The COOH-Terminal Domain of the Rap1A (Krev-1) Protein Is Isoprenylated and Supports Transformation by an H-Ras:Rap1A Chimeric Protein

REFERENCES

• Adari, H., D. R. Lowy, B. M. Willumsen, C. J. Der, and F. McCormick. 1988. Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science 240:518-521.
   PubMed Web of Science ®Google Scholar
• Buss, J. E., P. A. Solski, J. P. Schaeffer, M. J. MacDonald, and C. J. Der. 1989. Activation of the cellular proto-oncogene product p21Ras by addition of a myristylation signal. Science 243:1600-1603.
   PubMed Web of Science ®Google Scholar
• Calés, C., J. F. Hancock, C. J. Marshall, and A. Hall. 1988. The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product. Nature (London) 332:548-551.
   PubMed Web of Science ®Google Scholar
• Casey, P. Unpublished data.
   Google Scholar
• Casey, P. J., P. A. Solski, C. J. Der, and J. E. Buss. 1989. p21Ras is modified by the isoprenoid farnesol. Proc. Natl. Acad. Sci. USA 86:8323-8327.
   PubMed Web of Science ®Google Scholar
• Cepko, C. L., B. Roberts, and R. C. Mulligan. 1984. Construction and applications of a highly transmissible murine retrovirus shuttle vector. Cell 37:1053-1062.
   PubMed Web of Science ®Google Scholar
• Chelsky, D., N. I. Gutterson, and D. E. Koshland, Jr. 1984. A diffusion assay for detection and quantitation of methyl-esterified proteins on polyacrylamide gels. Anal. Biochem. 141:143-148.
   PubMedGoogle Scholar
• Chesa, P. G., W. J. Rettig, M. R. Melamed, L. J. Old, and H. Niman. 1987. Expression of p21ras in normal and malignant human tissues: lack of association with proliferation and malignancy. Proc. Natl. Acad. Sci. USA 84:3234-3238.
   PubMed Web of Science ®Google Scholar
• Clarke, S., J. P. Vogel, R. J. Deschenes, and J. Stock. 1988. Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases. Proc. Natl. Acad. Sci. USA 85:4643-4647.
   PubMed Web of Science ®Google Scholar
• Der, C. J., T. Finkel, and G. M. Cooper. 1986. Biological and biochemical properties of human rasH genes mutated at codon 61. Cell 44:167-176.
   PubMed Web of Science ®Google Scholar
• Der, C. J., B. Weissman, and M. J. MacDonald. 1988. Altered guanine nucleotide binding and H-ras transforming and differentiating activities. Oncogene 3:105-112.
   Google Scholar
• Deschenes, R. J., and J. R. Broach. 1987. Fatty acylation is important but not essential for Saccharomyces cerevisiae RAS function. Mol. Cell. Biol. 7:2344-2351.
   PubMedGoogle Scholar
• Deschenes, R. J., J. B. Stimmel, S. Clarke, J. Stock, and J. R. Broach. 1989. RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus. J. Biol. Chem. 264:11865-11873.
   PubMed Web of Science ®Google Scholar
• Didsbury, J. R., R. J. Uhing, and R. Snyderman. 1990. Isoprenylation of the low molecular mass GTP-binding proteins RAC 1 and RAC 2: possible role in membrane localization. Biochem. Biophys. Res. Commun. 171:804-812.
   PubMedGoogle Scholar
• Farnsworth, C. C., M. H. Gelb, and J. A. Glomset. 1990. Identification of geranylgeranyl-modified proteins in HeLa cells. Science 247:320-322.
   PubMed Web of Science ®Google Scholar
• Farnsworth, C. C., S. L. Wolda, M. H. Gelb, and J. A. Glomset. 1989. Human lamin B contains a farnesylated cysteine residue. J. Biol. Chem. 264:20422-20429.
