Evidence map›Paper›PMID 25109325›Full record

ArticleNature communications2014

Tension on the linker gates the ATP-dependent release of dynein from microtubules.

Frank B Cleary, Mark A Dewitt, Thomas Bilyard, Zaw Min Htet, Vladislav Belyy, Danna D Chan, Amy Y Chang, Ahmet Yildiz

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.3field-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

52 citing papers in PubMed, 97 citations in OpenAlex.

  1. Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  8. Multicolor Tracking of Molecular Motors at Nanometer Resolution.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Ultrafast Force-Clamp Spectroscopy of Microtubule-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Three-color single-molecule imaging reveals conformational dynamics of dynein undergoing motility.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021
    Review
  18. Article
  19. 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

8 authors at 1 institution in 1 country.

Frank B ClearyBiophysics Graduate Group, University of California, Berkeley, California 94720, USA.
Mark A DewittBiophysics Graduate Group, University of California, Berkeley, California 94720, USA.
Thomas BilyardDepartment of Physics, University of California, Berkeley, California 94720, USA.
Zaw Min HtetDepartment of Physics, University of California, Berkeley, California 94720, USA.
Vladislav BelyyBiophysics Graduate Group, University of California, Berkeley, California 94720, USA.
Danna D ChanDepartment of Physics, University of California, Berkeley, California 94720, USA.
Amy Y ChangDepartment of Physics, University of California, Berkeley, California 94720, USA.
Ahmet YildizDepartment of Physics, University of California, Berkeley, California 94720, USA.
University of California, Berkeley · US

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
NIGMS NIH HHS GM094522NIGMS NIH HHS R01 GM094522
6 · The paper itself

Abstract

Cytoplasmic dynein is a dimeric motor that transports intracellular cargoes towards the minus end of microtubules (MTs). In contrast to other processive motors, stepping of the dynein motor domains (heads) is not precisely coordinated. Therefore, the mechanism of dynein processivity remains unclear. Here, by engineering the mechanical and catalytic properties of the motor, we show that dynein processivity minimally requires a single active head and a second inert MT-binding domain. Processivity arises from a high ratio of MT-bound to unbound time, and not from interhead communication. In addition, nucleotide-dependent microtubule release is gated by tension on the linker domain. Intramolecular tension sensing is observed in dynein's stepping motion at high interhead separations. On the basis of these results, we propose a quantitative model for the stepping characteristics of dynein and its response to chemical and mechanical perturbation.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsCytoplasmDyneinsGlutathione TransferaseGreen Fluorescent ProteinsMicrotubulesMonte Carlo MethodMotionMutationNucleotidesOptics and PhotonicsProtein ConformationProtein EngineeringProtein MultimerizationAdenosine TriphosphatasesAdenosine TriphosphateDyneinsGlutathione TransferaseGreen Fluorescent ProteinsNucleotides

Identifiers

PMID25109325
PMCPMC4129465
OpenAlexW2161951202

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.