMed Web of Science ®Google Scholar
• Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110–149.
   PubMed Web of Science ®Google Scholar
• Brownawell, A. M., G. J. Kops, I. G. Macara, and B. M. Burgering. 2001. Inhibition of nuclear import by protein kinase B (AKT) regulates the subcellular distribution and activity of the Forkhead transcription factor AFX. Mol. Cell. Biol. 21:3534–3546.
   PubMedGoogle Scholar
• Burgering, B. M., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599–602.
   PubMed Web of Science ®Google Scholar
• Cantor, S. B., T. Urano, and L. A. Feig. 1995. Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases. Mol. Cell. Biol. 15:4578–4584.
   PubMed Web of Science ®Google Scholar
• de Ruiter, N. D., R. M. Wolthuis, H. van Dam, B. M. Burgering, and J. L. Bos. 2000. Ras-dependent regulation of c-Jun phosphorylation is mediated by the Ral guanine nucleotide exchange factor-Ral pathway. Mol. Cell. Biol. 20:8480–8488.
   PubMedGoogle Scholar
• Exton, J. H.. 1997. New developments in phospholipase D. J. Biol. Chem. 272:15579–15582.
   PubMedGoogle Scholar
• Feig, L. A., T. Urano, and S. Cantor. 1996. Evidence for a Ras/Ral signaling cascade. Trends Biochem. Sci. 21:438–441.
   PubMed Web of Science ®Google Scholar
• Fox, J. W., E. D. Lamperti, Y. Z. Eksioglu, S. E. Hong, Y. Feng, D. A. Graham, I. E. Scheffer, W. B. Dobyns, B. A. Hirsch, R. A. Radtke, S. F. Berkovic, P. R. Huttenlocher, and C. A. Walsh. 1998. Mutations in filamin 1 prevent migration of cerebral cortical neurons in human periventricular heterotopia. Neuron 21:1315–1325.
   PubMed Web of Science ®Google Scholar
• Frankel, P., M. Ramos, J. Flom, S. Bychenok, T. Joseph, E. Kerkhoff, U. R. Rapp, L. A. Feig, and D. A. Foster. 1999. Ral and Rho-dependent activation of phospholipase D in v-Raf-transformed cells. Biochem. Biophys. Res. Commun. 255:502–507.
   PubMedGoogle Scholar
• Goi, T., M. Shipitsin, Z. Lu, D. A. Foster, S. G. Klinz, and L. A. Feig. 2000. An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity. EMBO J. 19:623–630.
   PubMedGoogle Scholar
• Henry, D. O., S. A. Moskalenko, K. J. Kaur, M. Fu, R. G. Pestell, J. H. Camonis, and M. A. White. 2000. Ral GTPases contribute to regulation of cyclin D1 through activation of NF-κB. Mol. Cell. Biol. 20:8084–8092.
   PubMed Web of Science ®Google Scholar
• Jiang, H., J. Q. Luo, T. Urano, P. Frankel, Z. Lu, D. A. Foster, and L. A. Feig. 1995. Involvement of Ral GTPase in v-Src-induced phospholipase D activation. Nature 378:409–412.
   PubMed Web of Science ®Google Scholar
• Jullien-Flores, V., O. Dorseuil, F. Romero, F. Letourneur, S. Saragosti, R. Berger, A. Tavitian, G. Gacon, and J. H. Camonis. 1995. Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J. Biol. Chem. 270:22473–22477.
   PubMed Web of Science ®Google Scholar
• Kauffmann-Zeh, A., P. Rodriguez-Viciana, E. Ulrich, C. Gilbert, P. Coffer, J. Downward, and G. Evan. 1997. Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB. Nature 385:544–548.
   PubMed Web of Science ®Google Scholar
• Kops, G. J., and B. M. Burgering. 1999. Forkhead transcription factors: new insights into protein kinase B (c-akt) signaling. J. Mol. Med. 77:656–665.
   PubMed Web of Science ®Google Scholar
• Kops, G. J., N. D. de Ruiter, A. M. De Vries-Smits, D. R. Powell, J. L. Bos, and B. M. Burgering. 1999. Direct control of the Forkhead transcription factor AFX by protein kinase B. Nature 398:630–634.
   PubMed Web of Science ®Google Scholar
• Lu, Z., A. Hornia, T. Joseph, T. Sukezane, P. Frankel, M. Zhong, S. Bychenok, L. Xu, L. A. Feig, and D. A. Foster. 2000. Phospholipase D and RalA cooperate with the epidermal growth factor receptor to transform 3Y1 rat fibroblasts. Mol. Cell. Biol. 20:462–467.
