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• W3022377312 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." @default.
• W3022377312 created "2020-05-13" @default.
• W3022377312 creator A5037995194 @default.
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• W3022377312 date "2020-05-04" @default.
• W3022377312 modified "2023-10-15" @default.
• W3022377312 title "TALPID3 and ANKRD26 selectively orchestrate FBF1 localization and cilia gating" @default.
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• W3022377312 doi "https://doi.org/10.1038/s41467-020-16042-w" @default.
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