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… 

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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