Evidence map›Paper›PMID 31264960›Full record

ArticleeLife2019

Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.

Samuel E Lacey, Shaoda He, Sjors Hw Scheres, Andrew P Carter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.0field-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

56 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  4. A cryo-EM processing pipeline for microtubules using CryoSPARC.Acta crystallographica. Section D, Structural biology · 2026
    Article
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  6. Review
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  8. Review
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  12. Article
  13. Review
  14. Article
  15. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Samuel E LaceyMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0002-3807-8888
Shaoda HeMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Sjors Hw ScheresMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0002-0462-6540
Andrew P CarterMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-7292-5430
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_A025_1011Medical Research Council MC_UP_A025_1013Wellcome TrustWellcome Trust WT210711
6 · The paper itself

Abstract

Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule.

Indexed as

Cryoelectron MicroscopyAmino Acid SequenceAnimalsAxonemal DyneinsHumansMiceMicrotubulesModels, MolecularProtein BindingProtein DomainsProtein SubunitsTubulinAxonemal DyneinsProtein SubunitsTubulinaxonemeciliacryoEMdyneinE. colihumanmicrotublemolecular biophysicsmouseRelionstructural biology

Identifiers

PMID31264960
PMCPMC6629372
OpenAlexW2953716540

What OpenQuestion holds

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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.