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Reference Report
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| Citation | Pedraza, L.G., Stewart, R.A., Li, D.M., Xu, T. (2004). Drosophila Src-family kinases function with Csk to regulate cell proliferation and apoptosis. Oncogene 23(27): 4754--4762. (Export to RIS) | ||
| FlyBase ID | FBrf0179378 | ||
| Publication Type | Research paper | ||
| PubMed ID | 15107833 | ||
| PubMed Abstract | Elevated Src protein levels and activity are associated with the development and progression of a variety of cancers. The consequences of deregulated Src activity have been studied extensively in cell culture; however, the effects of this deregulation in vivo, as well as the mechanisms of Src-induced tumorigenesis, remain poorly understood. In this study, the effect of expressing wild-type and constitutively active Drosophila Src-family kinases (SFKs) in the developing eye was examined. Overexpression of either wild-type Drosophila SFK (Src64 and Src42) is sufficient to induce ectopic proliferation in G1/G0-arrested, uncommitted cells in eye imaginal discs. In addition, both kinases trigger apoptosis in vivo, in a dosage-dependent manner. Constitutively active mutants are hypermorphic as they trigger proliferation and death more potently than their wild-type counterparts. Moreover, SFK-induced proliferation and apoptosis are largely independent events, as blocking ectopic proliferation does not block cell death. Further, DCsk (the Drosophila homolog of the C-terminal Src kinase) phosphorylates and interacts genetically with the wild-type SFKs, but not with the constitutively active mutants in which a conserved C-terminal tyrosine was mutated to phenylalanine, providing the first in vivo evidence that Csk regulates SFKs during development through phosphorylation of their C-terminal tyrosine. | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | Oncogene | ||
| Title | Oncogene | ||
| Publication Year | 1987- | ||
| ISBN/ISSN | 0950-9232 | ||
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Data from Reference
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| Alleles (9)
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| Constructs (8)
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| Genes (7)
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| Insertions (25)
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