RhoGEF Specificity Mutants Implicate RhoA as a Target for Dbs Transforming Activity

REFERENCES

• Abe, K., K. L. Rossman, B. Liu, K. D. Ritola, D. Chiang, S. L. Campbell, K. Burridge, and C. J. Der. 2000. Vav2 is an activator of Cdc42, Rac1, and RhoA. J. Biol. Chem. 275: 10141–10149.
   PubMed Web of Science ®Google Scholar
• Alberts, A. S., and R. Treisman. 1998. Activation of RhoA and SAPK/JNK signalling pathways by the RhoA-specific exchange factor mNET1. EMBO J. 17: 4075–4085.
   PubMed Web of Science ®Google Scholar
• Avraham, H., and R. A. Weinberg. 1989. Characterization and expression of the human rhoH12 gene product. Mol. Cell. Biol. 9: 2058–2066.
   PubMed Web of Science ®Google Scholar
• Clark, G. J., A. D. Cox, S. M. Graham, and C. J. Der. 1995. Biological assays for Ras transformation. Methods Enzymol. 255: 395–412.
   PubMed Web of Science ®Google Scholar
• Debant, A., C. Serra-Pages, K. Seipel, S. O'Brien, M. Tang, S. H. Park, and M. Streuli. 1996. The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. Proc. Natl. Acad. Sci. USA 93: 5466–5471.
   PubMed Web of Science ®Google Scholar
• Gao, Y., J. Xing, M. Streuli, T. L. Leto, and Y. Zheng. 2001. Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors. J. Biol. Chem. 276: 47530–47541.
   PubMed Web of Science ®Google Scholar
• Glaven, J. A., I. Whitehead, S. Bagrodia, R. Kay, and R. A. Cerione. 1999. The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells. J. Biol. Chem. 274: 2279–2285.
   PubMed Web of Science ®Google Scholar
• Glaven, J. A., I. P. Whitehead, T. Nomanbhoy, R. Kay, and R. A. Cerione. 1996. Lfc and Lsc oncoproteins represent two new guanine nucleotide exchange factors for the Rho GTP-binding protein. J. Biol. Chem. 271: 27374–27381.
   PubMed Web of Science ®Google Scholar
• Han, J., B. Das, W. Wei, L. Van Aelst, R. D. Mosteller, R. Khosravi-Far, J. K. Westwick, C. J. Der, and D. Broek. 1997. Lck regulates Vav activation of members of the Rho family of GTPases. Mol. Cell. Biol. 17: 1346–1353.
   PubMed Web of Science ®Google Scholar
• Han, J., K. Luby-Phelps, B. Das, X. Shu, Y. Xia, R. D. Mosteller, U. M. Krishna, J. R. Falck, M. A. White, and D. Broek. 1998. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279: 558–560.
   PubMedGoogle Scholar
• Hart, M. J., A. Eva, D. Zangrilli, S. A. Aaronson, T. Evans, R. A. Cerione, and Y. Zheng. 1994. Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem. 269: 62–65.
   PubMed Web of Science ®Google Scholar
• Hauser, C. A., J. K. Westwick, and L. A. Quilliam. 1995. Ras-mediated transcription activation: analysis by transient cotransfection assays. Methods Enzymol. 255: 412–426.
   PubMedGoogle Scholar
• Hordijk, P. L., J. P. ten Klooster, R. A. van der Kammen, F. Michiels, L. C. Oomen, and J. G. Collard. 1997. Inhibition of invasion of epithelial cells by Tiam1-Rac signaling. Science 278: 1464–1466.
   PubMed Web of Science ®Google Scholar
• Horii, Y., J. F. Beeler, K. Sakaguchi, M. Tachibana, and T. Miki. 1994. A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways. EMBO J. 13: 4776–4786.
   PubMedGoogle Scholar
• Karnoub, A. E., D. K. Worthylake, K. L. Rossman, W. M. Pruitt, S. L. Campbell, J. Sondek, and C. J. Der. 2001. Molecular basis for Rac1 recognition by guanine nucleotide exchange factors. Nat. Struct. Biol. 8: 1037–1041.
