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Transition fibre protein FBF1 is required for the ciliary entry of assembled intraflagellar transport complexes

Author

Listed:
  • Qing Wei

    (Mayo Clinic)

  • Qingwen Xu

    (Mayo Clinic)

  • Yuxia Zhang

    (Mayo Clinic)

  • Yujie Li

    (Mayo Clinic)

  • Qing Zhang

    (Mayo Clinic)

  • Zeng Hu

    (Mayo Clinic)

  • Peter C. Harris

    (Mayo Clinic
    Mayo Translational PKD Center)

  • Vicente E. Torres

    (Mayo Clinic
    Mayo Translational PKD Center)

  • Kun Ling

    (Mayo Clinic
    Mayo Translational PKD Center)

  • Jinghua Hu

    (Mayo Clinic
    Mayo Clinic
    Mayo Translational PKD Center)

Abstract

Sensory organelle cilia have critical roles in mammalian embryonic development and tissue homeostasis. Intraflagellar transport (IFT) machinery is required for the assembly and maintenance of cilia. Yet, how this large complex passes through the size-dependent barrier at the ciliary base remains enigmatic. Here we report that FBF1, a highly conserved transition fibre protein, is required for the ciliary import of assembled IFT particles at the ciliary base. We cloned dyf-19, the Caenorhabditis elegans homologue of human FBF1, in a whole-genome screen for ciliogenesis mutants. DYF-19 localizes specifically to transition fibres and interacts directly with the IFT-B component DYF-11/IFT54. Although not a structural component of transition fibres, DYF-19 is required for the transit of assembled IFT particles through the ciliary base. Furthermore, we found that human FBF1 shares conserved localization and function with its worm counterpart. We conclude that FBF1 is a key functional transition fibre component that actively facilitates the ciliary entry of assembled IFT machinery.

Suggested Citation

  • Qing Wei & Qingwen Xu & Yuxia Zhang & Yujie Li & Qing Zhang & Zeng Hu & Peter C. Harris & Vicente E. Torres & Kun Ling & Jinghua Hu, 2013. "Transition fibre protein FBF1 is required for the ciliary entry of assembled intraflagellar transport complexes," Nature Communications, Nature, vol. 4(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3750
    DOI: 10.1038/ncomms3750
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    Cited by:

    1. Ting-Jui Ben Chang & Jimmy Ching-Cheng Hsu & T. Tony Yang, 2023. "Single-molecule localization microscopy reveals the ultrastructural constitution of distal appendages in expanded mammalian centrioles," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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