Antisense Rescue Defines Specialized and Generalized Functional Domains for c-Fos Protein

REFERENCES

• Abate, C., D. Luk, and T. Curran. 1991. Transcriptional regulation by Fos and Jun in vitro: interaction among multiple activator and regulatory domains. Mol. Cell. Biol. 11:3624–3632.
   PubMedGoogle Scholar
• Angel, P., K. Hattori, T. Smeal, and M. Karin. 1988. The Jun proto-oncogene is positively autoregulated by its product, Jun AP-1. Cell 55:875–885.
   PubMed Web of Science ®Google Scholar
• Ballard, D. W., W. H. Walker, S. Doerre, P. Sista, J. A. Mollitor, E. P. Dixon, N. J. Peffer, M. Hannick, and W. C. Greene. 1990. The v-rel oncogene encodes a κB enhancer binding protein that inhibits NF-κB function. Cell 63:803–814.
   PubMed Web of Science ®Google Scholar
• Blanar, M. A., and W. J. Rutter. 1992. Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-fos. Science 256:1014–1018.
   PubMedGoogle Scholar
• Chiu, R., W. J. Boyle, J. Meek, T. Smeal, T. Hunter, and M. Karin. 1988. The c-fos protein interacts with c-jun/AP-1 to stimulate transcription of AP-1 responsive genes. Cell 54:541–552.
   PubMed Web of Science ®Google Scholar
• Cohen, D. R., and T. Curran. 1988. Fra-1: a serum-inducible cellular immediate early gene that encodes a fos-related antigen. Mol. Cell. Biol. 8:2063–2069.
   PubMed Web of Science ®Google Scholar
• Damm, K., C. C. Thompson, and R. M. Evans. 1989. Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature (London) 339:593–597.
   PubMed Web of Science ®Google Scholar
• Diamond, M. I., J. N. Miner, S. K. Yoshinaga, and K. R. Yamamoto. 1990. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science 249:1266–1272.
   PubMed Web of Science ®Google Scholar
• Field, S., R. S. Johnson, R. Mortenson, V. E. Papaioannou, B. M. Spiegelman, and M. E. Greenberg. 1992. Fos is not required for the growth or differentiation of ES cells. Proc. Natl. Acad. Sci. USA 89:9306–9310.
   PubMedGoogle Scholar
• Franza, R. B., Jr., F. J. Rauscher III, S. F. Josephs, and T. Curran. 1988. The fos complex and fos-related antigens recognize sequence elements that contain AP-1 binding sites. Science 239:1150–1153.
   PubMed Web of Science ®Google Scholar
• Gentz, R., F. J. Rauscher III, C. Abate, and T. Curran. 1989. Parallel association of fos and jun leucine zippers juxtaposes DNA binding domains. Science 243:1695–1699.
   PubMed Web of Science ®Google Scholar
• Gius, D., X. Cao, F. J. Rauscher III, D. R. Cohen, T. Curran, and V. P. Sukhatme. 1990. Transcriptional activation and repression by Fos are independent functions: the C terminus represses immediate early gene expression via CarG elements. Mol. Cell. Biol. 10:4243–4255.
   PubMed Web of Science ®Google Scholar
• Hai, T., and T. Curran. 1991. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad. Sci. USA 88:3720–3724.
   PubMed Web of Science ®Google Scholar
• Holt, J. T., T. V. Gopal, A. D. Moulton, and A. W. Nienhuis. 1986. Inducible production of c-fos anti-sense RNA inhibits 3T3 cell proliferation. Proc. Natl. Acad. Sci. USA 83:4794–4798.
   PubMed Web of Science ®Google Scholar
• Inoue, J.-L, L. D. Kerr, L. J. Ransone, E. Bengal, T. Hunter, and I. M. Verma. 1991. c-rel activates but v-rel suppresses transcription from κB sites. Proc. Natl. Acad. Sci. USA 88:3715–3719.
   PubMedGoogle Scholar
• Jenuwein, T., and R. Müller. 1987. Structure-function analysis of fos protein: a single amino acid change activates the immortalizing potential of v-fos. Cell 48:647–657.
   PubMedGoogle Scholar
• Johnson, R. S., B. M. Spiegelman, and V. Papaioannou. 1992. Pleiotropic effects of a null mutation in the c-fos proto-oncogene. Cell 71:577–586.
   PubMed Web of Science ®Google Scholar
• Jonat, G., H. J. Rahmsdorf, K. K. Park, A. C. B Cato, S. Gebel, H. Ponta, and P. Herrlich. 1990. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos-Jun) activity by glucocorticoid hormone. Cell 62:1189–1204.
   PubMed Web of Science ®Google Scholar
• Kamata, N., and J. T. Holt. 1992. Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein. Mol. Cell. Biol. 12:876–882.
