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Papers In Press, published online ahead of print February 24, 2004
Physiology Dept., University of Pennsylvania, Philadelphia, PA 19104-6085
Corresponding Author: holzbaur{at}mail.med.upenn.edu
Cytoplasmic dynein and kinesin I are both unidirectional intracellular motors. Dynein moves cargo toward the cell center and kinesin 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.
J. Biol. Chem, 10.1074/jbc.M313472200
Submitted on December 9, 2003
Revised on February 18, 2004
Accepted on February 24, 2004
A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity
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