Abl tyrosine kinase and its substrate Ena/VASP have functional interactions with kinesin-1.

@article{Martn2005AblTK,
  title={Abl tyrosine kinase and its substrate Ena/VASP have functional interactions with kinesin-1.},
  author={M. Mart{\'i}n and Shawn M Ahern-Djamali and Francis Michael Hoffmann and William M. Saxton},
  journal={Molecular biology of the cell},
  year={2005},
  volume={16 9},
  pages={
          4225-30
        }
}
Relatively little is known about how microtubule motors are controlled or about how the functions of different cytoskeletal systems are integrated. A yeast two-hybrid screen for proteins that bind to Drosophila Enabled (Ena), an actin polymerization factor that is negatively regulated by Abl tyrosine kinase, identified kinesin heavy chain (Khc), a member of the kinesin-1 subfamily of microtubule motors. Coimmunoprecipitation from Drosophila cytosol confirmed a physical interaction between Khc… CONTINUE READING
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A genome database

  • Flybase.
  • http://flybase.bio.indiana.edu/.
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