   PubMedGoogle Scholar
• Kamata, N., R. M. Jotte, and J. T. Holt. 1991. Myristylation alters DNA binding and transactivation of FBR (Gag-Fos) protein. Mol. Cell. Biol. 11:765–772.
   PubMedGoogle Scholar
• Kerppola, T. K., and T. Curran. 1991. Fos-Jun heterodimers and Jun homdimers bend DNA in opposite orientations: implications for transcription factor cooperativity. 66:317–326.
   Google Scholar
• Kerr, L. D., J. T. Holt, and L. M. Matrisian. 1988. Growth factors regulate transin gene expression by c-fos dependent and c-fos independent pathways. Science 242:1424–1427.
   PubMed Web of Science ®Google Scholar
• Kim, S.-J., F. Denhez, K.-Y. Kim, J. T. Holt, M. B. Sporn, and A. B. Roberts. 1989. Activation of the second promoter of the TGF-betal gene by TGF-betal and phorbol ester occurs through the same target sequences. J. Biol. Chem. 264:19373–19378.
   PubMed Web of Science ®Google Scholar
• Konig, H., H. Ponta, U. Rahmsdorf, M. Buscher, A. Schonthal, H. J. Rahmsdorf, and P. Herrlich. 1989. Autoregulation of fos: the dyad symmetry element as the major target of repression. EMBO J. 8:2559–2566.
   PubMedGoogle Scholar
• Kovary, K., and R. Bravo. 1991. The Jun and Fos protein families are both required for cell cycle progression in fibroblasts. Mol. Cell. Biol. 11:4466–4472.
   PubMed Web of Science ®Google Scholar
• Landshulz, P., F. Johnson, and S. L. McKnight. 1988. The leucine zipper: a hypothetical structure common to a new class of DNA binding protein. Nature (London) 240:1759–1764.
   Google Scholar
• Lucibello, F. C., C. Lowag, M. Neuberg, and R. Müller. 1989. Transrepression of the mouse c-fos promoter: a novel mechanism of fos-mediated transregulation. Cell 49:741–752.
   Google Scholar
• Macgregor, P. F., C. Abate, and T. Curran. 1990. Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene 5:451–458.
   PubMed Web of Science ®Google Scholar
• Meijlink, F., T. Curran, A. D. Miller, and I. M. Verma. 1985. Removal of a 67 base pair sequence in the noncoding region of proto-oncogene fos converts it to a transforming gene. Proc. Natl. Acad. Sci. USA 82:4987–4991.
   PubMed Web of Science ®Google Scholar
• Nakabeppu, Y., and D. Nathans. 1991. A naturally occurring form of FosB that inhibits Fos/Jun transcriptional activity. Cell 64:751–759.
   PubMed Web of Science ®Google Scholar
• Nakabeppu, Y., K. Ryder, and D. Nathans. 1988. DNA binding activities of three murine jun proteins: stimulation by fos. Cell 55:907–915.
   PubMed Web of Science ®Google Scholar
• Nishikura, K., and J. M. Murray. 1987. Antisense RNA of proto-oncogene c-fos blocks renewed growth of quiescent 3T3 cells. Mol. Cell. Biol. 7:639–649.
   PubMed Web of Science ®Google Scholar
• Nishizawa, M., N. Goto, and S. Kawai. 1987. An avian transforming retrovirus isolated from a nephroblastoma that carries the fos gene as the oncogene. J. Virol. 61:3733–3740.
   PubMed Web of Science ®Google Scholar
• Ofir, R., V. J. Dwarki, D. Rashid, and I. M. Verma. 1990. Phosphorylation of the C-terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter. Nature (London) 348:80–82.
   PubMedGoogle Scholar
• O’Shea, E. K., R. Rutkowski, and P. S. Kim. 1989. Evidence that the leucine zipper is a coiled coil. Science 243:538–542.
   PubMed Web of Science ®Google Scholar
• Rauscher, F. J.III, L. C. Sambucetti, T. Curran, R. J. Distel, and B. M. Speigelman. 1988. Common DNA binding site for fos protein complexes and transcription factor AP-1. Cell 52:471–480.
   PubMed Web of Science ®Google Scholar
• Rauscher, F. J. III, P. J. Voulalas, B. R. Franza, and T. Curran. 1988. Fos and Jun bind cooperatively to the AP-1 site: reconstitution in vitro. Genes Dev. 2:1687–1699.
   PubMedGoogle Scholar
• Riabowol, K. T., R. J. Vosatka, E. B. Ziff, N. J. Lamb, and J. R. Feramisco. 1988. Microinjection of fos-specific antibodies blocks DNA synthesis in fibroblast cells. Mol. Cell. Biol. 8:1670–1676.
