ArticleThe Journal of biological chemistry2012
Functional architecture of the outer arm dynein conformational switch.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- 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
- 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
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain.Molecular biology of the cell · 2015Article
- Integrated control of axonemal dynein AAA(+) motors.Journal of structural biology · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dynein light chain 1 (LC1/DNAL1) is one of the most highly conserved components of ciliary axonemal outer arm dyneins, and it associates with both a heavy chain motor unit and tubulin located within the A-tubule of the axonemal outer doublet microtubules. In a variety of model systems, lack of LC1 or expression of mutant forms leads to profound defects in ciliary motility, including the failure of the hydrodynamic coupling needed for ciliary metachronal synchrony, random stalling during the power/recovery stroke transition, an aberrant response to imposed viscous load, and in some cases partial failure of motor assembly. These phenotypes have led to the proposal that LC1 acts as part of a mechanical switch to control motor function in response to alterations in axonemal curvature. Here we have used NMR chemical shift mapping to define the regions perturbed by a series of mutations in the C-terminal domain that yield a range of phenotypic effects on motility. In addition, we have identified the subdomain of LC1 involved in binding microtubules and characterized the consequences of an Asn → Ser alteration within the terminal leucine-rich repeat that in humans causes primary ciliary dyskinesia. Together, these data define a series of functional subdomains within LC1 and allow us to propose a structural model for the organization of the dynein heavy chain-LC1-microtubule ternary complex that is required for the coordinated activity of dynein motors in cilia.
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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.