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CCDC61/VFL3 Is a paralog of SAS6 and promotes ciliary functions

DOI: 10.1016/j.str.2020.04.010 DOI Help

Authors: Takashi Ochi (MRC Laboratory of Molecular Biology; University of Leeds) , Valentina Quarantotti (Cancer Research UK Cambridge Institute, University of Cambridge) , Huawen Lin (Washington University School of Medicine) , Jerome Jullien (Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge; CRTI, INSERM, UNIV Nantes) , Ivan Rosa E Silva (MRC Laboratory of Molecular Biology) , Francesco Boselli (University of Cambridge) , Deepak D. Barnabas (MRC Laboratory of Molecular Biology) , Christopher M. Johnson (MRC Laboratory of Molecular Biology) , Stephen H. Mclaughlin (MRC Laboratory of Molecular Biology) , Stefan M. V. Freund (MRC Laboratory of Molecular Biology) , Andrew N. Blackford (MRC Weatherall Institute of Molecular Medicine, University of Oxford; Cancer Research UK and Medical Research Council Oxford Institute for Radiation Oncology, University of Oxford) , Yuu Kimata (University of Cambridge; ShanghaiTech University) , Raymond E. Goldstein (University of Cambridge) , Stephen P. Jackson (Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge) , Tom L. Blundell (University of Cambridge) , Susan K. Dutcher (Washington University School of Medicine) , Fanni Gergely (Cancer Research UK Cambridge Institute, University of Cambridge) , Mark Van Breugel (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure

State: Published (Approved)
Published: May 2020
Diamond Proposal Number(s): 9537

Open Access Open Access

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.

Journal Keywords: centrosome; cilia; centriole; basal body; structural biology; CCDC61; SAS6; XRCC4l; Chlamydomonas; microtubule; VFL3

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography

Added On: 12/05/2020 15:43

Documents:
1-s2.0-S0969212620301313-main.pdf

Discipline Tags:

Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)