TALPID3 and ANKRD26 selectively orchestrate FBF1 localization and cilia gating

Hao Yan, Chuan Chen, Huicheng Chen, Hui Hong, Yan Huang, Kun Ling, Jinghua Hu () and Qing Wei ()
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Hao Yan: CAS Key Laboratory of Insect Developmental and Evolutionary Biology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences
Chuan Chen: Department of Biochemistry and Molecular Biology, Mayo Clinic
Huicheng Chen: CAS Key Laboratory of Insect Developmental and Evolutionary Biology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences
Hui Hong: CAS Key Laboratory of Insect Developmental and Evolutionary Biology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences
Yan Huang: Department of Biochemistry and Molecular Biology, Mayo Clinic
Kun Ling: Department of Biochemistry and Molecular Biology, Mayo Clinic
Jinghua Hu: Department of Biochemistry and Molecular Biology, Mayo Clinic
Qing Wei: Center for Reproduction and Health Development, Institute of Biomedicine and Biotechnology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences (CAS)

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract Transition fibers (TFs) regulate cilia gating and make the primary cilium a distinct functional entity. However, molecular insights into the biogenesis of a functional cilia gate remain elusive. In a forward genetic screen in Caenorhabditis elegans, we uncover that TALP-3, a homolog of the Joubert syndrome protein TALPID3, is a TF-associated component. Genetic analysis reveals that TALP-3 coordinates with ANKR-26, the homolog of ANKRD26, to orchestrate proper cilia gating. Mechanistically, TALP-3 and ANKR-26 form a complex with key gating component DYF-19, the homolog of FBF1. Co-depletion of TALP-3 and ANKR-26 specifically impairs the recruitment of DYF-19 to TFs. Interestingly, in mammalian cells, TALPID3 and ANKRD26 also play a conserved role in coordinating the recruitment of FBF1 to TFs. We thus report a conserved protein module that specifically regulates the functional component of the ciliary gate and suggest a correlation between defective gating and ciliopathy pathogenesis.

Date: 2020
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DOI: 10.1038/s41467-020-16042-w

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