ArticleCurrent biology : CB2015
Assembly of IFT trains at the ciliary base depends on IFT74.
Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 95 citations in OpenAlex.
- Article
- Structure Makes a Difference: IFT Complex in Ciliary Function and Ciliopathy.Cytoskeleton (Hoboken, N.J.) · 2026Review
- A lipid flippase shapes the ciliary membrane and is essential for ciliogenesis.Current biology : CB · 2025Article
- IFT139 regulates Hedgehog signaling and cilia structure through ciliary protein localization.Biology open · 2025Article
- ZO-2 is a scaffold at the centriole and mitotic spindle poles that enhances microtubule stability and supports the proper development of mitotic spindles and cilia.Cell and tissue research · 2025Article
- Delivery of intraflagellar transport proteins to the ciliary base and assembly into trains.Science advances · 2025Article
- Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- The DYRKP1 kinase regulates cell wall degradation in Chlamydomonas by inducing matrix metalloproteinase expression.The Plant cell · 2024Article
- Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins.Molecular biology of the cell · 2024Article
- Molecular and structural perspectives on protein trafficking to the primary cilium membrane.Biochemical Society transactions · 2024Review
- Identification of the principal neuropeptide MIP and its action pathway in larval settlement of the echiuran worm Urechis unicinctus.BMC genomics · 2024Article
- Defective airway intraflagellar transport underlies a combined motile and primary ciliopathy syndrome caused by IFT74 mutations.Human molecular genetics · 2023Article
- IFT74 variants cause skeletal ciliopathy and motile cilia defects in mice and humans.PLoS genetics · 2023Article
- Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train.Nature communications · 2023Article
- Article
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- A case of Bardet-Biedl syndrome caused by a recurrent variant inBiomedical reports · 2021Article
- In vivo imaging shows continued association of several IFT-A, IFT-B and dynein complexes while IFT trains U-turn at the tip.Journal of cell science · 2021Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Intraflagellar transport (IFT) moves IFT trains carrying cargoes from the cell body into the flagellum and from the flagellum back to the cell body. IFT trains are composed of complexes IFT-A and IFT-B and cargo adaptors such as the BBSome. The IFT-B core proteins IFT74 and IFT81 interact directly through central and C-terminal coiled-coil domains, and recently it was shown that the N termini of these proteins form a tubulin-binding module important for ciliogenesis. To investigate the function of IFT74 and its domains in vivo, we have utilized Chlamydomonas reinhardtii ift74 mutants. In a null mutant, lack of IFT74 destabilized IFT-B, leading to flagella assembly failure. In this null background, expression of IFT74 lacking 130 amino acids (aa) of the charged N terminus stabilized IFT-B and promoted slow assembly of nearly full-length flagella. A further truncation (lacking aa 1-196, including part of coiled-coil 1) also stabilized IFT-B, but failure in IFT-A/IFT-B interaction within the pool at the base of the flagellum prevented entry of IFT-A into the flagellum and led to severely decreased IFT injection frequency and flagellar-assembly defects. Decreased IFT-A in these short flagella resulted in aggregates of stalled IFT-B in the flagella. We conclude that IFT74 is required to stabilize IFT-B; aa 197-641 are sufficient for this function in vivo. The N terminus of IFT74 may be involved in, but is not required for, tubulin entry into flagella. It is required for association of IFT-A and IFT-B at the base of the flagellum and flagellar import of IFT-A.
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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.