Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled.

@article{Comer1998PhosphorylationOE,
  title={Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled.},
  author={Allen R Comer and Shawn M Ahern-Djamali and J L Juang and Paul D. Jackson and Francis Michael Hoffmann},
  journal={Molecular and cellular biology},
  year={1998},
  volume={18 1},
  pages={152-60}
}
Drosophila Enabled (Ena) is a member of a family of cytoskeleton-associated proteins including mammalian vasodilator-stimulated phosphoprotein and murine Enabled that regulate actin cytoskeleton assembly. Mutations in Drosophila ena were discovered as dominant genetic suppressors of mutations in the Abelson tyrosine kinase (Abl), suggesting that Ena and Abl function in the same pathway or process. We have identified six tyrosine residues on Ena that are phosphorylated by Abl in vitro and in… CONTINUE READING

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