Interaction of Serum Response Factor (SRF) with the Elk-1 B Box Inhibits RhoA-Actin Signaling to SRF and Potentiates Transcriptional Activation by Elk-1

REFERENCES

• Arsenian, S., B. Weinhold, M. Oelgeschlager, U. Ruther, and A. Nordheim. 1998. Serum response factor is essential for mesoderm formation during mouse embryogenesis. EMBO J. 17: 6289–6299.
   PubMed Web of Science ®Google Scholar
• Arthur, J. S., and P. Cohen. 2000. MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells. FEBS Lett. 482: 44–48.
   PubMed Web of Science ®Google Scholar
• Cruzalegui, F. H., E. Cano, and R. Treisman. 1999. ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry. Oncogene 18: 7948–7957.
   PubMed Web of Science ®Google Scholar
• Dalton, S., and R. Treisman. 1992. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 68: 597–612.
   PubMed Web of Science ®Google Scholar
• De Cesare, D., S. Jacquot, A. Hanauer, and P. Sassone-Corsi. 1998. Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene. Proc. Natl. Acad. Sci. USA 95: 12202–12207.
   PubMed Web of Science ®Google Scholar
• Favata, M. F., K. Y. Horiuchi, E. J. Manos, A. J. Daulerio, D. A. Stradley, W. S. Feeser, D. E. Van Dyk, W. J. Pitts, R. A. Earl, F. Hobbs, R. A. Copeland, R. L. Magolda, P. A. Scherle, and J. M. Trzaskos. 1998. Identification of a novel inhibitor of mitogen-activated protein kinase kinase. J. Biol. Chem. 273: 18623–18632.
   PubMed Web of Science ®Google Scholar
• Fringer, J., and F. Grinnell. 2001. Fibroblast quiescence in floating or released collagen matrices: contribution of the ERK signaling pathway and actin cytoskeletal organization. J. Biol. Chem. 276: 31047–31052.
   PubMed Web of Science ®Google Scholar
• Geneste, O., J. Copeland, and R. Treisman. 2002. LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics. J. Cell Biol. 157: 831–838.
   PubMed Web of Science ®Google Scholar
• Gille, H., M. Kortenjann, O. Thomae, C. Moomaw, C. Slaughter, M. H. Cobb, and P. E. Shaw. 1995. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J. 14: 951–962.
   PubMed Web of Science ®Google Scholar
• Gille, H., A. D. Sharrocks, and P. E. Shaw. 1992. Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter. Nature 358: 414–417.
   PubMed Web of Science ®Google Scholar
• Gineitis, D., and R. Treisman. 2001. Differential usage of signal transduction pathways defines two types of serum response factor target gene. J. Biol. Chem. 276: 24531–24539.
   PubMed Web of Science ®Google Scholar
• Graham, R., and M. Gilman. 1991. Distinct protein targets for signals acting at the c-fos serum response element. Science 251: 189–192.
   PubMedGoogle Scholar
• Hassler, M., and T. J. Richmond. 2001. The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. EMBO J. 20: 3018–3028.
   PubMedGoogle Scholar
• Herrera, R. E., P. E. Shaw, and A. Nordheim. 1989. Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth factor induction. Nature 340: 68–70.
   PubMedGoogle Scholar
• Hill, C. S., R. Marais, S. John, J. Wynne, S. Dalton, and R. Treisman. 1993. Functional analysis of a growth factor-responsive transcription factor complex. Cell 73: 395–406.
   PubMed Web of Science ®Google Scholar
• Hill, C. S., and R. Treisman. 1995. Differential activation of c-fos promoter elements by serum, lysophosphatidic acid, G proteins and polypeptide growth factors. EMBO J. 14: 5037–5047.
   PubMed Web of Science ®Google Scholar
• Hill, C. S., J. Wynne, and R. Treisman. 1995. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81: 1159–1170.
   PubMed Web of Science ®Google Scholar
• Hill, C. S., J. Wynne, and R. Treisman. 1994. Serum-regulated transcription by serum response factor (SRF): a novel role for the DNA-binding domain. EMBO J. 13: 5421–5432.
   PubMedGoogle Scholar
• Janknecht, R., W. H. Ernst, V. Pingoud, and A. Nordheim. 1993. Activation of ternary complex factor Elk-1 by MAP kinases. EMBO J. 12: 5097–5104.
