Evidence map›Paper›PMID 25209998›Full record

ArticleeLife2014

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins.

Joseph Atherton, Irene Farabella, I-Mei Yu, Steven S Rosenfeld, Anne Houdusse, Maya Topf, Carolyn A Moores

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

77 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  8. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  9. Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
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  12. Article
  13. Review
  14. Review
  15. Article
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  20. Article

17 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 4 institutions in 3 countries.

Joseph AthertonInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, United Kingdom.
Irene FarabellaInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, United Kingdom.
I-Mei YuStructural Motility, Institut Curie, Centre National de la Recherche Scientifique, Paris, France.
Steven S RosenfeldDepartment of Cancer Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, United States.
Anne HoudusseStructural Motility, Institut Curie, Centre National de la Recherche Scientifique, Paris, France.
Maya TopfInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, United Kingdom.
Carolyn A MooresInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, United Kingdom.
Birkbeck, University of London · GBInstitut Curie · FRCleveland Clinic Lerner College of Medicine · USInstitute of Structural and Molecular Biology · GB

Funding

Mechanisms of Processivity in Molecular MotorsR01GM102875 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI YI, QING · 2012 to 2015
$1.2M
Biotechnology and Biological Sciences Research Council BB/K01692X/1Medical Research Council MR/J000973/1NIGMS NIH HHS R01 GM102875NIGMS NIH HHS R01GM102875-07
6 · The paper itself

Abstract

Kinesins are a superfamily of microtubule-based ATP-powered motors, important for multiple, essential cellular functions. How microtubule binding stimulates their ATPase and controls force generation is not understood. To address this fundamental question, we visualized microtubule-bound kinesin-1 and kinesin-3 motor domains at multiple steps in their ATPase cycles--including their nucleotide-free states--at ∼ 7 Å resolution using cryo-electron microscopy. In both motors, microtubule binding promotes ordered conformations of conserved loops that stimulate ADP release, enhance microtubule affinity and prime the catalytic site for ATP binding. ATP binding causes only small shifts of these nucleotide-coordinating loops but induces large conformational changes elsewhere that allow force generation and neck linker docking towards the microtubule plus end. Family-specific differences across the kinesin-microtubule interface account for the distinctive properties of each motor. Our data thus provide evidence for a conserved ATP-driven mechanism for kinesins and reveal the critical mechanistic contribution of the microtubule interface.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateBinding SitesBiological TransportBiomechanical PhenomenaConserved SequenceCryoelectron MicroscopyHumansKinesinsKineticsMagnesiumMicrotubulesModels, MolecularProtein BindingProtein Structure, SecondaryAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateKinesinsMagnesiumATPasebiophysicscryo-electron microscopycytoskeletonhumankinesinmicrotubulemotorstructural biology

Identifiers

PMID25209998
PMCPMC4358365
OpenAlexW2165041848

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.