The Ras GTPase-Activating-Protein-Related Human Protein IQGAP2 Harbors a Potential Actin Binding Domain and Interacts with Calmodulin and Rho Family GTPases

REFERENCES

• Alexander, K. A., B. T. Wakim, G. S. Doyle, K. A. Walsh, and D. R. Storm. 1988. Identification and characterization of the calmodulin-binding domain of neuromodulin, a neurospecific calmodulin-binding protein. J. Biol. Chem. 263:7544–7549.
   PubMedGoogle Scholar
• Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403–410.
   PubMed Web of Science ®Google Scholar
• André, B., and J.-Y. Springdael. 1994. WWP, a new amino acid motif present in single and multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65. Biochem. Biophys. Res. Com-mun. 205:1202–1205.
   Google Scholar
• Ayme-Southgate, A., P. Lasko, C. French, and M. L. Pardue. 1989. Characterization of the gene for mp20: a Drosophila muscle protein that is not found in asynchronous oscillatory flight muscle. J. Cell Biol. 108:521–531.
   PubMedGoogle Scholar
• Barfod, E. T., Y. Zheng, W. J. Kuang, M. J. Hart, T. Evans, R. A. Cerione, and A. Ashkenazi. 1993. Cloning and expression of a human CDC42 GTP-ase-activating protein reveals a functional SH3-binding domain. J. Biol. Chem. 268:26059–26062.
   PubMedGoogle Scholar
• Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature (London) 366:643–654.
   PubMed Web of Science ®Google Scholar
• Bollag, G., and F. McCormick. 1991. Differential regulation of rasGAP and neurofibromatosis gene product activities. Nature (London) 351:576–579.
   PubMed Web of Science ®Google Scholar
• Bourne, H. R., D. A. Sanders, and F. McCormick. 1990. The GTPase super-family: a conserved switch for diverse cellular functions. Nature (London) 348:125–132.
   PubMed Web of Science ®Google Scholar
• Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase super-family: conserved structure and molecular mechanism. Nature (London) 349:117–127.
   PubMed Web of Science ®Google Scholar
• Burgess, W. H., D. K. Jemiolo, and R. H. Kretsinger. 1980. Interaction of calcium and calmodulin in the presence of sodium dodecyl sulfate. Biochim. Biophys. Acta 623:257–270.
   PubMedGoogle Scholar
• Castresana, J., and M. Saraste. 1995. Does Vav bind to F-actin through a CH domain? FEBS Lett. 374:149–151.
   PubMedGoogle Scholar
• Chan, D. C., M. T. Bedford, and P. Leder. 1996. Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15:1045–1054.
   PubMed Web of Science ®Google Scholar
• Cheney, R. E., and M. S. Mooseker. 1992. Unconventional myosins. Curr. Opin. Cell Biol. 4:27–35.
   PubMedGoogle Scholar
• Cheney, R. E., M. K. O’Shea, J. E. Heuser, M. V. Coelho, J. S. Wolenski, E. M. Espreafico, P. Forscher, R. E. Larson, and M. S. Mooseker. 1993. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75:13–23.
   PubMedGoogle Scholar
• Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387–395.
   PubMed Web of Science ®Google Scholar
• Eva, A., and S. A. Aaronson. 1985. Isolation of a new human oncogene from a diffuse B-cell lymphoma. Nature (London) 316:273–275.
   PubMed Web of Science ®Google Scholar
• Farnsworth, C. L., N. W. Freshney, L. B. Rosen, A. Ghosh, M. E. Greenberg, and L. A. Feig. 1995. Calcium activation of Ras mediated by neuronal exchange factor Ras-GRF. Nature (London) 376:524–527.
   PubMed Web of Science ®Google Scholar
• Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Foster, R., K.-Q. Hu, Y. Lu, K. M. Nolan, J. Thissen, and J. Settleman. 1996. Identification of a novel human Rho protein with unusual properties: GTP-ase deficiency and in vivo farnesylation. Mol. Cell. Biol. 16:2689–2699.
