Evidence map›Paper›PMID 29420470›Full record

ArticleNature2018

Cryo-EM shows how dynactin recruits two dyneins for faster movement.

Linas Urnavicius, Clinton K Lau, Mohamed M Elshenawy, Edgar Morales-Rios, Carina Motz, Ahmet Yildiz, Andrew P Carter

Abstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers.

0numbers the graph read from it
0cells of the map it votes in
182citing papers in PubMed
–field-weighted citation impact
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

182 citing papers in PubMed.

  1. Article
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  9. Review
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  15. Article
  16. Dynein upsizes under load.Nature cell biology · 2026
    Article
  17. Article
  18. A mutation inMolecular vision · 2026
    Article
  19. Review
  20. Article

122 more citing papers are in PubMed but not listed here.

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

7 authors.

Linas UrnaviciusMedical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Clinton K LauMedical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Mohamed M ElshenawyDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA.
Edgar Morales-RiosDepartment of Biochemistry, CINVESTAV, México D.F., Mexico.
Carina MotzMedical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Ahmet YildizDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA.
Andrew P CarterMedical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK.

Funding

Understanding the Mechanism and Regulation of the Human Cytoplasmic Dynein ComplexR01GM094522 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI YILDIZ, AHMET · 2011 to 2019
$2.8M
Structural and Functional Characterization of Telomere Protection and MaintenanceR01GM118773 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI YILDIZ, AHMET · 2016 to 2019
$1.2M
Medical Research Council MC_UP_A025_1011NIGMS NIH HHS R01 GM094522NIGMS NIH HHS R01 GM118773Wellcome Trust 210711/Z/18/Z
6 · The paper itself

Abstract

Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.

Indexed as

Cryoelectron MicroscopyMovementAdaptor Proteins, Vesicular TransportAnimalsBiological TransportDynactin ComplexDyneinsHumansMiceMicrotubule-Associated ProteinsMicrotubulesModels, MolecularSingle Molecule ImagingSwineAdaptor Proteins, Vesicular TransportBicd2 protein, mouseBicdl1 protein, mouseDynactin ComplexDyneinshook3 protein, humanMicrotubule-Associated Proteins

Identifiers

PMID29420470
PMCPMC5988349

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Registered trials

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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.