ArticleThe Journal of biological chemistry2016
Overall Architecture of the Intraflagellar Transport (IFT)-B Complex Containing Cluap1/IFT38 as an Essential Component of the IFT-B Peripheral Subcomplex.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Multiomics studies reveal how ambient temperature changes govern cellular responses of Chlamydomonas.The Plant cell · 2026Article
- In-depth analysis of obesity-associated changes in adipose tissue-derived mesenchymal stromal/stem cells and primary cilia function.Communications biology · 2025Article
- Assembly and mother centriole recruitment of IFT-B subcomplexes to form IFT-B holocomplex.Cell structure and function · 2025Article
- Coordinated roles of the CEP164 homodimer and TTBK2 are required for recruitment of the IFT machinery to the mother centriole for ciliogenesis.Molecular biology of the cell · 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
- RZZ-Spindly and CENP-E form an integrated platform to recruit dynein to the kinetochore corona.The EMBO journal · 2023Article
- The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.Nature structural & molecular biology · 2023Article
- A mechanism that integrates microtubule motors of opposite polarity at the kinetochore corona.bioRxiv : the preprint server for biology · 2023Article
- Multiple interactions of the dynein-2 complex with the IFT-B complex are required for effective intraflagellar transport.Journal of cell science · 2023Article
- Functional hierarchy among different Rab27 effectors involved in secretory granule exocytosis.eLife · 2023Article
- The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023Review
- Paralog-specific TTC30 regulation of Sonic hedgehog signaling.Frontiers in molecular biosciences · 2023Article
- Appearing and disappearing acts of cilia.Journal of biosciences · 2023Review
- Article
- Biochemically validated structural model of the 15-subunit intraflagellar transport complex IFT-B.The EMBO journal · 2022Article
- CEP19-RABL2-IFT-B axis controls BBSome-mediated ciliary GPCR export.Molecular biology of the cell · 2022Article
- Molecular basis underlying the ciliary defects caused byMolecular biology of the cell · 2022Article
- TTC30A and TTC30B Redundancy Protects IFT Complex B Integrity and Its Pivotal Role in Ciliogenesis.Genes · 2022Article
- Munc13b stimulus-dependently accumulates on granuphilin-mediated, docked granules prior to fusion.Cell structure and function · 2022Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intraflagellar transport (IFT) is essential for assembly and maintenance of cilia and flagella as well as ciliary motility and signaling. IFT is mediated by multisubunit complexes, including IFT-A, IFT-B, and the BBSome, in concert with kinesin and dynein motors. Under high salt conditions, purified IFT-B complex dissociates into a core subcomplex composed of at least nine subunits and at least five peripherally associated proteins. Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively. In particular, we identified TTC26/IFT56 and Cluap1/IFT38, neither of which was included with certainty in previous models of the IFT-B complex, as integral components of the core and peripheral subcomplexes, respectively. Consistent with this, a ciliogenesis defect of Cluap1-deficient mouse embryonic fibroblasts was rescued by exogenous expression of wild-type Cluap1 but not by mutant Cluap1 lacking the binding ability to other IFT-B components. The detailed interaction map as well as comparison of subcellular localization of IFT-B components between wild-type and Cluap1-deficient cells provides insights into the functional relevance of the architecture of the IFT-B complex.
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