Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein

@article{Macdonald1985ExpressionOT,
  title={Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein},
  author={Ian Macdonald and Julia G. Levy and Tony Pawson},
  journal={Molecular and Cellular Biology},
  year={1985},
  volume={5},
  pages={2543 - 2551}
}
The avian c-fps and mammalian c-fes proto-oncogenes are cognate cellular sequences. Antiserum raised against the P140gag-fps transforming protein of Fujinami avian sarcoma virus specifically recognized a 92,000-Mr protein in human and mouse hematopoietic cells which was closely related in structure to Snyder-Theilen feline sarcoma virus P87gag-fes. This polypeptide was apparently the product of the human c-fes gene and was therefore designated p92c-fes. Human p92c-fes was associated with a… 
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Myeloid expression of the human c-fps/fes proto-oncogene in transgenic mice

The 13-kilobase-pair fragment defines a genetic locus sufficient for the appropriate tissue-specific expression of the fps/fes protein-tyrosine kinase and includes a dominant cis-acting element that directs integration-independent myeloid expression in transgenic mice.

The human c-fps/fes gene product expressed ectopically in rat fibroblasts is nontransforming and has restrained protein-tyrosine kinase activity

A 13-kilobase EcoRI genomic restriction fragment containing the human c-fps/fes proto-oncogene locus was expressed transiently in Cos-1 monkey cells and stably in Rat-2 fibroblasts, suggesting that regulatory interactions within the host cell modify fps/ fes protein function and normally restrain its oncogenic potential.

Construction of a cDNA for the human c-fes protooncogene protein-tyrosine kinase and its expression in a baculovirus system.

The polymerase chain reaction is used to construct a full-length c-fes cDNA from overlapping 5' and 3' partial cDNA sequences, indistinguishable from the native protein in terms of its apparent molecular weight following SDS-PAGE.

Expression of c-Fes protein isoforms correlates with differentiation in myeloid leukemias.

It is inferred that alternative splicing generates a family of c-Fes proteins that may be a mechanism to direct the c- Fes kinase domain to different subcellular locations and/or substrates at specific stages of myeloid cell differentiation.

The myeloid-cell-specific c-fes promoter is regulated by Sp1, PU.1, and a novel transcription factor

It is concluded that the human c-fes gene contains a strong myeloid-cell-specific promoter that is regulated by Sp1, PU.1, and a novel transcription factor.

Phosphorylation of a Fes-related Protein in Response to Granulocyte-Macrophage Colony Stimulating Factor (*)

Two-dimensional gel electrophoresis demonstrated that p97 is not Fes but is probably a Fes-related protein, and limited proteolytic mapping of p97 and Fes suggested that these proteins may be related but not identical.

The Fes Protein-Tyrosine Kinase Phosphorylates a Subset of Macrophage Proteins That Are Involved in Cell Adhesion and Cell-Cell Signaling*

One of the macrophage substrates of Fes is identified as the crk-associated substrate (Cas) and a second substrate as a 130-kDa protein that has been previously described as a T cell activation-dependent substrate and is unrelated to Cas is identified.

The Fps/Fes protein-tyrosine kinase promotes angiogenesis in transgenic mice

Results indicate that fps/fes expression is intrinsic to cells of the vascular endothelial lineage and suggest a direct role of the Fps/Fes protein-tyrosine kinase in the regulation of angiogenesis.

Antipeptide antiserum identifies a widely distributed cellular tyrosine kinase related to but distinct from the c-fps/fes-encoded protein

The universal expression of NCP94 suggests that this protein may be involved in an essential function of normal cells and may be a new cellular tyrosine kinase of the src gene family.

Regulation of c-Fes Tyrosine Kinase and Biological Activities by N-Terminal Coiled-Coil Oligomerization Domains

It is shown that disruption or deletion of the first coiled-coil domain upregulates Fes tyrosine kinase and transforming activities in Rat-2 fibroblasts and enhances Fes differentiation-inducing activity in myeloid leukemia cells, suggesting a model in which Fes activation may involve coiledcoil-mediated interconversion of monomeric and oligomeric forms of the kinase.
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References

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A cellular protein is immunologically crossreactive with and functionally homologous to the Fujinami sarcoma virus transforming protein

Monoclonal antibodies to the transforming protein of Fujinami avian sarcoma virus discriminate between different fps-encoded proteins

Data indicate that the fps-encoded peptide sequences of 16L P142gag-fps and UR1 P150gag -fps are more closely related to NCP98 than that of FSV P140gag)-fps, which supports the view that 16L andUR1 viruses represent recent retroviral acquisitions of the c-fps oncogene.

Expression of cellular homologues of retroviral onc genes in human hematopoietic cells.

Total cellular poly(A)-enriched RNA from a variety of fresh human leukemic blood cells and hematopoietic cell lines was analyzed for homology with molecularly cloned DNA probes containing the onc…

Transforming genes of avian (v-fps) and mammalian (v-fes) retroviruses correspond to a common cellular locus.

Transformation-defective mutants of Snyder-Theilen feline sarcoma virus lack tyrosine-specific protein kinase activity

Findings provide genetic evidence that the tyrosine-specific protein kinase activity associated with ST-FeSV P85 is required for virus-induced transformation.

Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins

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Activation of the c-abl oncogene by viral transduction or chromosomal translocation generates altered c-abl proteins with similar in vitro kinase properties

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src- and fps-containing avian sarcoma viruses transform chicken erythroid cells.

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