ArticleMolecular biology of the cell2016
Structure and function of outer dynein arm intermediate and light chain complex.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- A Compound Heterozygous Missense Variant in TheInternational journal of fertility & sterility · 2026Article
- Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.Nature structural & molecular biology · 2025Article
- Proteomic analysis reveals molecular changes following genetic engineering in Chlamydomonas reinhardtii.BMC microbiology · 2024Article
- Novel PathogenicJournal of pediatric genetics · 2023Article
- Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.Nature structural & molecular biology · 2021Article
- Article
- Emerging Genotype-Phenotype Relationships in Primary Ciliary Dyskinesia.International journal of molecular sciences · 2021Review
- Defects in the cytoplasmic assembly of axonemal dynein arms cause morphological abnormalities and dysmotility in sperm cells leading to male infertility.PLoS genetics · 2021Article
- Structure of a microtubule-bound axonemal dynein.Nature communications · 2021Article
- Cryo-electron tomography of cardiac myofibrils reveals a 3D lattice spring within the Z-discs.Communications biology · 2020Article
- Article
- Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.PLoS genetics · 2017Article
- Electrostatic interaction between polyglutamylated tubulin and the nexin-dynein regulatory complex regulates flagellar motility.Molecular biology of the cell · 2017Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo-electron tomography and structural labeling. We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo. These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs.
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