Biological Function of Aplysia californica rho Gene

  • Rafael P. Ballestero
  • Pilar Esteve
  • Rosario Perona
  • Benilde Jiménez
  • Juan Carlos Lacal
Part of the NATO ASI Series book series (NSSA, volume 220)


rho genes are a family of genes which are structurally related to the oncogenic ras family. The primary structure of rho genes has been elucidated for the marine snail Aplysia californica, two S. cerevisiae genes, and three human versions, rho A, B and C. They all codify for proteins of an approximate M.W. of 21 kDa (rho-p21) which show 35% homology to the ras proteins. It has been observed that rho proteins are ADP-ribosylated by the botulinum toxin C3 exoenzyme, suggesting that rho proteins could be involved in regulating neuronal function. However very little is known about their actual biological functions. While the human rho A and rho C products have been related to cytoeskeleton organization, the rho A product has a weak transforming activity. We have investigated the biological properties of the Aplysia californica rho-p21 protein when introduced into an heterologous system, and found that it does not induce foci in a regular NIH-3T3 transfection assay. However, the morphology of the cells was slightly altered and cells grew to higher cell densities. Moreover, transforming activity was detected when isolated cell lines were inoculated into nude mice. To further investigate the potential transforming activity of the Aplysia gene, we have also generated a Gly→Val mutation at position 14, equivalent to the activating mutation found in oncogenic ras genes. No apparent increase in the transforming activity was observed, indicating that the effects on growth behaviour are probably not the primary function of rho proteins.


