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

Qing Wei, Qingwen Xu, Yuxia Zhang, Yujie Li, Qing Zhang, Zeng Hu, Peter C Harris, Vicente Torres, Kun Ling, Jinghua Hu

Research output: Contribution to journalArticle

43 Citations (Scopus)

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.

Original languageEnglish (US)
Article number3750
JournalNature Communications
Volume4
DOIs
StatePublished - Nov 15 2013

Fingerprint

Cilia
entry
proteins
fibers
Fibers
Caenorhabditis elegans
machinery
Organelles
Machinery
Embryonic Development
Tissue homeostasis
Proteins
Homeostasis
Maintenance
Genome
homeostasis
worms
organelles
genome
transit

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)
  • Physics and Astronomy(all)

Cite this

Transition fibre protein FBF1 is required for the ciliary entry of assembled intraflagellar transport complexes. / Wei, Qing; Xu, Qingwen; Zhang, Yuxia; Li, Yujie; Zhang, Qing; Hu, Zeng; Harris, Peter C; Torres, Vicente; Ling, Kun; Hu, Jinghua.

In: Nature Communications, Vol. 4, 3750, 15.11.2013.

Research output: Contribution to journalArticle

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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.",
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AU - Li, Yujie

AU - Zhang, Qing

AU - Hu, Zeng

AU - Harris, Peter C

AU - Torres, Vicente

AU - Ling, Kun

AU - Hu, Jinghua

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N2 - 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.

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