{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ochi T"],"funding":["University of Leeds","Cancer Research UK","Medical Research Council","NHLBI NIH HHS","National Institute for Health Research (NIHR)","ShanghaiTech University","Wellcome Trust","National Institute of General Medical Sciences","NIGMS NIH HHS","University of Cambridge","Engineering and Physical Sciences Research Council","Cambridge Biomedical Research Centre"],"pagination":["674-689.e11"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7267773"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["28(6)"],"pubmed_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 functi"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions."],"pmcid":["PMC7267773"],"funding_grant_id":["101050/Z/13/Z","18796","20772","CRUK-A12874","MC_UP_1201/3","EP/M017982/1","09316/Z/10/Z","17043","C14303/A17043","C29215/A20772","R35 GM131909","GM-131909","24455","C6/A18796","R01 HL128370","207510/Z/17/Z","GM-032843","MR/P00479/1","R01 GM032843","206388/Z/17/Z","200814/Z/16/Z","MR/P000479/1"],"pubmed_authors":["Boselli F","Quarantotti V","Jullien J","Jackson SP","Rosa E Silva I","Freund SMV","Kimata Y","McLaughlin SH","Blundell TL","Barnabas DD","Dutcher SK","van Breugel M","Gergely F","Lin H","Johnson CM","Blackford AN","Goldstein RE","Ochi T"],"additional_accession":[]},"is_claimable":false,"name":"CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.","description":"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 functi","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jun","modification":"2026-04-14T09:43:01.742Z","creation":"2026-04-07T13:41:59.717Z"},"accession":"S-EPMC7267773","cross_references":{"pubmed":["32375023"],"doi":["10.1016/j.str.2020.04.010"]}}