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Section of Molecular and Cellular Biology, University of California, Davis, California 95616
Heterotrimeric kinesin-II is a plus end-
directed microtubule (MT) motor protein consisting of
distinct heterodimerized motor subunits associated
with an accessory subunit. To probe the intracellular transport functions of kinesin-II, we microinjected fertilized sea urchin eggs with an anti-kinesin-II monoclonal antibody, and we observed a dramatic inhibition
of ciliogenesis at the blastula stage characterized by the
assembly of short, paralyzed, 9+0 ciliary axonemes that
lack central pair MTs. Control embryos show no such defect and form swimming blastulae with normal, motile, 9+2 cilia that contain kinesin-II as detected by
Western blotting. Injection of anti-kinesin-II into one
blastomere of a two-cell embryo leads to the development of chimeric blastulae covered on one side with short, paralyzed cilia, and on the other with normal,
beating cilia. We observed a unimodal length distribution of short cilia on anti-kinesin-II-injected embryos
corresponding to the first mode of the trimodal distribution of ciliary lengths observed for control embryos.
This short mode may represent a default ciliary assembly intermediate. We hypothesize that kinesin-II functions during ciliogenesis to deliver ciliary components
that are required for elongation of the assembly intermediate and for formation of stable central pair MTs.
Thus, kinesin-II plays a critical role in embryonic development by supporting the maturation of nascent cilia to
generate long motile organelles capable of producing the propulsive forces required for swimming and feeding.
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