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Centrosomes are important cell organizers. They consist of a pair of centrioles surrounded by pericentriolar material (PCM) that expands dramatically during mitosis-a process termed centrosome maturation. How centrosomes mature remains mysterious. Here, we identify a domain in Drosophila Cnn that appears to be phosphorylated by Polo/Plk1 specifically at centrosomes during mitosis. The phosphorylation promotes the assembly of a Cnn scaffold around the centrioles that is in constant flux, with Cnn molecules recruited continuously around the centrioles as the scaffold spreads slowly outward. Mutations that block Cnn phosphorylation strongly inhibit scaffold assembly and centrosome maturation, whereas phosphomimicking mutations allow Cnn to multimerize in vitro and to spontaneously form cytoplasmic scaffolds in vivo that organize microtubules independently of centrosomes. We conclude that Polo/Plk1 initiates the phosphorylation-dependent assembly of a Cnn scaffold around centrioles that is essential for efficient centrosome maturation in flies.

Original publication

DOI

10.1016/j.devcel.2014.02.013

Type

Journal article

Journal

Dev Cell

Publication Date

31/03/2014

Volume

28

Pages

659 - 669

Keywords

Amino Acid Sequence, Animals, Animals, Genetically Modified, Brain, Cell Cycle Proteins, Cells, Cultured, Centrosome, Cytoplasm, Drosophila Proteins, Drosophila melanogaster, Homeodomain Proteins, Image Processing, Computer-Assisted, Immunoprecipitation, Microtubules, Mitosis, Molecular Sequence Data, Phosphorylation, Protein Multimerization, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Two-Hybrid System Techniques