|Citation||Martin, M., Ahern-Djamali, S.M., Hoffmann, F.M., Saxton, W.M. (2005). Abl Tyrosine Kinase and Its Substrate Ena/VASP Have Functional Interactions with Kinesin-1. Mol. Biol. Cell 16(9): 4225--4230. (Export to RIS)|
|Publication Type||Research paper|
|PubMed Abstract||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 and Ena. Kinesin-1 motors can carry organelles and other macromolecular cargoes from neuronal cell bodies toward terminals in fast-axonal-transport. Ena distribution in larval axons was not affected by mutations in the Khc gene, suggesting that Ena is not itself a fast transport cargo of Drosophila kinesin-1. Genetic interaction tests showed that in a background sensitized by reduced Khc gene dosage, a reduction in Abl gene dosage caused distal paralysis and axonal swellings. A concomitant reduction in ena dosage rescued those defects. These results suggest that Ena/VASP, when not inhibited by the Abl pathway, can bind Khc and reduce its transport activity in axons.|
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|Language of Publication||English|
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|Also Published As|
|Abbreviation||Mol. Biol. Cell|
|Title||Molecular Biology of the Cell|
|Data from Reference|