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Vol. 9, Issue 2, 249-261, February 1998
Howard Hughes Medical Institute, Division of Cellular and Molecular
Medicine, Department of Pharmacology, University of California San
Diego, La Jolla, CA 92093-0683
Proteins of the kinesin superfamily define a class of
microtubule-dependent motors that play crucial roles in cell division and intracellular transport. To study the molecular mechanism of axonal
transport, a cDNA encoding a new kinesin-like protein called KIF3C was
cloned from a mouse brain cDNA library. Sequence and secondary
structure analysis revealed that KIF3C is a member of the KIF3 family.
In contrast to KIF3A and KIF3B, Northern and Western analysis indicated
that KIF3C expression is highly enriched in neural tissues such as
brain, spinal cord, and retina. When anti-KIF3C antibodies were used to
stain the cerebellum, the strongest signal came from the cell bodies
and dendrites of Purkinje cells. In retina, anti-KIF3C mainly stains
the ganglion cells. Immunolocalization showed that the KIF3C motor in
spinal cord and sciatic nerve is mainly localized in cytoplasm. In
spinal cord, the KIF3C staining was punctate; double labeling with
anti-giantin and anti-KIF3C showed a clear concentration of the motor
protein in the Golgi complex. Staining of ligated sciatic nerves
demonstrated that the KIF3C motor accumulated at the proximal side of
the ligated nerve, which suggests that KIF3C is an anterograde motor.
Immunoprecipitation experiments revealed that KIF3C and KIF3A, but not
KIF3B, were coprecipitated. These data, combined with previous data
from other labs, indicate that KIF3C and KIF3B are "variable"
subunits that associate with a common KIF3A subunit, but not with each
other. Together these results suggest that KIF3 family members
combinatorially associate to power anterograde axonal transport.
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