4yv4
From Proteopedia
Structure of the C. elegans SAS-5 coiled coil domain
Structural highlights
Function[SAS5_CAEEL] Required for centrosome duplication. Essential for daughter-centriole formation. Requires both maternal and partenal expression, suggesting that it regulates centriole duplication during both spermatogenesis and early embryogenesis.[1] [2] Publication Abstract from PubMedCentrioles 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. The protein SAS-5 forms large oligomeric assemblies critical for centriole formation.,Rogala KB, Dynes NJ, Hatzopoulos GN, Yan J, Pong SK, Robinson CV, Deane CM, Gonczy P, Vakonakis I Elife. 2015 May 29;4. doi: 10.7554/eLife.07410. PMID:26023830[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
