期刊
CELL
卷 144, 期 3, 页码 364-375出版社
CELL PRESS
DOI: 10.1016/j.cell.2011.01.008
关键词
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资金
- JSPS
- EMBO [ALTF-667-2007]
- Wellcome Trust
- FP7 Marie Curie Fellowship
- Oncosuisse [OCS KLS 02024-02-2007]
- ERC [AdG 233335]
- Swiss National Foundation [CRSII3_125463]
- Swiss National Science Foundation (SNF) [CRSII3_125463] Funding Source: Swiss National Science Foundation (SNF)
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.
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