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A more recent version of this article appeared on January 1, 2004
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Submitted on March 31, 2003
Revised on August 27, 2003
Accepted on August 28, 2003
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
-tubulin ring complex (
TuRC) 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 (
TuSC). These findings suggest that the microtubule
nucleating activity of the centrosome requires the function of CP309.
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