The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation
Abstract
Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In C. elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional homologs across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo.
Article and author information
Author details
Copyright
© 2015, Rogala et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
Metrics
-
- 2,256
- views
-
- 518
- downloads
-
- 36
- citations
Views, downloads and citations are aggregated across all versions of this paper published by eLife.