   PubMed Web of Science ®Google Scholar
• Finegold, A. A., W. R. Schafer, J. Rine, M. Whiteway, and F. Tamanoi. 1990. Common modifications of trimeric G proteins and ras protein: involvement of polyisoprenylation. Science 249:165-169.
   PubMedGoogle Scholar
• Frech, M., J. John, V. Pizon, P. Chardin, A. Tavitian, R. Clark, F. McCormick, and A. Wittinghofer. 1990. The protein product of the Krev-1 gene (rap1A) inhibits GAP activation of p21. Science 249:169-171.
   PubMed Web of Science ®Google Scholar
• Fujiyama, A., and F. Tamanoi. 1990. RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N terminus and removal of three amino acids at C terminus. J. Biol. Chem. 265:3362-3368.
   PubMed Web of Science ®Google Scholar
• Gibbs, J. B., M. D. Schaber, T. L. Schofield, E. M. Scolnick, and I. S. Sigal. 1989. Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant. Proc. Natl. Acad. Sci. USA 86:6630-6634.
   PubMed Web of Science ®Google Scholar
• Gutierrez, L., A. I. Magee, C. J. Marshall, and J. F. Hancock. 1989. Posttranslational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J. 8:1093-1098.
   PubMed Web of Science ®Google Scholar
• Hancock, J. F., A. I. Magee, J. E. Childs, and C. J. Marshall. 1989. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57:1167-1177.
   PubMed Web of Science ®Google Scholar
• Hata, J., A. Kikuchi, T. Sasaki, M. D. Schaber, J. B. Gibbs, and Y. Takai. 1990. Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s. J. Biol. Chem. 265:7104-7107.
   PubMed Web of Science ®Google Scholar
• Jackson, J. H., C. G. Cochrane, J. R. Bourne, P. A. Solski, J. E. Buss, and C. J. Der. 1990. Farnesol modification of Kirsten-ras exon 4B is essential for transformation. Proc. Natl. Acad. Sci. USA 87:3042-3046.
   PubMed Web of Science ®Google Scholar
• Kato, K. Unpublished data.
   Google Scholar
• Kawata, M., Y. Matsui, J. Kondo, T. Hishida, Y. Teranishi, and Y. Takai. 1988. A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. J. Biol. Chem. 263:18965-18971.
   PubMed Web of Science ®Google Scholar
• Kikuchi, A., T. Saski, S. Araki, Y. Hata, and Y. Takai. 1989. Purification and characterization of bovine brain cytosol of two GTPase activating proteins specific for smg p21, a GTP-binding protein having the same effector domain as c-ras p21s. J. Biol. Chem. 264:9133-9136.
   PubMedGoogle Scholar
• Kitayama, H., T. Matsuzaki, Y. Ikawa, and M. Noda. 1990. Genetic analysis of the Krev-1 gene: potentiation of its tumor suppressor activity by specific point mutations. Proc. Natl. Acad. Sci. USA 87:4284-4288.
   PubMed Web of Science ®Google Scholar
• Kitayama, H., Y. Sugimoto, T. Matsuzaki, Y. Ikawa, and M. Noda. 1989. A ras-related gene with transformation suppressor activity. Cell 56:77-84.
   PubMed Web of Science ®Google Scholar
• Lowe, D. G., M. Ricketts, A. D. Levinson, and D. V. Goeddel. 1988. Chimeric proteins define variable and essential regions of Ha-ras-encoded protein. Proc. Natl. Acad. Sci. USA 85:1015-1019.
   PubMedGoogle Scholar
• Lowe, P. N., M. Sydenham, and M. J. Page. 1990. The Ha-ras protein, p21, is modified by a derivative of mevalonate and methyl-esterified when espressed in the insect/baculovirus system. Oncogene 5:1045-1048.
   PubMedGoogle Scholar
• Luckow, V. A., and M. D. Summers. 1988. Trends in the development of baculovirus expression vectors. Bio/Technology 6:47-55.
   Web of Science ®Google Scholar
• Magee, T., and M. Hanley. 1988. Sticky fingers and CAAX boxes. Nature (London) 335:114.
