Disease relevance of Src42A

• Activation of Raf-1 via baculovirus coexpression with oncogenic Src or Ras in Sf9 cells was also strongly inhibited by dominant negative p50(cdc37) or by GA [1].

High impact information on Src42A

• Mutants for Src42A, a Drosophila c-src protooncogene homolog, are described [2].
• Src42A functions in epidermal closure during both embryogenesis and metamorphosis [2].
• Dominant-negative mutant phenotypes were suppressed and enhanced, respectively, by increasing and decreasing the copy number of wild-type Dsrc41 [3].
• Strikingly, we found that several cnk loss-of-function alleles have mutations clustered in this area and provide evidence that these mutations impair Src42 binding [4].
• Src42 binding activity regulates Drosophila RAF by a novel CNK-dependent derepression mechanism [4].

Biological context of Src42A

• Furthermore, Src42A mutations enhance the dfer mutant phenotype, suggesting that Src42A and DFer act in the same cellular process [5].
• In cultured S2 embryonic cells, Ddok tyrosine phosphorylation is Src dependent; Shark associates with Ddok and Ddok localizes at the cell cortex, together with a portion of the Shark protein [6].
• To isolate genes involved in the same pathway where Src42A functions, we carried out genetic screens for dominant suppressor mutations that prevented Su(Raf)1 from suppressing Raf [7].
• Protein folding kinetic data have been obtained for the marginally stable N-terminal Src homology 3 domain of the Drosophila protein drk (drkN SH3) in an investigation of the hydrodynamic properties of its folding transition state [8].
• Fes/FER_SR shows next to best homology with the Abl family of non-receptor PTKs, while Src-related PTKs from the fresh-water sponge Spongilla lacustris are related only distantly to Fes/FER_SR [9].

Associations of Src42A with chemical compounds

• Candidate testing implicates Src42A in a similar role, suggesting conservation with a vertebrate signaling pathway involving non-receptor tyrosine kinases [10].

Other interactions of Src42A

• 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 [11].
• A genetic screen for modifiers of drosophila Src42A identifies mutations in Egfr, rolled and a novel signaling gene [7].
• Requirements of genetic interactions between Src42A, armadillo and shotgun, a gene encoding E-cadherin, for normal development in Drosophila [12].
• This work provides the first genetic evidence that both Src42A and sag are modulators of RTK signaling [7].
• Mutations in Src42A cause defects in dorsal closure similar to those seen in dfer mutant embryos [5].

References