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- W2103166169 abstract "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." @default.
- W2103166169 created "2016-06-24" @default.
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- W2103166169 date "2015-05-29" @default.
- W2103166169 modified "2023-10-18" @default.
- W2103166169 title "The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation" @default.
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- W2103166169 doi "https://doi.org/10.7554/elife.07410" @default.
- W2103166169 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4471805" @default.
- W2103166169 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26023830" @default.
- W2103166169 hasPublicationYear "2015" @default.
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