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| Content Provider | PubMed Central |
|---|---|
| Author | Robinson, Carol V. Rogala, Kacper B. Dynes, Nicola J. Hatzopoulos, Georgios N. Yan, Jun Pong, Sheng Kai Deane, Charlotte M. Pierre, Gönczy Vakonakis, Ioannis |
| Editor | Hyman, Anthony A. |
| Copyright Year | 2015 |
| 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. |
| Related Links | http://dx.doi.org/10.7554/eLife.07410 |
| Starting Page | 7410 |
| File Format | |
| ISSN | 2050084X |
| e-ISSN | 2050084X |
| Journal | eLife |
| Volume Number | 4 |
| Language | English |
| Publisher | eLife Sciences Publications, Ltd |
| Publisher Date | 2015-05-29 |
| Access Restriction | Open |
| Rights Holder | eLife Sciences Publications, Ltd |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Neuroscience Immunology and Microbiology Medicine Biochemistry, Genetics and Molecular Biology |
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