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Vol. 15, Issue 1, 37-45, January 2004
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Department of Embryology, Carnegie Institution of Washington and Howard Hughes Medical Institute, Baltimore, Maryland 21210
Submitted March 31, 2003;
Revised August 27, 2003;
Accepted August 28, 2003
Monitoring Editor: Tim Stearns
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. Biochemical studies reveal that this novel Drosophila centrosome protein, centrosome protein of 309 kDa (CP309), cofractionates with the 
-tubulin ring complex and the centrosome-complementing activity. We show that CP309 is required for microtubule nucleation mediated by centrosomes and that it interacts with the -tubulin small complex. These findings suggest that the microtubule-nucleating activity of the centrosome requires the function of CP309.
Abbreviations used: CaM, calmodulin; CP309, centrosome protein of 309 kDa; Dgrip, Drosophila gamma ring protein; NR, nonimmunized rabbit IgG; TuSC, -tubulin small complex; TuRC, -tubulin ring complex.
*Corresponding author. E-mail address: zheng{at}ciwemb.edu.
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