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Vol. 9, Issue 3, 637-652, March 1998
*Department of Cell Biology, Harvard Medical School, Boston,
Massachusetts 02115; and Department of Neurology, Beth Israel Deaconess
Medical Center, Harvard Institutes of Medicine, Boston, Massachusetts
02115
We have cloned from rat brain the cDNA encoding an 89,828-Da
kinesin-related polypeptide KIF3C that is enriched in brain, retina,
and lung. Immunocytochemistry of hippocampal neurons in culture shows
that KIF3C is localized to cell bodies, dendrites, and, in lesser
amounts, to axons. In subcellular fractionation experiments, KIF3C
cofractionates with a distinct population of membrane vesicles. Native
KIF3C binds to microtubules in a kinesin-like, nucleotide-dependent
manner. KIF3C is most similar to mouse KIF3B and KIF3A, two closely
related kinesins that are normally present as a heteromer. In sucrose
density gradients, KIF3C sediments at two distinct densities,
suggesting that it may be part of two different multimolecular
complexes. Immunoprecipitation experiments show that KIF3C is in part
associated with KIF3A, but not with KIF3B. Unlike KIF3B, a significant
portion of KIF3C is not associated with KIF3A. Consistent with these
biochemical properties, the distribution of KIF3C in the CNS has both
similarities and differences compared with KIF3A and KIF3B. These
results suggest that KIF3C is a vesicle-associated motor that functions
both independently and in association with KIF3A.
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