Evidence map›Paper›PMID 28602352›Full record

ArticleCell2017

Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated.

Kai Zhang, Helen E Foster, Arnaud Rondelet, Samuel E Lacey, Nadia Bahi-Buisson, Alexander W Bird, Andrew P Carter

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 183 papers.

0numbers the graph read from it
0cells of the map it votes in
183citing papers in PubMed
16.0field-weighted citation impact, top 1% 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

183 citing papers in PubMed, 326 citations in OpenAlex.

  1. Article
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  5. AnbioRxiv : the preprint server for biology · 2026
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  17. Dynein upsizes under load.Nature cell biology · 2026
    Article
  18. Article
  19. Review
  20. Review

123 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 at 3 institutions in 3 countries.

Kai ZhangMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Helen E FosterMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Arnaud RondeletMax Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Samuel E LaceyMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Nadia Bahi-BuissonDepartment of Pediatric Neurology, Université Paris Descartes, Imaging Institute, INSERM U781, Paris, France.
Alexander W BirdMax Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.
Andrew P CarterMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK. Electronic address: cartera@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GBMax Planck Institute of Molecular Physiology · DEDélégation Paris 5 · FR

Funding

Medical Research Council MC_UP_A025_1011Wellcome TrustWorldwide Cancer Research 16-0093
6 · The paper itself

Abstract

Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves poorly on its own or how it is activated by dynactin. Here, we present a cryoelectron microscopy structure of the complete 1.4-megadalton human dynein-1 complex in an inhibited state known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor domains locks them in a conformation with low microtubule affinity. Disrupting motor dimerization with structure-based mutagenesis drives dynein-1 into an open form with higher affinity for both microtubules and dynactin. We find the open form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail directly stimulates its motor activity.

Indexed as

AnimalsCryoelectron MicroscopyCytoplasmic DyneinsDimerizationDynactin ComplexHumansMiceMicrotubulesModels, MolecularMolecular Motor ProteinsMultiprotein ComplexesSf9 CellsSpodopteraSwineCytoplasmic DyneinsDynactin ComplexMolecular Motor ProteinsMultiprotein Complexesactivationauto-inhibitioncryo-EMdynactindyneinmicrotubulemotorphi-particle

Identifiers

PMID28602352
PMCPMC5473941
OpenAlexW2623370846

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.