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A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity.

Authors: Ligon, LA  Tokito, M  Finklestein, JM  Grossman, FE  Holzbaur, EL 
Citation: Ligon LA, etal., J Biol Chem. 2004 Apr 30;279(18):19201-8. Epub 2004 Feb 24.
Pubmed: (View Article at PubMed) PMID:14985359
DOI: Full-text: DOI:10.1074/jbc.M313472200

Cytoplasmic dynein and kinesin I are both unidirectional intracellular motors. Dynein moves cargo toward the cell center, and kinesin moves cargo toward the cell periphery. There is growing evidence that bi-directional motility is regulated in the cell, potentially through direct interactions between oppositely oriented motors. We have identified a direct interaction between cytoplasmic dynein and kinesin I. Using the yeast two-hybrid assay and affinity chromatography, we demonstrate that the intermediate chain of dynein binds to kinesin light chains 1 and 2. The interaction is both direct and specific. Co-immunoprecipitation experiments demonstrate an interaction between endogenous proteins in rat brain cytosol. Double-label immunocytochemistry reveals a partial co-localization of vesicle-associated motor proteins. Together these observations suggest that soluble motors can interact, potentially allowing kinesin I to actively localize dynein to cellular sites of function. There is also a vesicle population with both dynein and kinesin I bound that may be capable of bi-directional motility along cellular microtubules.

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CRRD Object Information
CRRD ID: 8553555
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.