Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1987 May;61(5):1678–1681. doi: 10.1128/jvi.61.5.1678-1681.1987

The membrane-binding domain and myristylation of p60v-src are not essential for stimulation of cell proliferation.

G Calothy, D Laugier, F R Cross, R Jove, T Hanafusa, H Hanafusa
PMCID: PMC254154  PMID: 3106650

Abstract

Previous studies showed that the amino-terminal domain of Rous sarcoma virus p60v-src involved in myristylation and membrane association of the protein is required for morphological transformation and anchorage independence. Analysis of src delection mutants revealed that the amino-terminal one-third of p60v-src, including the membrane-binding domain, is not essential for induction of cell proliferation. These results demonstrated that, in contrast to the cellular target(s) involved in morphological transformation and anchorage independence, the target(s) involved in mitogenic activity is accessible to nonmyristylated src proteins.

Full text

PDF
1678

Images in this article

1680Image
on p.1680

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson D. D., Beckmann R. P., Harms E. H., Nakamura K., Weber M. J. Biological properties of "partial" transformation mutants of Rous sarcoma virus and characterization of their pp60src kinase. J Virol. 1981 Jan;37(1):445–458. doi: 10.1128/jvi.37.1.445-458.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brugge J. S., Darrow D. Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins. J Biol Chem. 1984 Apr 10;259(7):4550–4557. [PubMed] [Google Scholar]
  3. Calothy G., Pessac B. Growth stimulation of chicl embryo neuroretinal cells infected with Rous sarcoma virus: relationship to viral replication and morphological transformation. Virology. 1976 May;71(1):336–345. doi: 10.1016/0042-6822(76)90117-3. [DOI] [PubMed] [Google Scholar]
  4. Calothy G., Poirier F., Dambrine G., Mignatti P., Combes P., Pessac B. Expression of viral oncogenes in differentiating chick embryo neuroretinal cells infected with avian tumor viruses. Cold Spring Harb Symp Quant Biol. 1980;44(Pt 2):983–990. doi: 10.1101/sqb.1980.044.01.106. [DOI] [PubMed] [Google Scholar]
  5. Calothy G., Poirier F., Dambrine G., Pessac B. A transformation defective mutant of Rous sarcoma virus inducing chick embryo neuroretinal cell proliferation. Virology. 1978 Aug;89(1):75–84. doi: 10.1016/0042-6822(78)90041-7. [DOI] [PubMed] [Google Scholar]
  6. Cross F. R., Garber E. A., Hanafusa H. N-terminal deletions in Rous sarcoma virus p60src: effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene. Mol Cell Biol. 1985 Oct;5(10):2789–2795. doi: 10.1128/mcb.5.10.2789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cross F. R., Garber E. A., Pellman D., Hanafusa H. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol Cell Biol. 1984 Sep;4(9):1834–1842. doi: 10.1128/mcb.4.9.1834. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cross F. R., Hanafusa H. Local mutagenesis of Rous sarcoma virus: the major sites of tyrosine and serine phosphorylation of pp60src are dispensable for transformation. Cell. 1983 Sep;34(2):597–607. doi: 10.1016/0092-8674(83)90392-6. [DOI] [PubMed] [Google Scholar]
  9. Garber E. A., Cross F. R., Hanafusa H. Processing of p60v-src to its myristylated membrane-bound form. Mol Cell Biol. 1985 Oct;5(10):2781–2788. doi: 10.1128/mcb.5.10.2781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hunter T., Cooper J. A. Protein-tyrosine kinases. Annu Rev Biochem. 1985;54:897–930. doi: 10.1146/annurev.bi.54.070185.004341. [DOI] [PubMed] [Google Scholar]
  11. Jove R., Garber E. A., Iba H., Hanafusa H. Biochemical properties of p60v-src mutants that induce different cell transformation parameters. J Virol. 1986 Dec;60(3):849–857. doi: 10.1128/jvi.60.3.849-857.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jove R., Mayer B. J., Iba H., Laugier D., Poirier F., Calothy G., Hanafusa T., Hanafusa H. Genetic analysis of p60v-src domains involved in the induction of different cell transformation parameters. J Virol. 1986 Dec;60(3):840–848. doi: 10.1128/jvi.60.3.840-848.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kamps M. P., Buss J. E., Sefton B. M. Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4625–4628. doi: 10.1073/pnas.82.14.4625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kamps M. P., Buss J. E., Sefton B. M. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation. Cell. 1986 Apr 11;45(1):105–112. doi: 10.1016/0092-8674(86)90542-8. [DOI] [PubMed] [Google Scholar]
  15. Kitamura N., Yoshida M. Small deletion in src of Rous sarcoma virus modifying transformation phenotypes: identification of 207-nucleotide deletion and its smaller product with protein kinase activity. J Virol. 1983 Jun;46(3):985–992. doi: 10.1128/jvi.46.3.985-992.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Krueger J. G., Garber E. A., Goldberg A. R. Subcellular localization of pp60src in RSV-transformed cells. Curr Top Microbiol Immunol. 1983;107:51–124. [PubMed] [Google Scholar]
  17. Levinson A. D., Courtneidge S. A., Bishop J. M. Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src). Proc Natl Acad Sci U S A. 1981 Mar;78(3):1624–1628. doi: 10.1073/pnas.78.3.1624. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pellman D., Garber E. A., Cross F. R., Hanafusa H. Fine structural mapping of a critical NH2-terminal region of p60src. Proc Natl Acad Sci U S A. 1985 Mar;82(6):1623–1627. doi: 10.1073/pnas.82.6.1623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pessac B., Calothy G. Transformation of chick embryo neuroretinal cells by Rous sarcoma virus in vitro: induction of cell proliferation. Science. 1974 Aug;185(4152):709–710. doi: 10.1126/science.185.4152.709. [DOI] [PubMed] [Google Scholar]
  20. Poirier F., Jullien P., Dezelee P., Dambrine G., Esnault E., Benatre A., Calothy G. Role of the mitogenic property and kinase activity of p60src in tumor formation by Rous sarcoma virus. J Virol. 1984 Feb;49(2):325–332. doi: 10.1128/jvi.49.2.325-332.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sefton B. M., Hunter T., Beemon K., Eckhart W. Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell. 1980 Jul;20(3):807–816. doi: 10.1016/0092-8674(80)90327-x. [DOI] [PubMed] [Google Scholar]
  22. Tanaka A., Parker C., Kaji A. Stimulation of growth rate of chondrocytes by Rous sarcoma virus is not coordinated with other expressions of the src gene phenotype. J Virol. 1980 Aug;35(2):531–541. doi: 10.1128/jvi.35.2.531-541.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Weber M. J., Friis R. R. Dissociation of transformation parameters using temperature-conditional mutants of Rous sarcoma virus. Cell. 1979 Jan;16(1):25–32. doi: 10.1016/0092-8674(79)90184-3. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES