Autor: |
Kacper B Rogala, Nicola J Dynes, Georgios N Hatzopoulos, Jun Yan, Sheng Kai Pong, Carol V Robinson, Charlotte M Deane, Pierre Gönczy, Ioannis Vakonakis |
Jazyk: |
angličtina |
Rok vydání: |
2015 |
Předmět: |
|
Zdroj: |
eLife, Vol 4 (2015) |
Druh dokumentu: |
article |
ISSN: |
2050-084X |
DOI: |
10.7554/eLife.07410 |
Popis: |
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. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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