Evidence map›Paper›PMID 25417161›Full record

ArticleCell2014

Allosteric communication in the dynein motor domain.

Gira Bhabha, Hui-Chun Cheng, Nan Zhang, Arne Moeller, Maofu Liao, Jeffrey A Speir, Yifan Cheng, Ronald D Vale

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.7field-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

64 citing papers in PubMed, 118 citations in OpenAlex.

  1. Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026
    Article
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  3. Article
  4. Review
  5. Article
  6. Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025
    Article
  7. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Stepping dynamics of dynein characterized by MINFLUX.bioRxiv : the preprint server for biology · 2024
    Article
  13. The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024
    Article
  14. Article
  15. Review
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  17. Article
  18. Article
  19. Article
  20. Article

4 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

8 authors at 3 institutions in 1 country.

Gira BhabhaHoward Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.
Hui-Chun ChengHoward Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: hccheng@life.nthu.edu.tw.
Nan ZhangHoward Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.
Arne MoellerNational Resource for Automated Molecular Microscopy, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Maofu LiaoDepartment of Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Jeffrey A SpeirNational Resource for Automated Molecular Microscopy, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Yifan ChengDepartment of Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Ronald D ValeHoward Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: ron.vale@ucsf.edu.
Howard Hughes Medical Institute · USScripps Research Institute · USUniversity of California, San Francisco · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Structure and mechanism of the dynein motorR01GM097312 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2011 to 2016
$1.5M
GPU Computing Enabled Linux Computer ClusterS10RR026814 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2010 to 2010
$228k
NCRR NIH HHS S10 RR026814NCRR NIH HHS S10RR026814NIGMS NIH HHS 9 P41 GM103310NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01GM09731NIGMS NIH HHS R01 GM097312
6 · The paper itself

Abstract

Dyneins power microtubule motility using ring-shaped, AAA-containing motor domains. Here, we report X-ray and electron microscopy (EM) structures of yeast dynein bound to different ATP analogs, which collectively provide insight into the roles of dynein's two major ATPase sites, AAA1 and AAA3, in the conformational change mechanism. ATP binding to AAA1 triggers a cascade of conformational changes that propagate to all six AAA domains and cause a large movement of the "linker," dynein's mechanical element. In contrast to the role of AAA1 in driving motility, nucleotide transitions in AAA3 gate the transmission of conformational changes between AAA1 and the linker, suggesting that AAA3 acts as a regulatory switch. Further structural and mutational studies also uncover a role for the linker in regulating the catalytic cycle of AAA1. Together, these results reveal how dynein's two major ATP-binding sites initiate and modulate conformational changes in the motor domain during motility.

Indexed as

Adenosine TriphosphateAllosteric RegulationCatalysisCrystallography, X-RayDictyosteliumDyneinsMicroscopy, ElectronModels, MolecularProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDYN1 protein, S cerevisiaeDyneinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25417161
PMCPMC4269335
OpenAlexW2058768471

What OpenQuestion holds

Textmetadata
LicenceTDM
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.