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MBC in Press, published online ahead of print October 17, 2003
Mol. Biol. Cell 10.1091/mbc.E03-03-0191

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Submitted on March 31, 2003
Revised on August 27, 2003
Accepted on August 28, 2003

Characterization of a Drosophila centrosome protein CP309 that shares homology with Kendrin and CG-NAP

Shin-ichi Kawaguchi1 and Yixian Zheng1*

1 Department of Embryology, Carnegie Institution of Washington and Howard Hughes Medical Institute, Baltimore, MD 21210

* Corresponding author. E-mail address: zheng{at}ciwemb.edu.

The centrosome in animal cells provides a major microtubule-nucleating site that regulates the microtubule cytoskeleton temporally and spatially throughout the cell cycle. We report the identification in Drosophila melanogaster of a large coiled-coil centrosome protein that can bind to calmodulin (CaM). Biochemical studies reveal that this novel Drosophila centrosome protein, CP309 (Centrosome Protein of 309 kDa), cofractionates with the {gamma}-tubulin ring complex ({gamma}TuRC) and the centrosome complementing activity. We show that CP309 is required for microtubule nucleation mediated by centrosomes and that it interacts with the {gamma}-tubulin small complex ({gamma}TuSC). These findings suggest that the microtubule nucleating activity of the centrosome requires the function of CP309.




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