   PubMedGoogle Scholar
• Luo, J. Q., X. Liu, S. M. Hammond, W. C. Colley, L. A. Feig, M. A. Frohman, A. J. Morris, and D. A. Foster. 1997. RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1. Biochem. Biophys. Res. Commun. 235:854–859.
   PubMedGoogle Scholar
• Medema, R. H., G. J. Kops, J. L. Bos, and B. M. Burgering. 2000. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature 404:782–787.
   PubMed Web of Science ®Google Scholar
• Medema, R. H., R. Wubbolts, and J. L. Bos. 1991. Two dominant inhibitory mutants of p21ras interfere with insulin-induced gene expression. Mol. Cell. Biol. 11:5963–5967.
   PubMed Web of Science ®Google Scholar
• Ohta, Y., N. Suzuki, S. Nakamura, J. H. Hartwig, and T. P. Stossel. 1999. The small GTPase RalA targets filamin to induce filopodia. Proc. Natl. Acad. Sci. USA 96:2122–2128.
   PubMed Web of Science ®Google Scholar
• Olson, M. F., H. F. Paterson, and C. J. Marshall. 1998. Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1. Nature 394:295–299.
   PubMed Web of Science ®Google Scholar
• Reedquist, K. A., T. Fukazawa, G. Panchamoorthy, W. Y. Langdon, S. E. Shoelson, B. J. Druker, and H. Band. 1996. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J. Biol. Chem. 271:8435–8442.
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., H. F. Paterson, M. Noble, and H. Land. 1988. Ras-mediated cell cycle arrest is altered by nuclear oncogenes to induce Schwann cell transformation. EMBO J. 7:1635–1645.
   PubMedGoogle Scholar
• Rodriguez-Viciana, P., P. H. Warne, A. Khwaja, B. M. Marte, D. Pappin, P. Das, M. D. Waterfield, A. Ridley, and J. Downward. 1997. Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell 89:457–467.
   PubMed Web of Science ®Google Scholar
• Serrano, M., A. W. Lin, M. E. McCurrach, D. Beach, and S. W. Lowe. 1997. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88:593–602.
   PubMed Web of Science ®Google Scholar
• Sewing, A., B. Wiseman, A. C. Lloyd, and H. Land. 1997. High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1. Mol. Cell. Biol. 17:5588–5597.
   PubMed Web of Science ®Google Scholar
• Unterman, T. G., A. Fareeduddin, M. A. Harris, R. G. Goswami, A. Porcella, R. H. Costa, and R. G. Lacson. 1994. Hepatocyte nuclear factor-3 (HNF-3) binds to the insulin response sequence in the IGF binding protein-1 (IGFBP-1) promoter and enhances promoter function. Biochem. Biophys. Res. Commun. 203:1835–1841.
   PubMed Web of Science ®Google Scholar
• Urano, T., R. Emkey, and L. A. Feig. 1996. Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation. EMBO J. 15:810–816.
   PubMed Web of Science ®Google Scholar
• van Weering, D. H., T. C. Moen, I. Braakman, P. D. Baas, and J. L. Bos. 1998. Expression of the receptor tyrosine kinase Ret on the plasma membrane is dependent on calcium. J. Biol. Chem. 273:12077–12081.
   PubMedGoogle Scholar
• Verheijen, M. H., R. M. Wolthuis, L. H. Defize, J. den Hertog, and J. L. Bos. 1999. Interdependent action of RalGEF and Erk in Ras-induced primitive endoderm differentiation of F9 embryonal carcinoma cells. Oncogene 18:4435–4439.
   PubMedGoogle Scholar
• White, M. A., T. Vale, J. H. Camonis, E. Schaefer, and M. H. Wigler. 1996. A role for the Ral guanine nucleotide dissociation stimulator in mediating Ras-induced transformation. J. Biol. Chem. 271:16439–16442.
   PubMed Web of Science ®Google Scholar
• Wolthuis, R. M., and J. L. Bos. 1999. Ras caught in another affair: the exchange factors for Ral. Curr. Opin. Genet. Dev. 9:112–117.
   PubMed Web of Science ®Google Scholar
• Wolthuis, R. M., N. D. de Ruiter, R. H. Cool, and J. L. Bos. 1997. Stimulation of gene induction and cell growth by the Ras effector Rlf. EMBO J. 16:6748–6761.
   PubMed Web of Science ®Google Scholar
• Wolthuis, R. M., F. Zwartkruis, T. C. Moen, and J. L. Bos. 1998. Ras-dependent activation of the small GTPase Ral. Curr. Biol. 8:471–474.
   PubMed Web of Science ®Google Scholar
• Woods, D., D. Parry, H. Cherwinski, E. Bosch, E. Lees, and M. McMahon. 1997. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1. Mol. Cell. Biol. 17:5598–5611.
   PubMed Web of Science ®Google Scholar