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The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate

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  • Qing Wei

    (Mayo Clinic
    Key Laboratory of Insect Developmental and Evolutionary Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Yingyi Zhang

    (Mayo Clinic)

  • Clementine Schouteden

    (Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna)

  • Yuxia Zhang

    (Mayo Clinic)

  • Qing Zhang

    (Mayo Clinic)

  • Jinhong Dong

    (Mayo Clinic)

  • Veronika Wonesch

    (Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna)

  • Kun Ling

    (Mayo Clinic)

  • Alexander Dammermann

    (Max F. Perutz Laboratories, Vienna Biocenter (VBC), University of Vienna)

  • Jinghua Hu

    (Mayo Clinic
    Mayo Clinic
    Mayo Translational PKD Center, Mayo Clinic)

Abstract

Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly.

Suggested Citation

  • Qing Wei & Yingyi Zhang & Clementine Schouteden & Yuxia Zhang & Qing Zhang & Jinhong Dong & Veronika Wonesch & Kun Ling & Alexander Dammermann & Jinghua Hu, 2016. "The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate," Nature Communications, Nature, vol. 7(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12437
    DOI: 10.1038/ncomms12437
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    Cited by:

    1. Yutaka Takeda & Takumi Chinen & Shunnosuke Honda & Sho Takatori & Shotaro Okuda & Shohei Yamamoto & Masamitsu Fukuyama & Koh Takeuchi & Taisuke Tomita & Shoji Hata & Daiju Kitagawa, 2024. "Molecular basis promoting centriole triplet microtubule assembly," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Xiaoyu Ma & Yingyi Zhang & Yuanyuan Zhang & Xu Zhang & Yan Huang & Kai He & Chuan Chen & Jielu Hao & Debiao Zhao & Nathan K. LeBrasseur & James L. Kirkland & Eduardo N. Chini & Qing Wei & Kun Ling & J, 2023. "A stress-induced cilium-to-PML-NB route drives senescence initiation," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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