Neurodegenerative Mutation in Cytoplasmic Dynein Alters Its Organization and Dynein-Dynactin and Dynein-Kinesin Interactions*

@article{Deng2010NeurodegenerativeMI,
  title={Neurodegenerative Mutation in Cytoplasmic Dynein Alters Its Organization and Dynein-Dynactin and Dynein-Kinesin Interactions*},
  author={Wenhan Deng and Caroline A Garrett and Benjamin Dombert and Violetta Soura and Gareth T. Banks and Elizabeth M. C. Fisher and Marcel P. van der Brug and Majid Hafezparast},
  journal={The Journal of Biological Chemistry},
  year={2010},
  volume={285},
  pages={39922 - 39934}
}
A single amino acid change, F580Y (Legs at odd angles (Loa), Dync1h1Loa), in the highly conserved and overlapping homodimerization, intermediate chain, and light intermediate chain binding domain of the cytoplasmic dynein heavy chain can cause severe motor and sensory neuron loss in mice. The mechanism by which the Loa mutation impairs the neuron-specific functions of dynein is not understood. To elucidate the underlying molecular mechanisms of neurodegeneration arising from this mutation, we… Expand
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