| Literature DB >> 25017693 |
Chii Shyang Fong1, Minhee Kim2, T Tony Yang3, Jung-Chi Liao3, Meng-Fu Bryan Tsou4.
Abstract
Centrioles are 9-fold symmetric structures duplicating once per cell cycle. Duplication involves self-oligomerization of the centriolar protein SAS-6, but how the 9-fold symmetry is invariantly established remains unclear. Here, we found that SAS-6 assembly can be shaped by preexisting (or mother) centrioles. During S phase, SAS-6 molecules are first recruited to the proximal lumen of the mother centriole, adopting a cartwheel-like organization through interactions with the luminal wall, rather than via their self-oligomerization activity. The removal or release of luminal SAS-6 requires Plk4 and the cartwheel protein STIL. Abolishing either the recruitment or the removal of luminal SAS-6 hinders SAS-6 (or centriole) assembly at the outside wall of mother centrioles. After duplication, the lumen of engaged mother centrioles becomes inaccessible to SAS-6, correlating with a block for reduplication. These results lead to a proposed model that centrioles may duplicate via a template-based process to preserve their geometry and copy number.Entities:
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Year: 2014 PMID: 25017693 PMCID: PMC4116473 DOI: 10.1016/j.devcel.2014.05.008
Source DB: PubMed Journal: Dev Cell ISSN: 1534-5807 Impact factor: 12.270