Journal
STRUCTURE
Volume 28, Issue 6, Pages 674-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2020.04.010
Keywords
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Funding
- University of Leeds
- Medical Research Council (MRC) [MC_UP_1201/3]
- MRC LMB Cesar Milstein Fellowship
- Cancer Research UK [C14303/A17043, C6/A18796, CRUK-A12874]
- NIHR Cambridge Biomedical Research Centre
- University of Cambridge
- Hutchison Whampoa
- National Institute of General Medical Sciences [GM-032843, GM-131909]
- Wellcome Trust [09316/Z/10/Z, 200814/Z/16/Z, 206388/Z/17/Z, 101050/Z/13/Z, 207510/Z/17/Z]
- Cancer Research UK Career Development Fellowship [C29215/A20772]
- MRC [MR/P00479/1]
- ShanghaiTech University
- EPSRC [EP/M017982/1] Funding Source: UKRI
- MRC [MR/P000479/1, MC_UP_1201/3] Funding Source: UKRI
- Wellcome Trust [207510/Z/17/Z] Funding Source: Wellcome Trust
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Centrioles are cylindrical assemblies whose peripheral microtubule array displays a 9-fold rotational symmetry that is established by the scaffolding protein SAS6. Centriole symmetry can be broken by centriole-associated structures, such as the striated fibers in Chlamydomonas that are important for ciliary function. The conserved protein CCDC61/VFL3 is involved in this process, but its exact role is unclear Here, we show that CCDC61 is a paralog of SAS6. Crystal structures of CCDC61 demonstrate that it contains two homodimerization interfaces that are similar to those found in SAS6, but result in the formation of linear filaments rather than rings. Furthermore, we show that CCDC61 binds microtubules and that residues involved in CCDC61 microtubule binding are important for ciliary function in Chlamydomonas. Together, our findings suggest that CCDC61 and SAS6 functionally diverged from a common ancestor while retaining the ability to scaffold the assembly of basal body-associated structures or centrioles, respectively.
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