   PubMed Web of Science ®Google Scholar
• Fukui, Y., T. Kozasa, Y. Kaziro, T. Takeda, and M. Yamamoto. 1986. Role of a ras homolog in the life cycle of Schizosaccharomyces pombe. Cell 44:329–336.
   PubMed Web of Science ®Google Scholar
• Geissler, E. N., M. Liao, J. D. Brook, F. H. Martin, K. M. Zsebo, D. E. Housman, and S. J. Galli. 1991. Stem cell factor (SCF), a novel hematopoietic growth factor and ligand for c-kit tyrosine kinase receptor, maps on human chromosome 12 between 12q14.3 and 12qter. Somatic Cell Mol. Genet. 17:207–214.
   PubMedGoogle Scholar
• Hall, A., and A. J. Self. 1986. The effect of Mg2+ on the guanine nucleotide exchange rate of p21N-ras. J. Biol. Chem. 261:10963–10965.
   PubMedGoogle Scholar
• Hart, M. J., M. G. Callow, B. Souza, and P. Polakis. 1996. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs. EMBO J. 15:2997–3005.
   PubMedGoogle Scholar
• Imai, Y., S. Miyake, D. A. Hughes, and M. Yamamoto. 1991. Identification of a GTPase-activating protein homolog in Schizosaccharomyces pombe. Mol. Cell. Biol. 11:3088–3094.
   PubMed Web of Science ®Google Scholar
• Janknecht, R., G. de Martynoff, J. Lou, R. A. Hipskind, A. Nordheim, and H. G. Stunnenberg. 1991. Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. Sci. USA 88:8972–8976.
   PubMedGoogle Scholar
• Katzav, S., J. L. Cleveland, H. E. Heslop, and D. Pulido. 1991. Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential. Mol. Cell. Biol. 11:1912–1920.
   PubMed Web of Science ®Google Scholar
• Knight, A. E. 1994. The diversity of myosin-like proteins. Ph.D. thesis. Cambridge University, Cambridge.
   Google Scholar
• Lancaster, C. A., P. M. Taylor-Harris, A. J. Self, S. Brill, H. E. van Erp, and A. Hall. 1994. Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases. J. Biol. Chem. 269:1137–1142.
   PubMedGoogle Scholar
• Lupas, A., M. van Dyke, and J. Stock. 1991. Predicting coiled-coils from protein sequences. Science 252:1162–1164.
   PubMed Web of Science ®Google Scholar
• Manser, E., T. Leung, H. Salihuddin, L. Tan, and L. Lim. 1993. A nonreceptor tyrosine kinase that inhibits the GTPase activity of p21cdc42. Nature (London) 363:364–367.
   PubMed Web of Science ®Google Scholar
• Manser, E., T. Leung, H. Salihuddin, Z.-S. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature (London) 367:40–46.
   PubMed Web of Science ®Google Scholar
• Marcus, S., A. Polverino, E. Chang, D. Robbins, M. H. Cobb, and M. H. Wigler. 1995. Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 92:6180–6184.
   PubMedGoogle Scholar
• McCormick, F. 1989. ras GTPase activating protein: signal transmitter and signal terminator. Cell 56:5–8.
   PubMed Web of Science ®Google Scholar
• Morgenstern, J. P., and H. Land. 1990. A series of mammalian expression vectors and characterization of their expression of a reporter gene in stably and transiently transfected cells. Nucleic Acids Res. 18:1068.
   PubMed Web of Science ®Google Scholar
• Murthy, A. E., A. Bernards, D. Church, J. Wasmuth, and F. F. Gusella. Identification and characterization of two novel TPR containing genes. DNA Mol. Biol., in press.
   Google Scholar
• Nadin-Davis, S., A. Nasin, and D. Beach. 1986. Involvement of ras in sexual differentiation but not in growth control in fission yeast. EMBO J. 5:2963–2971.
