ArticleThe Journal of cell biology2009
An outer arm dynein light chain acts in a conformational switch for flagellar motility.
Article in The Journal of cell biology, 2009. 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, 52 citations in OpenAlex.
- Isoform-specific phosphorylation of axonemal dynein heavy chains.Molecular biology of the cell · 2025Article
- Outer-arm dynein light chain LC1 is required for normal motor assembly kinetics, ciliary stability, and motility.Molecular biology of the cell · 2023Article
- Review
- 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
- 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
- Direction of flagellum beat propagation is controlled by proximal/distal outer dynein arm asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 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
- Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain.Molecular biology of the cell · 2015Article
- The oligomeric outer dynein arm assembly factor CCDC103 is tightly integrated within the ciliary axoneme and exhibits periodic binding to microtubules.The Journal of biological chemistry · 2015Article
- The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane.Molecular & cellular proteomics : MCP · 2014Article
- A solid-state control system for dynein-based ciliary/flagellar motility.The Journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A system distinct from the central pair-radial spoke complex was proposed to control outer arm dynein function in response to alterations in the mechanical state of the flagellum. In this study, we examine the role of a Chlamydomonas reinhardtii outer arm dynein light chain that associates with the motor domain of the gamma heavy chain (HC). We demonstrate that expression of mutant forms of LC1 yield dominant-negative effects on swimming velocity, as the flagella continually beat out of phase and stall near or at the power/recovery stroke switchpoint. Furthermore, we observed that LC1 interacts directly with tubulin in a nucleotide-independent manner and tethers this motor unit to the A-tubule of the outer doublet microtubules within the axoneme. Therefore, this dynein HC is attached to the same microtubule by two sites: via both the N-terminal region and the motor domain. We propose that this gamma HC-LC1-microtubule ternary complex functions as a conformational switch to control outer arm activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.