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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Genes, fms

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Disease relevance of Genes, fms


High impact information on Genes, fms


Biological context of Genes, fms

  • The COOH-terminal 40 amino acids of the c-fms gene product are replaced in the v-fms gene product by 11 amino acids encoded by the retroviral genome [9].
  • Tyrosine autophosphorylation of the v-Fms oncogene product results in the formation of high affinity binding sites for cellular proteins with Src homology 2 (SH2) domains that are involved in various signal cascades [10].
  • CSF-1 treatment also increased both the number and size of foci that arose from fibroblasts following transfection with the v-fms oncogene [11].
  • A fragment of the v-fms gene encoding a major portion of the extracellular amino terminal domain, the membrane-spanning segment, and the entire carboxyl terminal tyrosine kinase domain of the glycoprotein was molecularly cloned into an inducible prokaryotic expression plasmid [12].
  • We show that, similar to the mouse gene, the human c-FMS gene possesses a promoter and an intronic enhancer element (c-fms intronic regulatory element or FIRE) [13].

Anatomical context of Genes, fms


Associations of Genes, fms with chemical compounds

  • The mature protein product of the v-fms gene (gp140fms) is found on the surface of transformed cells; this glycoprotein has external, transmembrane, and cytoplasmic domains [18].
  • These results demonstrate the necessity of carbohydrate processing for cell surface expression of the v-fms gene product and illustrate the unique ability to modulate the transformed state of SM-FRE cells with the glycosylational-processing inhibitors CA and MdN [19].

Gene context of Genes, fms

  • The v-fms oncogene product has undergone genetic alterations which constitutively activate the receptor kinase in the absence of CSF 1 [20].
  • By contrast, the mature cell surface glycoprotein encoded by the v-fms oncogene was phosphorylated on tyrosine in the absence of CSF-1, suggesting that it functions as a ligand-independent kinase [21].
  • The c-FMS gene encodes the macrophage colony-stimulating factor receptor (M-CSFR or CSF1-R), which is a tyrosine kinase growth factor receptor essential for macrophage development [13].
  • Expression of the v-fms gene product does not transmodulate the normal receptors for CSF-1 or IL-3 and affects neither their affinity, number, nor potential to be independently down-regulated by their ligands or by phorbol esters [22].
  • Thus, the synthesis of high levels of the v-fms gene product in FDC-P1 cells abrogated their requirement for IL-3 and rendered the cells tumorigenic by a nonautocrine mechanism [17].


  1. Reassessment of the v-fms sequence: threonine phosphorylation of the COOH-terminal domain. Smola, U., Hennig, D., Hadwiger-Fangmeier, A., Schütz, B., Pfaff, E., Niemann, H., Tamura, T. J. Virol. (1991) [Pubmed]
  2. Biological activity of the receptor for macrophage colony-stimulating factor in the human endometrial cancer cell line, Ishikawa. Takeda, S., Soutter, W.P., Dibb, N.J., White, J.O. Br. J. Cancer (1996) [Pubmed]
  3. Organization and nature of fortimicin A (astromicin) biosynthetic genes studied using a cosmid library of Micromonospora olivasterospora DNA. Dairi, T., Ohta, T., Hashimoto, E., Hasegawa, M. Mol. Gen. Genet. (1992) [Pubmed]
  4. Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes. Roberts, W.M., Look, A.T., Roussel, M.F., Sherr, C.J. Cell (1988) [Pubmed]
  5. A point mutation in the extracellular domain of the human CSF-1 receptor (c-fms proto-oncogene product) activates its transforming potential. Roussel, M.F., Downing, J.R., Rettenmier, C.W., Sherr, C.J. Cell (1988) [Pubmed]
  6. Transforming potential of the c-fms proto-oncogene (CSF-1 receptor). Roussel, M.F., Dull, T.J., Rettenmier, C.W., Ralph, P., Ullrich, A., Sherr, C.J. Nature (1987) [Pubmed]
  7. The v-fms oncogene induces factor independence and tumorigenicity in CSF-1 dependent macrophage cell line. Wheeler, E.F., Rettenmier, C.W., Look, A.T., Sherr, C.J. Nature (1986) [Pubmed]
  8. The mutated, myeloid cell-specific growth factor receptor v-fms transforms avian erythroid but not myeloid cells. Fuhrmann, U., Vennström, B., Beug, H. Genes Dev. (1989) [Pubmed]
  9. "Replacement" of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential. Browning, P.J., Bunn, H.F., Cline, A., Shuman, M., Nienhuis, A.W. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  10. Tyrosine phosphorylation of the juxtamembrane domain of the v-Fms oncogene product is required for its association with a 55-kDa protein. Joos, H., Trouliaris, S., Helftenbein, G., Niemann, H., Tamura, T. J. Biol. Chem. (1996) [Pubmed]
  11. Colony stimulating factor-1 induced growth stimulation of v-fms transformed fibroblasts. Lyman, S.D., Park, L., Rohrschneider, L.R. Oncogene (1988) [Pubmed]
  12. Antibodies to distal carboxyl terminal epitopes in the v-fms-coded glycoprotein do not cross-react with the c-fms gene product. Furman, W.L., Rettenmier, C.W., Chen, J.H., Roussel, M.F., Quinn, C.O., Sherr, C.J. Virology (1986) [Pubmed]
  13. Differential transcription factor occupancy but evolutionarily conserved chromatin features at the human and mouse M-CSF (CSF-1) receptor loci. Follows, G.A., Tagoh, H., Lefevre, P., Morgan, G.J., Bonifer, C. Nucleic Acids Res. (2003) [Pubmed]
  14. Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene. Sacca, R., Stanley, E.R., Sherr, C.J., Rettenmier, C.W. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  15. Colony-stimulating factor 1-mediated regulation of a chimeric c-fms/v-fms receptor containing the v-fms-encoded tyrosine kinase domain. Roussel, M.F., Downing, J.R., Ashmun, R.A., Rettenmier, C.W., Sherr, C.J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  16. Mouse NIH 3T3 cells expressing human colony-stimulating factor 1 (CSF-1) receptors overgrow in serum-free medium containing human CSF-1 as their only growth factor. Roussel, M.F., Sherr, C.J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  17. The v-fms oncogene induces factor-independent growth and transformation of the interleukin-3-dependent myeloid cell line FDC-P1. Wheeler, E.F., Askew, D., May, S., Ihle, J.N., Sherr, C.J. Mol. Cell. Biol. (1987) [Pubmed]
  18. Analysis of functional domains of the v-fms-encoded protein of Susan McDonough strain feline sarcoma virus by linker insertion mutagenesis. Lyman, S.D., Rohrschneider, L.R. Mol. Cell. Biol. (1987) [Pubmed]
  19. Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression. Nichols, E.J., Manger, R., Hakomori, S., Herscovics, A., Rohrschneider, L.R. Mol. Cell. Biol. (1985) [Pubmed]
  20. The role of the CSF-1 receptor gene (C-fms) in cell transformation. Sherr, C.J. Leukemia (1988) [Pubmed]
  21. Ligand-induced tyrosine kinase activity of the colony-stimulating factor 1 receptor in a murine macrophage cell line. Downing, J.R., Rettenmier, C.W., Sherr, C.J. Mol. Cell. Biol. (1988) [Pubmed]
  22. Fibroblast and hematopoietic cell transformation by the fms oncogene (CSF-1 receptor). Sherr, C.J. Journal of cellular physiology. Supplement. (1987) [Pubmed]
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