ArticleMolecular biology of the cell2015
Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 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
- Review
- Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility.Molecular biology of the cell · 2023Article
- 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
- 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
- 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.The Journal of biological chemistry · 2020Article
- WDR92 is required for axonemal dynein heavy chain stability in cytoplasm.Molecular biology of the cell · 2019Article
- Turning dyneins off bends cilia.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Parasite motility is critical for virulence of African trypanosomes.Scientific reports · 2018Article
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- Axonemal Dynein Arms.Cold Spring Harbor perspectives in biology · 2016Review
- Structure and function of outer dynein arm intermediate and light chain complex.Molecular biology of the cell · 2016Article
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11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The outer arm dynein (OAD) complex is the main propulsive force generator for ciliary/flagellar beating. In Chlamydomonas and Tetrahymena, the OAD complex comprises three heavy chains (α, β, and γ HCs) and >10 smaller subunits. Dynein light chain-1 (LC1) is an essential component of OAD. It is known to associate with the Chlamydomonas γ head domain, but its precise localization within the γ head and regulatory mechanism of the OAD complex remain unclear. Here Ni-NTA-nanogold labeling electron microscopy localized LC1 to the stalk tip of the γ head. Single-particle analysis detected an additional structure, most likely corresponding to LC1, near the microtubule-binding domain (MTBD), located at the stalk tip. Pull-down assays confirmed that LC1 bound specifically to the γ MTBD region. Together with observations that LC1 decreased the affinity of the γ MTBD for microtubules, we present a new model in which LC1 regulates OAD activity by modulating γ MTBD's affinity for the doublet microtubule.
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