ArticleNature communications2013
Transition fibre protein FBF1 is required for the ciliary entry of assembled intraflagellar transport complexes.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
75 citing papers in PubMed, 123 citations in OpenAlex.
- Centrosome-Signaling Pathway Crosstalk: A Core Hub From Cellular Homeostasis to Disease.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Nonsense-mediated mRNA decay orchestrates neuronal migration and cortical lamination while modulating Reelin and ciliary gene regulatory networks.Cell reports · 2026Article
- C. elegans: An elegant experimental system for the study of cilia biology.Seminars in cell & developmental biology · 2025Review
- Cilia at the crossroad: convergence of regulatory mechanisms to govern cilia dynamics during cell signaling and the cell cycle.Cell & bioscience · 2025Review
- Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole.Molecular biology of the cell · 2025Article
- Biallelic Variants in LRRC45 Impair Ciliogenesis and Cause a Severe Neurological Disorder.Clinical genetics · 2025Article
- Neuronal guidance behaviours: the primary cilium perspective.Frontiers in cell and developmental biology · 2025Review
- Transiently formed nucleus-to-cilium microtubule arrays mediate senescence initiation in a KIFC3-dependent manner.Nature communications · 2024Article
- The ARPKD Protein DZIP1L Regulates Ciliary Protein Entry by Modulating the Architecture and Function of Ciliary Transition Fibers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Genetic mutation ofLife science alliance · 2024Article
- The relationship between intraflagellar transport and upstream protein trafficking pathways and macrocyclic lactone resistance in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2024Article
- Exercise AltersMicroRNA (Shariqah, United Arab Emirates) · 2024Article
- Article
- WDR31 displays functional redundancy with GTPase-activating proteins (GAPs) ELMOD and RP2 in regulating IFT complex and recruiting the BBSome to cilium.Life science alliance · 2023Article
- The Caenorhabditis elegans Shugoshin regulates TAC-1 in cilia.Scientific reports · 2023Article
- A stress-induced cilium-to-PML-NB route drives senescence initiation.Nature communications · 2023Article
- Single-molecule localization microscopy reveals the ultrastructural constitution of distal appendages in expanded mammalian centrioles.Nature communications · 2023Article
- Composition, organization and mechanisms of the transition zone, a gate for the cilium.EMBO reports · 2022Review
- The Primary Cilium and Neuronal Migration.Cells · 2022Review
- Cilia proteins getting to work - how do they commute from the cytoplasm to the base of cilia?Journal of cell science · 2022Review
15 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.