   PubMedGoogle Scholar
• Maltese, W. A., and K. M. Sheridan. 1990. Isoprenoid modification of G25K (Gp), a low molecular mass GTP-binding protein distinct from p21ras. J. Biol. Chem. 265:17883-17890.
   PubMedGoogle Scholar
• Michaeli, T., J. Field, R. Ballester, K. O’Neill, and M. Wigler. 1989. Mutants of H-ras that interfere with RAS effector function in Saccharomyces cerevisiae. EMBO J. 8:3039-3044.
   PubMedGoogle Scholar
• Mumby, S. M., P. J. Casey, A. G. Gilman, S. Gutowski, and P. Sternweis. 1990. G protein gamma subunits contain a 20-carbon isoprenoid. Proc. Natl. Acad. Sci. USA 87:5873-5877.
   PubMedGoogle Scholar
• Pizon, V., P. Chardin, I. Lerosey, B. Olofsson, and A. Tavitian. 1988. Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the ‘effector’ region. Oncogene 3:201-204.
   PubMed Web of Science ®Google Scholar
• Powers, S., S. Michaelis, D. Broek, S. Santa Anna-A, J. Field, I. Herskowitz, and M. Wigler. 1986. RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Cell 47:413-422.
   PubMedGoogle Scholar
• Quilliam, L. A., C. J. Der, R. Clark, E. C. O’Rourke, K. Zhang, F. McCormick, and G. M. Bokoch. 1990. Biochemical characterization of baculovirus-expressed, rapla/Krev-1 protein and its regulation by GTPase-activating proteins. Mol. Cell. Biol. 10:2901-2908.
   PubMedGoogle Scholar
• Reiss, Y., J. L. Goldstein, M. C. Seabra, P. J. Casey, and M. S. Brown. 1990. Inhibition of purified p21 ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cell 62:81-88.
   PubMed Web of Science ®Google Scholar
• Rilling, H. C., E. Breunger, W. W. Epstein, and P. F. Crain. 1990. Prenylated proteins: the structure of the isoprenoid group. Science 247:318-320.
   PubMed Web of Science ®Google Scholar
• Schafer, W. R., R. Kim, R. Sterne, J. Thorner, S.-H. Kim, and J. Rine. 1989. Genetic and pharmacological suppression of oncogenic mutations in RAS genes of yeast and humans. Science 245:379-385.
   PubMed Web of Science ®Google Scholar
• Summers, M. D., and G. E. Smith. 1989. A manual of methods for baculovirus vectors and insect cell culture procedures. Texas Agricultural Experiment Station Bulletin no. 1555. Texas A&M University, College Station, Tex.
   Google Scholar
• Willumsen, B. M., A. Christensen, N. L. Hubbert, A. G. Papageorge, and D. R. Lowy. 1984. The p21 ras C-terminus is required for transformation and membrane association. Nature (London) 310:583-586.
   PubMed Web of Science ®Google Scholar
• Willumsen, B. M., K. Norris, A. G. Papageorge, N. L. Hubbert, and D. R. Lowy. 1984. Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus. EMBO J. 3:2581-2585.
   PubMed Web of Science ®Google Scholar
• Yamane, H. K., C. C. Farnsworth, H. Xie, W. Howald, B. K.-K. Fung, S. Clarke, M. H. Gelb, and J. A. Glomset. 1990. Brain G protein gamma subunits contain an all-trans-geranylgaranyl- cysteine methyl ester at their carboxyl termini. Proc. Natl. Acad. Sci. USA 87:5868-5872.
   PubMed Web of Science ®Google Scholar
• Zhang, K., M. Noda, W. C. Vass, and D. R. Lowy. 1990. A small number of divergent amino acids mediate the opposing effects of ras and Krev-1. Science 249:162-165.
   PubMed Web of Science ®Google Scholar
• Zoller, M. J., and M. Smith. 1983. Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors. Methods Enzymol. 100:468-500.
   PubMed Web of Science ®Google Scholar