Skip to main content
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1986 Dec;6(12):4745–4748. doi: 10.1128/mcb.6.12.4745

gp140v-fms molecules expressed at the surface of cells transformed by the McDonough strain of feline sarcoma virus are phosphorylated in tyrosine and serine.

T Tamura, E Simon, H Niemann, G T Snoek, H Bauer
PMCID: PMC367261  PMID: 2432405

Abstract

Cells transformed by the McDonough strain of feline sarcoma virus express at their surface a v-fms-specific transmembrane glycoprotein designated gp140v-fms. By labeling with 32Pi, gp140v-fms was shown to be phosphorylated 30-fold more in serine residues than were the cytosolic v-fms polypeptides gp180gag-fms and gp120v-fms. By using the phosphotyrosine phosphatase-specific inhibitor sodium orthovanadate, an additional tyrosine phosphorylation was observed in vivo, again involving predominantly gp140v-fms. In vitro studies showed that the v-fms proteins were phosphorylated by protein kinase C in a calcium- and phosphatidylserine-dependent manner.

Full text

PDF
4748

Images in this article

Selected References

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

  1. Anderson S. J., Gonda M. A., Rettenmier C. W., Sherr C. J. Subcellular localization of glycoproteins encoded by the viral oncogene v-fms. J Virol. 1984 Sep;51(3):730–741. doi: 10.1128/jvi.51.3.730-741.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barbacid M., Lauver A. V. Gene products of McDonough feline sarcoma virus have an in vitro-associated protein kinase that phosphorylates tyrosine residues: lack of detection of this enzymatic activity in vivo. J Virol. 1981 Dec;40(3):812–821. doi: 10.1128/jvi.40.3.812-821.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hadwiger A., Niemann H., Käbisch A., Bauer H., Tamura T. Appropriate glycosylation of the fms gene product is a prerequisite for its transforming potency. EMBO J. 1986 Apr;5(4):689–694. doi: 10.1002/j.1460-2075.1986.tb04268.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hampe A., Gobet M., Sherr C. J., Galibert F. Nucleotide sequence of the feline retroviral oncogene v-fms shows unexpected homology with oncogenes encoding tyrosine-specific protein kinases. Proc Natl Acad Sci U S A. 1984 Jan;81(1):85–89. doi: 10.1073/pnas.81.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hunter T., Sefton B. M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1311–1315. doi: 10.1073/pnas.77.3.1311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Klarlund J. K. Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins. Cell. 1985 Jul;41(3):707–717. doi: 10.1016/s0092-8674(85)80051-9. [DOI] [PubMed] [Google Scholar]
  7. Leis J. F., Kaplan N. O. An acid phosphatase in the plasma membranes of human astrocytoma showing marked specificity toward phosphotyrosine protein. Proc Natl Acad Sci U S A. 1982 Nov;79(21):6507–6511. doi: 10.1073/pnas.79.21.6507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Manger R., Najita L., Nichols E. J., Hakomori S., Rohrschneider L. Cell surface expression of the McDonough strain of feline sarcoma virus fms gene product (gp 140fms). Cell. 1984 Dec;39(2 Pt 1):327–337. doi: 10.1016/0092-8674(84)90011-4. [DOI] [PubMed] [Google Scholar]
  9. Nichols E. J., Manger R., Hakomori S., Herscovics A., Rohrschneider L. R. Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression. Mol Cell Biol. 1985 Dec;5(12):3467–3475. doi: 10.1128/mcb.5.12.3467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Rettenmier C. W., Roussel M. F., Quinn C. O., Kitchingman G. R., Look A. T., Sherr C. J. Transmembrane orientation of glycoproteins encoded by the v-fms oncogene. Cell. 1985 Apr;40(4):971–981. doi: 10.1016/0092-8674(85)90357-5. [DOI] [PubMed] [Google Scholar]
  11. Reynolds F. H., Jr, Van de Ven W. J., Blomberg J., Stephenson J. R. Differences in mechanisms of transformation by independent feline sarcoma virus isolates. J Virol. 1981 Jun;38(3):1084–1089. doi: 10.1128/jvi.38.3.1084-1089.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Roussel M. F., Rettenmier C. W., Look A. T., Sherr C. J. Cell surface expression of v-fms-coded glycoproteins is required for transformation. Mol Cell Biol. 1984 Oct;4(10):1999–2009. doi: 10.1128/mcb.4.10.1999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sacca R., Stanley E. R., Sherr C. J., Rettenmier C. W. Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene. Proc Natl Acad Sci U S A. 1986 May;83(10):3331–3335. doi: 10.1073/pnas.83.10.3331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tamura T., Bauer H., Birr C., Pipkorn R. Antibodies against synthetic peptides as a tool for functional analysis of the transforming protein pp60src. Cell. 1983 Sep;34(2):587–596. doi: 10.1016/0092-8674(83)90391-4. [DOI] [PubMed] [Google Scholar]
  15. Tamura T., Friis R. R., Bauer H. pp60c-src is a substrate for phosphorylation when cells are stimulated to enter cycle. FEBS Lett. 1984 Nov 5;177(1):151–156. doi: 10.1016/0014-5793(84)81001-7. [DOI] [PubMed] [Google Scholar]
  16. Woolford J., Rothwell V., Rohrschneider L. Characterization of the human c-fms gene product and its expression in cells of the monocyte-macrophage lineage. Mol Cell Biol. 1985 Dec;5(12):3458–3466. doi: 10.1128/mcb.5.12.3458. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES