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Cell. 2011 Feb 4;144(3):364-75. doi: 10.1016/j.cell.2011.01.008.

Structural basis of the 9-fold symmetry of centrioles.

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  • 1Swiss Institute for Experimental Cancer Research, School of Life Sciences, Swiss Federal Institute of Technology, EPFL, Lausanne, Switzerland.

Abstract

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.

Copyright © 2011 Elsevier Inc. All rights reserved.

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PMID:
21277013
[PubMed - indexed for MEDLINE]
PMCID:
PMC3089914
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