Journal
ELIFE
Volume 4, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.07410
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Funding
- Wellcome Trust [088497/Z/09/Z]
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/J008265/1]
- European Research Council (ERC) [AdG 233335, AdG 340227, 268851]
- BBSRC [BB/J008265/1] Funding Source: UKRI
- Wellcome Trust [088497/Z/09/Z] Funding Source: Wellcome Trust
- European Research Council (ERC) [268851] Funding Source: European Research Council (ERC)
- Biotechnology and Biological Sciences Research Council [BB/J008265/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1104702] Funding Source: researchfish
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Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In Caenorhabditis elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional equivalents 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.
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