ArticleMolecular biology of the cell2007
Chlamydomonas outer arm dynein alters conformation in response to Ca2+.
Article in Molecular biology of the cell, 2007. 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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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.
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Who cites it
33 citing papers in PubMed, 75 citations in OpenAlex.
- Heme-binding protein CYB5D1 couples intraflagellar redox to calcium signaling for coordinated flagellar beating.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Review
- Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes.Molecular biology of the cell · 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
- Calaxin stabilizes the docking of outer arm dyneins onto ciliary doublet microtubule in vertebrates.eLife · 2023Article
- Calcium signal transmission by axonemal microtubules as an optimized information pathway in cilia and flagella.Journal of bioenergetics and biomembranes · 2021Article
- Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.Nature structural & molecular biology · 2021Article
- Chlamydomonas reinhardtii cellular compartments and their contribution to intracellular calcium signalling.Journal of experimental botany · 2021Review
- 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
- Calcium signaling modulates the dynamics of cilia and flagella.European biophysics journal : EBJ · 2020Article
- WDR92 is required for axonemal dynein heavy chain stability in cytoplasm.Molecular biology of the cell · 2019Article
- Intracellular Ca2+ threshold reversibly switches flagellar beat off and on.Biology of reproduction · 2018Article
- The flagellar protein Enkurin is required for mouse sperm motility and for transport through the female reproductive tract.Biology of reproduction · 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
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- Axonemal Dynein Arms.Cold Spring Harbor perspectives in biology · 2016Review
- Two-headed outer- and inner-arm dyneins ofBiochemistry and biophysics reports · 2015Article
- Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
We have previously shown that Ca(2+) directly activates ATP-sensitive microtubule binding by a Chlamydomonas outer arm dynein subparticle containing the beta and gamma heavy chains (HCs). The gamma HC-associated LC4 light chain is a member of the calmodulin family and binds 1-2 Ca(2+) with K(Ca) = 3 x 10(-5) M in vitro, suggesting it may act as a Ca(2+) sensor for outer arm dynein. Here we investigate interactions between the LC4 light chain and gamma HC. Two IQ consensus motifs for binding calmodulin-like proteins are located within the stem domain of the gamma heavy chain. In vitro experiments indicate that LC4 undergoes a Ca(2+)-dependent interaction with the IQ motif domain while remaining tethered to the HC. LC4 also moves into close proximity of the intermediate chain IC1 in the presence of Ca(2+). The sedimentation profile of the gamma HC subunit changed subtly upon Ca(2+) addition, suggesting that the entire complex had become more compact, and electron microscopy of the isolated gamma subunit revealed a distinct alteration in conformation of the N-terminal stem in response to Ca(2+) addition. We propose that Ca(2+)-dependent conformational change of LC4 has a direct effect on the stem domain of the gamma HC, which eventually leads to alterations in mechanochemical interactions between microtubules and the motor domain(s) of the outer dynein arm.
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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.