ArticleThe Journal of biological chemistry2020
The complex of outer-arm dynein light chain-1 and the microtubule-binding domain of the γ heavy chain shows how axonemal dynein tunes ciliary beating.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.The EMBO journal · 2025Article
- Article
- CFAP410 has a bimodular architecture with a conserved surface patch on its N-terminal leucine-rich repeat motif for binding interaction partners.Frontiers in cell and developmental biology · 2025Article
- Comparative transcriptome analysis reveals molecular damage associated with cryopreservation in Crassostrea angulata D-larvae rather than to cryoprotectant exposure.BMC genomics · 2024Article
- Review
- Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility.Molecular biology of the cell · 2023Article
- Article
- Regulation of motor activity of ciliary outer-arm dynein by the light chain 1; Implications from the structure of the light chain bound to the microtubule-binding domain of the heavy chain.Biophysics and physicobiology · 2023Article
- Light chain 2 is a Tctex-type related axonemal dynein light chain that regulates directional ciliary motility in Trypanosoma brucei.PLoS pathogens · 2022Article
- Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.Nature structural & molecular biology · 2021Article
- Article
- Cytoplasmic factories for axonemal dynein assembly.Journal of cell science · 2021Article
- Heme-binding protein CYB5D1 is a radial spoke component required for coordinated ciliary beating.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure of a microtubule-bound axonemal dynein.Nature communications · 2021Article
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Authors and funding
5 authors.
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Abstract
Axonemal dynein is a microtubule-based molecular motor that drives ciliary/flagellar beating in eukaryotes. In axonemal dynein, the outer-arm dynein (OAD) complex, which comprises three heavy chains (α, β, and γ), produces the main driving force for ciliary/flagellar motility. It has recently been shown that axonemal dynein light chain-1 (LC1) binds to the microtubule-binding domain (MTBD) of OADγ, leading to a decrease in its microtubule-binding affinity. However, it remains unclear how LC1 interacts with the MTBD and controls the microtubule-binding affinity of OADγ. Here, we have used X-ray crystallography and pulldown assays to examine the interaction between LC1 and the MTBD, identifying two important sites of interaction in the MTBD. Solving the LC1-MTBD complex from
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