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© The Rockefeller University Press, 0021-9525/1997//1009 $5.00
The Journal of Cell Biology, Volume 138, Number 5, , 1997 1009-1022

Article

Heterotrimeric Kinesin-II Is Required for the Assembly of Motile 9+2 Ciliary Axonemes on Sea Urchin Embryos



Robert L. Morris and Jonathan M. Scholey

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.

Abbreviations used in this paper: MT, microtubule; SpKAP115, Strongylocentrotus purpuratus kinesin-related protein of molecular mass 85 kD; SpKRP35, Strongylocentrotus purpuratus kinesin accessory protein of molecular mass 115 kD.

In addition, we gratefully acknowledge support from National Institutes of Health (NIH) grant GM50718 to J.M. Scholey and NIH postdoctoral fellowship GM17516 to R.L. Morris.

Address all correspondence to Jonathan M. Scholey, Section of Molecular and Cellular Biology, University of California, Davis, CA 95616. Tel.: (916) 752-2271. Fax: (916) 752-1449. e-mail: jmscholey{at}ucdavis.edu


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