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

ABSTRACT: 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 gamma-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 gamma-tubulin small complex. These findings suggest that the microtubule-nucleating activity of the centrosome requires the function of CP309.

SUBMITTER: Kawaguchi S

PROVIDER: S-EPMC307525 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature

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

Kawaguchi Shin-ichi S Zheng Yixian Y

Molecular biology of the cell 20031017 1

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 gamma-tubulin ring complex and the centrosome-complementing acti ...[more]

PMID: 14565985

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