Regulated assembly of a supramolecular centrosome scaffold in vitro

Jeffrey B. Woodruff, Oliver Wueseke, Valeria Viscardi, Julia Mahamid, Stacy D. Ochoa, Jakob Bunkenborg, Per O. Widlund, Andrei Pozniakovsky, Esther Zanin, Shirin Bahmanyar, Andrea Zinke, Sun Hae Hong, Marcus Decker, Wolfgang Baumeister, Jens S. Andersen, Karen Oegema, Anthony A. Hyman

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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.

Original languageEnglish (US)
Pages (from-to)808-812
Number of pages5
JournalScience
Volume348
Issue number6236
DOIs
Publication statusPublished - May 15 2015
Externally publishedYes

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Cite this

Woodruff, J. B., Wueseke, O., Viscardi, V., Mahamid, J., Ochoa, S. D., Bunkenborg, J., ... Hyman, A. A. (2015). Regulated assembly of a supramolecular centrosome scaffold in vitro. Science, 348(6236), 808-812. https://doi.org/10.1126/science.aaa3923