Evidence map›Paper›PMID 22863569›Full record

ArticleStructure (London, England : 1993)2012

ATP-driven remodeling of the linker domain in the dynein motor.

Anthony J Roberts, Bara Malkova, Matt L Walker, Hitoshi Sakakibara, Naoki Numata, Takahide Kon, Reiko Ohkura, Thomas A Edwards, Peter J Knight, Kazuo Sutoh and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 97 citations in OpenAlex.

  1. Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026
    Article
  2. Article
  3. Review
  4. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Article
  7. Stepping dynamics of dynein characterized by MINFLUX.bioRxiv : the preprint server for biology · 2024
    Article
  8. The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024
    Article
  9. Frontiers in cell and developmental biology · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble.International journal of molecular sciences · 2020
    Review
  19. Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Anthony J RobertsAstbury Centre for Structural Molecular Biology, Institute of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. anthony_roberts@hms.harvard.edu
Bara Malkova
Matt L Walker
Hitoshi Sakakibara
Naoki Numata
Takahide Kon
Reiko Ohkura
Thomas A Edwards
Peter J Knight
Kazuo Sutoh
Kazuhiro Oiwa
Stan A Burgess
University of Leeds · GBThe University of Tokyo · JPNational Institute of Information and Communications Technology · JP

Funding

Biotechnology and Biological Sciences Research Council BB/E00928X/1Wellcome TrustWellcome Trust 078115/Z/05/ZWellcome Trust 080709/Z/06/ZWellcome Trust 092436/Z/10/Z
6 · The paper itself

Abstract

Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped enzymes, but how they harness this architecture to produce movement is poorly understood. Here, we have used cryo-EM to determine 3D maps of native flagellar dynein-c and a cytoplasmic dynein motor domain in different nucleotide states. The structures show key sites of conformational change within the AAA+ ring and a large rearrangement of the "linker" domain, involving a hinge near its middle. Analysis of a mutant in which the linker "undocks" from the ring indicates that linker remodeling requires energy that is supplied by interactions with the AAA+ modules. Fitting the dynein-c structures into flagellar tomograms suggests how this mechanism could drive sliding between microtubules, and also has implications for cytoplasmic cargo transport.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAxonemal DyneinsAxonemeChlamydomonas reinhardtiiCryoelectron MicroscopyDictyosteliumMicroscopy, VideoMicrotubulesModels, MolecularPlant ProteinsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryProtozoan ProteinsStructural Homology, ProteinAdenosine DiphosphateAdenosine TriphosphateAxonemal DyneinsPlant ProteinsProtozoan Proteins

Identifiers

PMID22863569
PMCPMC3469822
OpenAlexW2019327581

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.