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Centrosomes. Regulated assembly of a supramolecular centrosome scaffold in vitro.

MPS-Authors
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Woodruff,  Jeffrey
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Wueseke,  Oliver
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Mahamid,  J.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Widlund,  Per
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Pozniakovsky,  Andrei I.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zinke,  Andrea
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Decker,  Markus
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

Baumeister,  W.
Max Planck Society;

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Oegema,  Karen
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Hyman,  Anthony
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Woodruff, J., Wueseke, O., Viscardi, V., Mahamid, J., Ochoa, S. D., Bunkenborg, J., et al. (2015). Centrosomes. Regulated assembly of a supramolecular centrosome scaffold in vitro. Science (New York, N.Y.), 348(6236), 808-812.


Cite as: https://hdl.handle.net/21.11116/0000-0001-0406-4
Abstract
The centrosome organizes microtubule arrays within animal cells and comprises two centrioles surrounded by an amorphous protein mass called the pericentriolar material (PCM). Despite the importance of centrosomes as microtubule-organizing centers, the mechanism and regulation of PCM assembly are not well understood. In Caenorhabditis elegans, PCM assembly requires the coiled-coil protein SPD-5. We found that recombinant SPD-5 could polymerize to form micrometer-sized porous networks in vitro. Network assembly was accelerated by two conserved regulators that control PCM assembly in vivo, Polo-like kinase-1 and SPD-2/Cep192. Only the assembled SPD-5 networks, and not unassembled SPD-5 protein, functioned as a scaffold for other PCM proteins. Thus, PCM size and binding capacity emerge from the regulated polymerization of one coiled-coil protein to form a porous network.