   PubMed Web of Science ®Google Scholar
• Rivera, V. M., M. Sheng, and M. E. Greenberg. 1990. The inner core of the serum response element mediates both the rapid induction and subsequent repression of c-fos transcription following serum stimulation. Genes Dev. 4:255–268.
   PubMedGoogle Scholar
• Robinson-Benion, C., N. Kamata, and J. T. Holt. 1991. Antisense mapping of the c-fos promoter: role of the serum response element. Antisense Res. Dev. 1:21–33.
   PubMedGoogle Scholar
• Sassone-Corsi, P., W. W. Lamph, M. Kamps, and I. M. Verma. 1988. Fos associated cellular p39 is related to nuclear transcription factor AP-1. Cell 54:553–560.
   PubMed Web of Science ®Google Scholar
• Sassone-Corsi, P., J. C. Sisson, and I. M. Verma. 1988. Transcriptional autoregulation of the protooncogene fos. Nature (London) 334:314–319.
   PubMed Web of Science ®Google Scholar
• Schönthal, A., P. Herrlich, Rahmsdorf, and H. Ponta. 1988. Requirement for fos gene expression in the transcriptional activation of collagenase by other oncogenes and phorbol esters. Cell 54:325–334.
   PubMed Web of Science ®Google Scholar
• Schüle, R., P. Rangarajan, S. Kliewer, L. J. Ransone, J. Bolado, N. Yang, I. M. Verma, and R. M. Evans. 1990. Functional antagonism between oncoprotein c-jun and the glucocorticoid receptor. Cell 62:1217–1226.
   PubMed Web of Science ®Google Scholar
• Schutte, J., J. D. Minna, and M. J. Birrer. 1989. Deregulated expression of human c-jun transforms primary rat embryo cells in cooperation with an activated c-Ha-ras gene and transforms Rat-la cells as a single gene. Proc. Natl. Acad. Sci. USA 86:2257–2261.
   PubMed Web of Science ®Google Scholar
• Shaw, P. E., S. Frisch, and A. Nordheim. 1989. Repression of c-fos transcription is mediated through p67SRF bound to the SRE. EMBO J. 8:2567–2574.
   PubMedGoogle Scholar
• Shaw, P. E., H. Schroter, and A. Nordheim. 1989. The ability of a ternary complex to form over the serum response element correlates with serum inducibility of the human c-fos promoter. Cell 56:563–572.
   PubMed Web of Science ®Google Scholar
• Sonnenberg, J. L., F. J. Rauscher III, J. I. Morgan, and T. Curran. 1989. Regulation of proenkephalin by Fos and Jun. Science 246:1622–1625.
   PubMed Web of Science ®Google Scholar
• Subramaniam, M., L. J. Schmidt, C. E. Crutchfield III, and M. J. Getz. 1989. Negative regulation of serum-responsive elements. Nature (London) 340:64–66.
   PubMedGoogle Scholar
• Turner, R., and R. Tjian. 1989. Leucine repeats and an adjacent DNA binding domain mediate the formation of functional c-fos c-jun heterodimers. Science 243:1689–1694.
   PubMed Web of Science ®Google Scholar
• Van Beveren, C., S. Enami, T. Curran, and I. M. Verma. 1984. FBR murine osteosarcoma virus. Virology 135:229–243.
   PubMed Web of Science ®Google Scholar
• Van Beveren, C., F. van Straaten, T. Curran, R. Müller, and I. M. Verma. 1983. Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals that viral and cellular fos gene products have different carboxy termini. Cell 32:1241–1255.
   PubMed Web of Science ®Google Scholar
• Wilson, T., and R. Treisman. 1988. Fos C-terminal mutations block downregulation of c-fos transcription following serum stimulation. EMBO J. 7:4193–4202.
   PubMedGoogle Scholar
• Yang-Yen, H. F., J. C. Chambard, Y. L. Sun, T. Smeal, T. J. Schmidt, J. Drouin, and M. Karin. 1990. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62:1205–1215.
   PubMed Web of Science ®Google Scholar
• Yen, J., R. M. Wisdom, I. Tratner, and I. M. Verma. 1991. An alternative spliced from of FosB is a negative regulator of transcriptional activation and transformation by Fos proteins. Proc. Natl. Acad. Sci. USA 88:5077–5081.
   PubMedGoogle Scholar
• Zenke, M., A. Muñoz, J. Sap, B. Vennström, and H. Beug. 1990. v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of v-erbA. Cell 61:1035–1042.
   PubMedGoogle Scholar
• Zerial, M., L. Toschi, R. P. Ryseck, M. Schuermann, R. Müller, and R. Bravo. 1989. The product of a novel growth factor activated gene fosB interacts with Jun proteins enhancing their DNA binding activity. EMBO J. 8:805–813.
   PubMed Web of Science ®Google Scholar