   PubMedGoogle Scholar
• Khosravi-Far, R., M. Chrzanowska-Wodnicka, P. A. Solski, A. Eva, K. Burridge, and C. J. Der. 1994. Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras. Mol. Cell. Biol. 14: 6848–6857.
   PubMedGoogle Scholar
• Khosravi-Far, R., P. A. Solski, G. J. Clark, M. S. Kinch, and C. J. Der. 1995. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell. Biol. 15: 6443–6453.
   PubMed Web of Science ®Google Scholar
• Lamarche, N., and A. Hall. 1994. GAPs for rho-related GTPases. Trends Genet. 10: 436–440.
   PubMed Web of Science ®Google Scholar
• Lin, R., R. A. Cerione, and D. Manor. 1999. Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation. J. Biol. Chem. 274: 23633–23641.
   PubMedGoogle Scholar
• Liu, X., H. Wang, M. Eberstadt, A. Schnuchel, E. T. Olejniczak, R. P. Meadows, J. M. Schkeryantz, D. A. Janowick, J. E. Harlan, E. A. Harris, D. E. Staunton, and S. W. Fesik. 1998. NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. Cell 95: 269–277.
   PubMedGoogle Scholar
• Nur-E-Kamal, M. S., J. M. Kamal, M. M. Qureshi, and H. Maruta. 1999. The CDC42-specific inhibitor derived from ACK-1 blocks v-Ha-Ras-induced transformation. Oncogene 18: 7787–7793.
   PubMed Web of Science ®Google Scholar
• Qiu, R. G., A. Abo, F. McCormick, and M. Symons. 1997. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol. Cell. Biol. 17: 3449–3458.
   PubMedGoogle Scholar
• Qiu, R. G., J. Chen, D. Kirn, F. McCormick, and M. Symons. 1995. An essential role for Rac in Ras transformation. Nature 374: 457–459.
   PubMed Web of Science ®Google Scholar
• Qiu, R. G., J. Chen, F. McCormick, and M. Symons. 1995. A role for Rho in Ras transformation. Proc. Natl. Acad. Sci. USA 92: 11781–11785.
   PubMed Web of Science ®Google Scholar
• Quilliam, L. A., R. Khosravi-Far, S. Y. Huff, and C. J. Der. 1995. Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bioessays 17: 395–404.
   PubMed Web of Science ®Google Scholar
• Rameh, L. E., A. Arvidsson, K. L. Carraway III, A. D. Couvillon, G. Rathbun, A. Crompton, B. VanRenterghem, M. P. Czech, K. S. Ravichandran, S. J. Burakoff, D. S. Wang, C. S. Chen, and L. C. Cantley. 1997. A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272: 22059–22066.
   PubMed Web of Science ®Google Scholar
• Reid, T., A. Bathoorn, M. R. Ahmadian, and J. G. Collard. 1999. Identification and characterization of hPEM-2, a guanine nucleotide exchange factor specific for Cdc42. J. Biol. Chem. 274: 33587–33593.
   PubMed Web of Science ®Google Scholar
• Reid, T., T. Furuyashiki, T. Ishizaki, G. Watanabe, N. Watanabe, K. Fujisawa, N. Morii, P. Madaule, and S. Narumiya. 1996. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J. Biol. Chem. 271: 13556–13560.
   PubMed Web of Science ®Google Scholar
• Rossman, K. L., D. K. Worthylake, J. T. Snyder, D. P. Siderovski, S. L. Campbell, and J. Sondek. 2002. A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. EMBO J. 21: 1315–1326.
   PubMed Web of Science ®Google Scholar
• Sandberg, W. S., and T. C. Terwilliger. 1993. Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl. Acad. Sci. USA 90: 8367–8371.
   PubMedGoogle Scholar
• Sander, E. E., J. P. ten Klooster, S. van Delft, R. A. van der Kammen, and J. G. Collard. 1999. Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147: 1009–1022.
