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Proteomic and functional analysis of the mitotic Drosophila centrosome.

MPS-Authors
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Müller,  H.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Mirgorodskaya,  E.
Max Planck Society;

Lehmann,  V.
Max Planck Society;

/persons/resource/persons50184

Habermann,  K.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

/persons/resource/persons50137

Dreher,  F.
Bioinformatics (Ralf Herwig), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Gustavsson,  N.
Max Planck Society;

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Kessler,  T.
Systems Biology (Christoph Wierling), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

/persons/resource/persons50409

Lehrach,  H.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Herwig,  R.
Max Planck Society;

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Gobom,  J.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Ploubidou,  A.
Max Planck Society;

Lange,  B. M.
Max Planck Society;

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Citation

Müller, H., Schmidt, D., Steinbrink, S., Mirgorodskaya, E., Lehmann, V., Habermann, K., et al. (2010). Proteomic and functional analysis of the mitotic Drosophila centrosome. The EMBO Journal, 29(19), 3344-3357. doi:10.1038/emboj.2010.210.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7A2C-F
Abstract
Regulation of centrosome structure, duplication and segregation is integrated into cellular pathways that control cell cycle progression and growth. As part of these pathways, numerous proteins with well-established non-centrosomal localization and function associate with the centrosome to fulfill regulatory functions. In turn, classical centrosomal components take up functional and structural roles as part of other cellular organelles and compartments. Thus, although a comprehensive inventory of centrosome components is missing, emerging evidence indicates that its molecular composition reflects the complexity of its functions. We analysed the Drosophila embryonic centrosomal proteome using immunoisolation in combination with mass spectrometry. The 251 identified components were functionally characterized by RNA interference. Among those, a core group of 11 proteins was critical for centrosome structure maintenance. Depletion of any of these proteins in Drosophila SL2 cells resulted in centrosome disintegration, revealing a molecular dependency of centrosome structure on components of the protein translation machinery, actin- and RNA-binding proteins. In total, we assigned novel centrosome-related functions to 24 proteins and confirmed 13 of these in human cells.