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Vol. 11, Issue 6, 2161-2173, June 2000
Department of Cell Biology and Neuroscience, University of Texas
Southwestern Medical Center, Dallas, Texas 75390-9039
The nature of kinesin interactions with membrane-bound organelles
and mechanisms for regulation of kinesin-based motility have both been
surprisingly difficult to define. Most kinesin is recovered in
supernatants with standard protocols for purification of motor
proteins, but kinesin recovered on membrane-bound organelles is
tightly bound. Partitioning of kinesin between vesicle and cytosolic
fractions is highly sensitive to buffer composition. Addition of either
N-ethylmaleimide or EDTA to homogenization buffers
significantly increased the fraction of kinesin bound to organelles.
Given that an antibody against kinesin light chain tandem repeats also
releases kinesin from vesicles, these observations indicated that
specific cytoplasmic factors may regulate kinesin release from
membranes. Kinesin light tandem repeats contain DnaJ-like motifs, so
the effects of hsp70 chaperones were evaluated. Hsc70 released kinesin
from vesicles in an MgATP-dependent and
N-ethylmaleimide-sensitive manner. Recombinant
kinesin light chains inhibited kinesin release by hsc70 and stimulated
the hsc70 ATPase. Hsc70 actions may provide a mechanism to regulate
kinesin function by releasing kinesin from cargo in specific
subcellular domains, thereby effecting delivery of axonally
transported materials.
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