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Vol. 10, Issue 2, 345-360, February 1999
Section of Molecular and Cellular Biology, University of California
at Davis, Davis, California 95616
Chemosensation in the nervous system of the nematode
Caenorhabditis elegans depends on sensory cilia, whose
assembly and maintenance requires the transport of components such as
axonemal proteins and signal transduction machinery to their site of
incorporation into ciliary structures. Members of the heteromeric
kinesin family of microtubule motors are prime candidates for playing
key roles in these transport events. Here we describe the molecular
characterization and partial purification of two heteromeric kinesin
complexes from C. elegans, heterotrimeric CeKinesin-II
and dimeric CeOsm-3. Transgenic worms expressing green fluorescent
protein driven by endogenous heteromeric kinesin promoters reveal that
both CeKinesin-II and CeOsm-3 are expressed in amphid, inner labial,
and phasmid chemosensory neurons. Additionally, immunolocalization
experiments on fixed worms show an intense concentration of
CeKinesin-II and CeOsm-3 polypeptides in the ciliated endings of these
chemosensory neurons and a punctate localization pattern in the
corresponding cell bodies and dendrites. These results, together with
the phenotypes of known mutants in the pathway of sensory ciliary
assembly, suggest that CeKinesin-II and CeOsm-3 drive the transport of
ciliary components required for sequential steps in the assembly of
chemosensory cilia.
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