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The centriole, and the related basal body, is an ancient organelle characterized by a universal 9-fold radial symmetry and is critical for generating cilia, flagella, and centrosomes. The mechanisms directing centriole formation are incompletely understood and represent a fundamental open question in biology. Here, we demonstrate that the centriolar protein SAS-6 forms rod-shaped homodimers that interact through their N-terminal domains to form oligomers. We establish that such oligomerization is essential for centriole formation in C. elegans and human cells. We further generate a structural model of the related protein Bld12p from C. reinhardtii, in which nine homodimers assemble into a ring from which nine coiled-coil rods radiate outward. Moreover, we demonstrate that recombinant Bld12p self-assembles into structures akin to the central hub of the cartwheel, which serves as a scaffold for centriole formation. Overall, our findings establish a structural basis for the universal 9-fold symmetry of centrioles.

Original publication

DOI

10.1016/j.cell.2011.01.008

Type

Journal article

Journal

Cell

Publication Date

04/02/2011

Volume

144

Pages

364 - 375

Keywords

Amino Acid Sequence, Animals, Caenorhabditis, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Cycle Proteins, Cell Line, Centrioles, Humans, Models, Molecular, Molecular Sequence Data, Protein Multimerization, Recombinant Proteins, Sequence Alignment