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CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.

Authors :
Ochi T
Quarantotti V
Lin H
Jullien J
Rosa E Silva I
Boselli F
Barnabas DD
Johnson CM
McLaughlin SH
Freund SMV
Blackford AN
Kimata Y
Goldstein RE
Jackson SP
Blundell TL
Dutcher SK
Gergely F
van Breugel M
Source :
Structure (London, England : 1993) [Structure] 2020 Jun 02; Vol. 28 (6), pp. 674-689.e11. Date of Electronic Publication: 2020 May 05.
Publication Year :
2020

Abstract

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.<br />Competing Interests: Declaration of Interests The authors declare no competing interests.<br /> (Copyright © 2020 MRC Laboratory of Molecular Biology. Published by Elsevier Ltd.. All rights reserved.)

Details

Language :
English
ISSN :
1878-4186
Volume :
28
Issue :
6
Database :
MEDLINE
Journal :
Structure (London, England : 1993)
Publication Type :
Academic Journal
Accession number :
32375023
Full Text :
https://doi.org/10.1016/j.str.2020.04.010