ArticlePloS one2012
Dissecting the sequential assembly and localization of intraflagellar transport particle complex B in Chlamydomonas.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 61 citations in OpenAlex.
- Structure Makes a Difference: IFT Complex in Ciliary Function and Ciliopathy.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Ift46 deficiency causes renal cyst via enhanced Limk2 through lack of autophagy flux.Cell communication and signaling : CCS · 2026Article
- Assembly and mother centriole recruitment of IFT-B subcomplexes to form IFT-B holocomplex.Cell structure and function · 2025Article
- Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole.Molecular biology of the cell · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Review
- The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.Nature structural & molecular biology · 2023Article
- Article
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- Cilia proteins getting to work - how do they commute from the cytoplasm to the base of cilia?Journal of cell science · 2022Review
- Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins.Molecular biology of the cell · 2021Article
- Diffusion rather than intraflagellar transport likely provides most of the tubulin required for axonemal assembly inJournal of cell science · 2020Article
- Intraflagellar transport protein 74 is essential for spermatogenesis and male fertility in mice†.Biology of reproduction · 2019Article
- Review
- Crystal structure of intraflagellar transport protein 80 reveals a homo-dimer required for ciliogenesis.eLife · 2018Article
- Rab GTPases in cilium formation and function.Small GTPases · 2018Review
- The N-terminus of IFT46 mediates intraflagellar transport of outer arm dynein and its cargo-adaptor ODA16.Molecular biology of the cell · 2017Article
- Article
- Structural basis of outer dynein arm intraflagellar transport by the transport adaptor protein ODA16 and the intraflagellar transport protein IFT46.The Journal of biological chemistry · 2017Article
- Building a multipurpose insertional mutant library for forward and reverse genetics inPlant methods · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intraflagellar transport (IFT), the key mechanism for ciliogenesis, involves large protein particles moving bi-directionally along the entire ciliary length. IFT particles contain two large protein complexes, A and B, which are constructed with proteins in a core and several peripheral proteins. Prior studies have shown that in Chlamydomonas reinhardtii, IFT46, IFT52, and IFT88 directly interact with each other and are in a subcomplex of the IFT B core. However, ift46, bld1, and ift88 mutants differ in phenotype as ift46 mutants are able to form short flagella, while the other two lack flagella completely. In this study, we investigated the functional differences of these individual IFT proteins contributing to complex B assembly, stability, and basal body localization. We found that complex B is completely disrupted in bld1 mutant, indicating an essential role of IFT52 for complex B core assembly. Ift46 mutant cells are capable of assembling a relatively intact complex B, but such complex is highly unstable and prone to degradation. In contrast, in ift88 mutant cells the complex B core still assembles and remains stable, but the peripheral proteins no longer attach to the B core. Moreover, in ift88 mutant cells, while complex A and the anterograde IFT motor FLA10 are localized normally to the transition fibers, complex B proteins instead are accumulated at the proximal ends of the basal bodies. In addition, in bld2 mutant, the IFT complex B proteins still localize to the proximal ends of defective centrioles which completely lack transition fibers. Taken together, these results revealed a step-wise assembly process for complex B, and showed that the complex first localizes to the proximal end of the centrioles and then translocates onto the transition fibers via an IFT88-dependent mechanism.
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