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

Takashi Ochi, Valentina Quarantotti, Huawen Lin, Jerome Jullien, Ivan Rosa e Silva, Francesco Boselli, Deepak D. Barnabas, Christopher M. Johnson, Stephen H. McLaughlin, Stefan M.V. Freund, Andrew N. Blackford, Yuu Kimata, Raymond E. Goldstein, Stephen P. Jackson, Tom L. Blundell, Susan K. Dutcher, Fanni Gergely, Mark van Breugel

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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.

Original languageEnglish
Pages (from-to)674-689.e11
JournalStructure
Volume28
Issue number6
DOIs
StatePublished - Jun 2 2020

Keywords

  • CCDC61
  • Chlamydomonas
  • SAS6
  • VFL3
  • XRCC4
  • basal body
  • centriole
  • centrosome
  • cilia
  • microtubule
  • structural biology

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