High Cell Density Transforming Activity Transfected Cell Line Marine Snail Intrinsic GTPase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Harvey, J.J. (1964). Nature 204: 1104–1105.PubMedCrossRefGoogle Scholar
  2. 2.
    Kirsten, W.H. and Mayer, L.A. (1967) J. Natl. Cancer Inst. 39:311–334.PubMedGoogle Scholar
  3. 3.
    Shih, T.Y., Weeks, M.O., Young, H.A., and Scolnick, E.M.(1979) Virology 96: 64–79.PubMedCrossRefGoogle Scholar
  4. 4.
    Scolnick, E.M., Papageorge, A.G., Stokes, P.E., and Shih, T.Y.(1979) Proc. Natl. Acad. Sci. USA 76: 5355–5359.PubMedCrossRefGoogle Scholar
  5. 5.
    Shih, T.Y., Papageorge, A.G., Stokes, P.E., Weeks, M.O., and Scolnick, E.M. (1980). Nature 287: 686–691.PubMedCrossRefGoogle Scholar
  6. 6.
    Willingham, M.C., Pastanm, I., Shih, T.Y., and Scolnick, E.M.(1980) Cell 19: 1005–1014.PubMedCrossRefGoogle Scholar
  7. 7.
    Barbacid, M. (1987) Ann. Rev. Bioch. 56: 779–827.CrossRefGoogle Scholar
  8. 8.
    Lacal, J.C., and Tronick, S.E. (1988) The ras oncogene. In The Oncogene Handbook. Reddy, P., Curran, T., and Skalka, A. edts. Elsvier, Holland.Google Scholar
  9. 9.
    Bos, J.L. et al. (1985) Nature 315:726–730.PubMedCrossRefGoogle Scholar
  10. 10.
    Reynolds, S. et al (1987) Science 237:1309–1316.PubMedCrossRefGoogle Scholar
  11. 11.
    McGrath, J.P., Capon, D.J., Goeddel, D.V., and Levinson, A.D. (1984) Nature 310: 644–649.PubMedCrossRefGoogle Scholar
  12. 12.
    Gibbs, J.B., Sigal, I.S., Poe, M., and Scolnick, E.M. (1984) Proc. Natl. Acad. Sci. USA 81:5704–5708.PubMedCrossRefGoogle Scholar
  13. 13.
    Sweet, R.W., Yokoyama, S., Kamata, T., Feramisco, J.R., Rosenberg, M., and Gross, M. (1984) Nature 311:273–275.PubMedCrossRefGoogle Scholar
  14. 14.
    Trahey, M., and McCormick, F. (1987) Science 238: 542–545.PubMedCrossRefGoogle Scholar
  15. 15.
    Adari, H., Lowy, D.R., Willumsen, B.M., Der, C.J., and McCormick, F. (1988) Science 240: 518–521.PubMedCrossRefGoogle Scholar
  16. 16.
    Huang, Y.K., Kung, H.-F., and Kamata, T. (1990) Proc. Natl. Acad. Sci. USA 87, 8008–8012PubMedCrossRefGoogle Scholar
  17. 17.
    Wolfman, A., and Macara, I. (1990). Science 248, 67–70.PubMedCrossRefGoogle Scholar
  18. 18.
    Downward, J., Riehl, R., Wu, L. and Weinberg, R.A. (1990) Proc. natl. Acad. Sci. 87, 5998–6002PubMedCrossRefGoogle Scholar
  19. 19.
    Berridge, M.J., and Irvine, R.F. (1984) Nature 312: 315–319PubMedCrossRefGoogle Scholar
  20. 20.
    Gilman, A.G. (1984) Cell 36: 577–579.PubMedCrossRefGoogle Scholar
  21. 21.
    Stryer, L. (1986) Ann. Rev. Neurosc. 9: 787–819.CrossRefGoogle Scholar
  22. 22.
    Ochoa, S. (1986) Arch. Biochem. Biophys. 223: 325–349.CrossRefGoogle Scholar
  23. 23.
    Madaule, P. & Axel, R.. (1985). Cell. 41: 31–40.PubMedCrossRefGoogle Scholar
  24. 24.
    Anderson, P.S., and Lacal, J.C. (1987) Mol. Cel. Biol. 7, 3620–3628.Google Scholar
  25. 25.
    Yamamoto, K.; Kondo, J.; Hishida, T.; Teranishi, Y. & Takai, Y., (1988). J. Biol. Chem. 263: 9926–9932.PubMedGoogle Scholar
  26. 26.
    Olofsson, B.; Chardin, P.; Touchot, N.; Zahraoui, A. & Tavitian, A., (1988). Oncogene. 3: 231–234.PubMedGoogle Scholar
  27. 27.
    Narumiya, S.; Sekine, A. & Fujiwara, M. (1988). J. Biol. Chem. 263: 17255–17257.PubMedGoogle Scholar
  28. 28.
    Kim, S.; Kikuchi, A.; Mizoguchi, A. & Takai, Y., (1989). Mol. Brain Res. 6: 167–176.PubMedCrossRefGoogle Scholar
  29. 29.
    Toki, C.; Oda, K. & Ikehara, Y. (1989). Biochem. Biophys. Res. Commun. 164: 333–338.PubMedCrossRefGoogle Scholar
  30. 30.
    Wieland, T.; Ulibarri, I.; Gierschik, P.; Hall, A.; Aktories, K. & Jakobs, K. H.. (1990). FEBS Lett. 274: 111–114.PubMedCrossRefGoogle Scholar
  31. 31.
    Kikuchi, A.; Yamamoto, K.; Fujita, T. & Takai, Y. (1988) J. Biol. Chem. 263: 16303–16308.PubMedGoogle Scholar
  32. 32.
    Didsbury, J.; Weber, R. F.; Bokoch, G. M.; Evans, T. & Snyderman, R. (1989). J. Biol. Chem. 264: 16378–16382.PubMedGoogle Scholar
  33. 33.
    Sekine, A.; Fujiwara, M. & Narumiya, S. (1989). J. Biol. Chem. 264: 8602–8605.PubMedGoogle Scholar
  34. 34.
    Paterson, H. F.; Self, A. J.; Garrett, M. D.; Just, I.; Aktories, K. & Hall, A. (1990). J. Cell Biol. 111: 1001–1007.PubMedCrossRefGoogle Scholar
  35. 35.
    Avraham, H. & Weinberg, R. A. (1989). Mol. Cell. Biol. 9: 2058–2066.PubMedGoogle Scholar
  36. 36.
    Sanger, F., Nicklen, S., and Coulson, A.R. (1977) Proc. natl. Acadm. Sci. 74:5463–5467.CrossRefGoogle Scholar
  37. 37.
    Gillies, R.J., Didier, N., and Denton, M. (1986) Anal. Biochem. 159:109–113.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Rafael P. Ballestero
    • 1
  • Pilar Esteve
    • 1
  • Rosario Perona
    • 1
  • Benilde Jiménez
    • 1
  • Juan Carlos Lacal
    • 1
  1. 1.Instituto de Investigaciones BiomédicasMadridSpain

Personalised recommendations