ArticleNature structural & molecular biology2021
Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 89 citations in OpenAlex.
- Post-LECA Origin and Diversification of an Axonemal Outer Arm Dynein Motor.Cytoskeleton (Hoboken, N.J.) · 2026Review
- A Compound Heterozygous Missense Variant in TheInternational journal of fertility & sterility · 2026Article
- A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.Nature chemical biology · 2026Article
- Article
- Atomic models of the Toxoplasma cell invasion machinery.Nature structural & molecular biology · 2026Article
- 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
- Advances in high-resolution imaging of centrioles and cilia.Journal of cell science · 2025Review
- The wavelength of the ciliary beat in Chlamydomonas saturates at long ciliary lengths.Biophysical journal · 2025Article
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Isoform-specific phosphorylation of axonemal dynein heavy chains.Molecular biology of the cell · 2025Article
- InhaledProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes.Molecular biology of the cell · 2025Article
- An amino acid-resolution interactome for motile cilia identifies the structure and function of ciliopathy protein complexes.Developmental cell · 2025Article
- Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.Science (New York, N.Y.) · 2025Article
- DNAHX: a novel, non-motile dynein heavy chain subfamily, identified by cryo-EM endogenously.bioRxiv : the preprint server for biology · 2025Article
- Molecular basis for the assembly of the dynein transport machinery on microtubules.bioRxiv : the preprint server for biology · 2024Article
- Inherently disordered regions of axonemal dynein assembly factors.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Structure, interaction and nervous connectivity of beta cell primary cilia.Nature communications · 2024Article
- ARL3 GTPases facilitate ODA16 unloading from IFT in motile cilia.Science advances · 2024Article
- Cytoplasmic preassembly of the flagellar outer dynein arm complex inMolecular biology of the cell · 2024Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Thousands of outer-arm dyneins (OADs) are arrayed in the axoneme to drive a rhythmic ciliary beat. Coordination among multiple OADs is essential for generating mechanical forces to bend microtubule doublets (MTDs). Using electron microscopy, we determined high-resolution structures of Tetrahymena thermophila OAD arrays bound to MTDs in two different states. OAD preferentially binds to MTD protofilaments with a pattern resembling the native tracks for its distinct microtubule-binding domains. Upon MTD binding, free OADs are induced to adopt a stable parallel conformation, primed for array formation. Extensive tail-to-head (TTH) interactions between OADs are observed, which need to be broken for ATP turnover by the dynein motor. We propose that OADs in an array sequentially hydrolyze ATP to slide the MTDs. ATP hydrolysis in turn relaxes the TTH interfaces to effect free nucleotide cycles of downstream OADs. These findings lead to a model explaining how conformational changes in the axoneme produce coordinated action of dyneins.
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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.