ArticleNature2015
Structure of human cytoplasmic dynein-2 primed for its power stroke.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
What it found
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Who cites it
98 citing papers in PubMed, 181 citations in OpenAlex.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- Structural and functional characterization of DNAH5 variants in a Portuguese family with primary ciliary dyskinesia.Journal of assisted reproduction and genetics · 2026Article
- A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.Nature chemical biology · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- Novel DNAH17 Splice-Site Mutations Truncating the AAA6 Domain Cause Asthenozoospermia with MMAF.Reproductive sciences (Thousand Oaks, Calif.) · 2025Article
- 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
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.Science (New York, N.Y.) · 2025Article
- Article
- Virus infection and vesicle trafficking.Frontiers in immunology · 2025Review
- Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles.Nature communications · 2024Article
- Stepping dynamics of dynein characterized by MINFLUX.bioRxiv : the preprint server for biology · 2024Article
- The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Review
- Methylation of ciliary dynein motors involves the essential cytosolic assembly factor DNAAF3/PF22.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge.Nature structural & molecular biology · 2023Article
- ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography.The EMBO journal · 2023Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Members of the dynein family, consisting of cytoplasmic and axonemal isoforms, are motors that move towards the minus ends of microtubules. Cytoplasmic dynein-1 (dynein-1) plays roles in mitosis and cellular cargo transport, and is implicated in viral infections and neurodegenerative diseases. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Here we present the crystal structure of the human cytoplasmic dynein-2 motor bound to the ATP-hydrolysis transition state analogue ADP.vanadate. The structure reveals a closure of the motor's ring of six AAA+ domains (ATPases associated with various cellular activites: AAA1-AAA6). This induces a steric clash with the linker, the key element for the generation of movement, driving it into a conformation that is primed to produce force. Ring closure also changes the interface between the stalk and buttress coiled-coil extensions of the motor domain. This drives helix sliding in the stalk which causes the microtubule binding domain at its tip to release from the microtubule. Our structure answers the key questions of how ATP hydrolysis leads to linker remodelling and microtubule affinity regulation.
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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.