ArticleCellular and molecular life sciences : CMLS2017
IFT54 regulates IFT20 stability but is not essential for tubulin transport during ciliogenesis.
Article in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 44 citations in OpenAlex.
- 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
- Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Actin Depolymerizing Factor Destrin Regulates Cilia Development and Function during Vertebrate Embryogenesis.Development & reproduction · 2024Article
- The relationship between intraflagellar transport and upstream protein trafficking pathways and macrocyclic lactone resistance in Caenorhabditis elegans.G3 (Bethesda, Md.) · 2024Article
- Article
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- FBB18 participates in preassembly of almost all axonemal dyneins independent of R2TP complex.PLoS genetics · 2022Article
- IFT54 directly interacts with kinesin-II and IFT dynein to regulate anterograde intraflagellar transport.The EMBO journal · 2021Article
- Intraflagellar Transport Proteins as Regulators of Primary Cilia Length.Frontiers in cell and developmental biology · 2021Review
- Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control ineLife · 2020Article
- Diffusion rather than intraflagellar transport likely provides most of the tubulin required for axonemal assembly inJournal of cell science · 2020Article
- FLS2 is a CDK-like kinase that directly binds IFT70 and is required for proper ciliary disassembly in Chlamydomonas.PLoS genetics · 2020Article
- Intraflagellar transport protein RABL5/IFT22 recruits the BBSome to the basal body through the GTPase ARL6/BBS3.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Non-ciliary Roles of IFT Proteins in Cell Division and Polycystic Kidney Diseases.Frontiers in cell and developmental biology · 2020Review
- Chlamydomonas WDR92 in association with R2TP-like complex and multiple DNAAFs to regulate ciliary dynein preassembly.Journal of molecular cell biology · 2019Article
- Nourseothricin N-acetyl transferase (NAT), a new selectable marker for nuclear gene expression inPlant methods · 2019Article
- Dissecting the Vesicular Trafficking Function of IFT Subunits.Frontiers in cell and developmental biology · 2019Review
- Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intraflagellar transport (IFT) is required for ciliogenesis by ferrying ciliary components using IFT complexes as cargo adaptors. IFT54 is a component of the IFT-B complex and is also associated with cytoplasmic microtubules (MTs). Loss of IFT54 impairs cilia assembly as well as cytoplasmic MT dynamics. The N-terminal calponin homology (CH) domain of IFT54 interacts with tubulins/MTs and has been proposed to transport tubulin during ciliogenesis, whereas the C-terminal coiled-coil (CC) domain binds IFT20. However, the precise function of these domains in vivo is not well understood. We showed that in Chlamydomonas, loss of IFT54 completely blocks ciliogenesis but does not affect spindle formation and proper cell cycle progression, even though IFT54 interacts with mitotic MTs. Interestingly, IFT54 lacking the CH domain allows proper flagellar assembly. The CH domain is required for the association of IFT54 with the axoneme but not with mitotic MTs, and also regulates the flagellar import of IFT54 but not IFT81 and IFT46. The C-terminal CC domain is essential for IFT54 to bind IFT20, and for its recruitment to the basal body and incorporation into IFT complexes. Complete loss of IFT54 or the CC domain destabilizes IFT20. ift54 mutant cells expressing the CC domain alone rescue the stability of IFT20 and form stunted flagella with accumulation of both IFT-A component IFT43 and IFT-B component IFT46, indicating that IFT54 also functions in IFT turn-around at the flagellar tip.
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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.