   PubMedGoogle Scholar
• Nakafuku, M., M. Nagamine, A. Ohtoshi, K. Tanaka, A. Toh-E, and Y. Kaziro. 1993. Suppression of oncogenic Ras by mutant neurofibromatosis type 1 genes with single amino acid substitutions. Proc. Natl. Acad. Sci. USA 90:6706–6710.
   PubMedGoogle Scholar
• Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filipodia. Cell 81:53–62.
   PubMed Web of Science ®Google Scholar
• Pelletier, J., J. D. Brook, and D. E. Housman. 1991. Assignment of two of the translation initiation factor-4E (EIF4EL1 and EIF4EL2) genes to human chromosomes 4 and 20. Genomics 10:1079–1082.
   PubMedGoogle Scholar
• Qiu, R.-G., J. Chen, D. Kirn, F. McCormick, and M. Symons. 1995. An essential role for Rac in Ras transformation. Nature (London) 374:457–459.
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein rho regulates assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389–399.
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401–410.
   PubMed Web of Science ®Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Snijders, A. J., V. H. Haase, and A. Bernards. 1993. Four tissue-specific mouse ltk mRNAs predict tyrosine kinases that differ upstream of their transmembrane segment. Oncogene 8:27–35.
   PubMedGoogle Scholar
• Sudol, M., H. I. Chen, C. Bougeret, A. Einbond, and P. Bork. 1995. Characterization of a novel protein-binding module—the WW domain. FEBS Lett. 369:67–71.
   PubMed Web of Science ®Google Scholar
• Symons, M., J. M. J. Derry, B. Karlak, S. Jiang, V. Lemahieu, F. McCor-mick, U. Francke, and A. Abo. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723–734.
   PubMed Web of Science ®Google Scholar
• Vogel, U. S., R. A. F. Dixon, M. D. Schaber, R. E. Diehl, M. S. Marshall, E. M. Scolnick, I. S. Sigal, and J. B. Gibbs. 1988. Cloning of bovine GAP and its interaction with oncogenic ras p21. Nature (London) 335:90–93.
   PubMed Web of Science ®Google Scholar
• Wang, Y., M. Boguski, M. Riggs, L. Rodgers, and M. Wigler. 1991. Sar1, a gene from Schizosaccharomyces pombe encoding a protein that regulates ras1. Cell Regul. 2:453–465.
   PubMedGoogle Scholar
• Weissbach, L., J. Settleman, M. F. Kalady, A. J. Snijders, A. E. Murthy, Y.-X. Yan, and A. Bernards. 1994. Identification of a human rasGAP-related protein containing calmodulin-binding motifs. J. Biol. Chem. 269:20517–20521.
   PubMed Web of Science ®Google Scholar
• Wilson, R., R. Ainscough, K. Anderson, C. Baynes, M. Berks, J. Bonfield, J. Burton, M. Connell, T. Copsey, J. Cooper, et al. 1994. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature (London) 368:32–38.
   PubMed Web of Science ®Google Scholar
• Winder, S. J., and M. P. Walsh. 1993. Calponin: thin filament-linked regulation of smooth muscle contraction. Cell. Signalling 5:677–686.
   PubMed Web of Science ®Google Scholar
• Zhang, K., J. E. DeClue, W. C. Vass, A. G. Papageorge, F. McCormick, and D. R. Lowy. 1990. Suppression of c-ras transformation by GTPase-activating protein. Nature (London) 346:754–756.
   PubMedGoogle Scholar
• Zhang, X.-F., J. Settleman, J. M. Kyriakis, E. Takeuchi-Suzuki, S. J. Elledge, S. Marshall, J. T. Bruder, U. R. Rapp, and J. Avruch. 1993. Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature (London) 364:308–313.
   PubMed Web of Science ®Google Scholar