   PubMed Web of Science ®Google Scholar
• Sander, E. E., S. van Delft, J. P. ten Klooster, T. Reid, R. A. van der Kammen, F. Michiels, and J. G. Collard. 1998. Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143: 1385–1398.
   PubMed Web of Science ®Google Scholar
• Schuebel, K. E., X. R. Bustelo, D. A. Nielsen, B. J. Song, M. Barbacid, D. Goldman, and I. J. Lee. 1996. Isolation and characterization of murine vav2, a member of the vav family of proto-oncogenes. Oncogene 13: 363–371.
   PubMedGoogle Scholar
• Snyder, J. T., K. L. Rossman, M. A. Baumeister, W. M. Pruitt, D. P. Siderovski, C. J. Der, M. A. Lemmon, and J. Sondek. 2001. Quantitative analysis of the effect of phosphoinositide interactions on the function of Dbl family proteins. J. Biol. Chem. 276: 45868–45875.
   PubMed Web of Science ®Google Scholar
• Snyder, J. T., D. K. Worthylake, K. L. Rossman, L. Betts, W. M. Pruitt, D. P. Siderovski, C. J. Der, and J. Sondek. 2002. Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat. Struct. Biol. 9: 468–475.
   PubMedGoogle Scholar
• Westwick, J. K., Q. T. Lambert, G. J. Clark, M. Symons, L. Van Aelst, R. G. Pestell, and C. J. Der. 1997. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17: 1324–1335.
   PubMed Web of Science ®Google Scholar
• Whitehead, I., H. Kirk, and R. Kay. 1995. Retroviral transduction and oncogenic selection of a cDNA encoding Dbs, a homolog of the Dbl guanine nucleotide exchange factor. Oncogene 10: 713–721.
   PubMedGoogle Scholar
• Whitehead, I., H. Kirk, C. Tognon, G. Trigo-Gonzalez, and R. Kay. 1995. Expression cloning of lfc, a novel oncogene with structural similarities to guanine nucleotide exchange factors and to the regulatory region of protein kinase C. J. Biol. Chem. 270: 18388–18395.
   PubMed Web of Science ®Google Scholar
• Whitehead, I. P., S. Campbell, K. L. Rossman, and C. J. Der. 1997. Dbl family proteins. Biochim. Biophys. Acta 1332: F1–F23.
   PubMed Web of Science ®Google Scholar
• Whitehead, I. P., Q. T. Lambert, J. A. Glaven, K. Abe, K. L. Rossman, G. M. Mahon, J. M. Trzaskos, R. Kay, S. L. Campbell, and C. J. Der. 1999. Dependence of Dbl and Dbs transformation on MEK and NF-κB activation. Mol. Cell. Biol. 19: 7759–7770.
   PubMedGoogle Scholar
• Worthylake, D. K., K. L. Rossman, and J. Sondek. 2000. Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 408: 682–688.
   PubMed Web of Science ®Google Scholar
• Zheng, Y., R. Cerione, and A. Bender. 1994. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J. Biol. Chem. 269: 2369–2372.
   PubMed Web of Science ®Google Scholar
• Zheng, Y., D. J. Fischer, M. F. Santos, G. Tigyi, N. G. Pasteris, J. L. Gorski, and Y. Xu. 1996. The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor. J. Biol. Chem. 271: 33169–33172.
   PubMed Web of Science ®Google Scholar
• Zheng, Y., M. F. Olson, A. Hall, R. A. Cerione, and D. Toksoz. 1995. Direct involvement of the small GTP-binding protein Rho in lbc oncogene function. J. Biol. Chem. 270: 9031–9034.
   PubMed Web of Science ®Google Scholar
• Zohn, I. E., M. Symons, M. Chrzanowska-Wodnicka, J. K. Westwick, and C. J. Der. 1998. Mas oncogene signaling and transformation require the small GTP-binding protein Rac. Mol. Cell. Biol. 18: 1225–1235.
   PubMedGoogle Scholar