   PubMed Web of Science ®Google Scholar
• Janknecht, R., R. Zinck, W. H. Ernst, and A. Nordheim. 1994. Functional dissection of the transcription factor elk-1. Oncogene 9: 1273–1278.
   PubMedGoogle Scholar
• Kortenjann, M., O. Thomae, and P. E. Shaw. 1994. Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk 2. Mol. Cell. Biol. 14: 4815–4824.
   PubMed Web of Science ®Google Scholar
• Ling, Y., J. H. Lakey, C. E. Roberts, and A. D. Sharrocks. 1997. Molecular characterization of the B-box protein-protein interaction motif of the ETS-domain transcription factor Elk-1. EMBO J. 16: 2431–2440.
   PubMedGoogle Scholar
• Ling, Y., A. G. West, E. C. Roberts, J. H. Lakey, and A. D. Sharrocks. 1998. Interaction of transcription factors with serum response factor. Identification of the Elk-1 binding surface. J. Biol. Chem. 273: 10506–10514.
   PubMedGoogle Scholar
• Mack, C. P., A. V. Somlyo, M. Hautmann, A. P. Somlyo, and G. K. Owens. 2001. Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization. J. Biol. Chem. 276: 341–347.
   PubMed Web of Science ®Google Scholar
• Marais, R., J. Wynne, and R. Treisman. 1993. The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell 73: 381–393.
   PubMed Web of Science ®Google Scholar
• McMahon, S. B., and J. G. Monroe. 1995. A ternary complex factor-dependent mechanism mediates induction of egr-1 through selective serum response elements following antigen receptor cross-linking in B lymphocytes. Mol. Cell. Biol. 15: 1086–1093.
   PubMedGoogle Scholar
• Price, M. A., F. H. Cruzalegui, and R. H. Treisman. 1996. The p38 and ERK MAP kinase pathways cooperate to activate ternary complex factors and c-fos transcription in response to UV light. EMBO J. 15: 6552–6563.
   PubMedGoogle Scholar
• Price, M. A., A. E. Rogers, and R. Treisman. 1995. Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET). EMBO J. 14: 2589–2601.
   PubMed Web of Science ®Google Scholar
• Robertson, L. M., T. K. Kerppola, M. Vendrell, D. Luk, R. J. Smeyne, C. Bocchiaro, J. I. Morgan, and T. Curran. 1995. Regulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elements. Neuron 14: 241–252.
   PubMed Web of Science ®Google 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
• Shore, P., and A. D. Sharrocks. 1994. The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1. Mol. Cell. Biol. 14: 3283–3291.
   PubMedGoogle Scholar
• Sotiropoulos, A., D. Gineitis, J. Copeland, and R. Treisman. 1999. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 98: 159–169.
   PubMed Web of Science ®Google Scholar
• Tan, S., and T. J. Richmond. 1998. Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. Nature 391: 660–666.
   PubMedGoogle Scholar
• Tominaga, T., E. Sahai, P. Chardin, F. McCormick, S. A. Courtneidge, and A. S. Alberts. 2000. Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling. Mol. Cell 5: 13–25.
   PubMedGoogle Scholar
• Treisman, R. 1995. Journey to the surface of the cell: the SRE and c-fos regulation. EMBO J. 14: 4905–4913.
   PubMedGoogle Scholar
• Treisman, R. 1994. Ternary complex factors: growth factor regulated transcriptional activators. Curr. Opin. Genet. Dev. 4: 96–101.
   PubMedGoogle Scholar
• Treisman, R. 1985. Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences. Cell 42: 889–902.
   PubMed Web of Science ®Google Scholar
• Treisman, R., R. Marais, and J. Wynne. 1992. Spatial flexibility in ternary complexes between SRF and its accessory proteins. EMBO J. 11: 4631–4640.
   PubMedGoogle Scholar
• Yang, S. H., P. Shore, N. Willingham, J. H. Lakey, and A. D. Sharrocks. 1999. The mechanism of phosphorylation-inducible activation of the ETS-domain transcription factor Elk-1. EMBO J. 18: 5666–5674.
   PubMed Web of Science ®Google Scholar