ArticleMolecular biology of the cell2013
WD60/FAP163 is a dynein intermediate chain required for retrograde intraflagellar transport in cilia.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Structure and tethering mechanism of dynein-2 intermediate chains in intraflagellar transport.The EMBO journal · 2024Article
- Review
- 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
- Disease-associated mutations in WDR34 lead to diverse impacts on the assembly and function of dynein-2.Journal of cell science · 2023Article
- Review
- A novel WDR60 variant contributes to a late diagnosis of Jeune asphyxiating thoracic dystrophy in a Chinese patient: A case report.Clinical case reports · 2022Article
- Consensus nomenclature for dyneins and associated assembly factors.The Journal of cell biology · 2022Article
- WDR60-mediated dynein-2 loading into cilia powers retrograde IFT and transition zone crossing.The Journal of cell biology · 2022Article
- Ciliary Dyneins and Dynein Related Ciliopathies.Cells · 2021Review
- Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020Review
- Pharmacological or genetic targeting of Transient Receptor Potential (TRP) channels can disrupt the planarian escape response.PloS one · 2019Article
- Dynein-2 intermediate chains play crucial but distinct roles in primary cilia formation and function.eLife · 2018Article
- Emerging mechanisms of dynein transport in the cytoplasm versus the cilium.Biochemical Society transactions · 2018Review
- Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the dynein-2 complex is crucial for ciliary protein trafficking.Molecular biology of the cell · 2018Article
- Intraflagellar transport: mechanisms of motor action, cooperation, and cargo delivery.The FEBS journal · 2017Review
- Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements.Nature structural & molecular biology · 2017Article
- Intraflagellar Transport and Ciliary Dynamics.Cold Spring Harbor perspectives in biology · 2017Review
- Evolution of Cilia.Cold Spring Harbor perspectives in biology · 2017Review
- The role of the dynein light intermediate chain in retrograde IFT and flagellar function in Chlamydomonas.Molecular biology of the cell · 2016Article
- A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia.Molecular biology of the cell · 2016Article
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4 authors.
Funding
Abstract
Retrograde intraflagellar transport (IFT) is required for assembly of cilia. We identify a Chlamydomonas flagellar protein (flagellar-associated protein 163 [FAP163]) as being closely related to the D1bIC(FAP133) intermediate chain (IC) of the dynein that powers this movement. Biochemical analysis revealed that FAP163 is present in the flagellar matrix and is actively trafficked by IFT. Furthermore, FAP163 copurified with D1bIC(FAP133) and the LC8 dynein light chain, indicating that it is an integral component of the retrograde IFT dynein. To assess the functional role of FAP163, we generated an RNA interference knockdown of the orthologous protein (WD60) in planaria. The Smed-wd60(RNAi) animals had a severe ciliary assembly defect that dramatically compromised whole-organism motility. Most cilia were present as short stubs that had accumulated large quantities of IFT particle-like material between the doublet microtubules and the membrane. The few remaining approximately full-length cilia had a chaotic beat with a frequency reduced from 24 to ∼10 Hz. Thus WD60/FAP163 is a dynein IC that is absolutely required for retrograde IFT and ciliary assembly.
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