Evidence map›Paper›PMID 24015359›Full record

ArticleeLife2013

Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains.

Marvin E Tanenbaum, Ronald D Vale, Richard J McKenney

Open access · goldAbstract read
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

48 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Reconstitution of Neuronal Motor Traffic on Septin-Associated Microtubules.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
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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

3 authors at 2 institutions in 1 country.

Marvin E TanenbaumDepartment Cellular and Molecular Pharmacology , Howard Hughes Medical Institute, University of California, San Francisco , San Francisco , United States.
Ronald D Vale
Richard J McKenney
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

Microtubule Complexes Involved in Intracelluar TransportR37GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2006 to 2015
$3.2M
Structure and mechanism of the dynein motorR01GM097312 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2011 to 2016
$1.5M
Tuning the Biophysical Properties of Dynein 2 for Intraflagellar TransportF32GM096484 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MCKENNEY, RICHARD JAMES · 2011 to 2013
$148k
NIGMS NIH HHS F32 GM096484NIGMS NIH HHS F32GM096484NIGMS NIH HHS R01 GM097312NIGMS NIH HHS R01GM097312NIGMS NIH HHS R37 GM038499NIGMS NIH HHS R37GM038499
6 · The paper itself

Abstract

Cytoplasmic dynein is the predominant minus-end-directed microtubule (MT) motor in most eukaryotic cells. In addition to transporting vesicular cargos, dynein helps to organize MTs within MT networks such as mitotic spindles. How dynein performs such non-canonical functions is unknown. Here we demonstrate that dynein crosslinks and slides anti-parallel MTs in vitro. Surprisingly, a minimal dimeric motor lacking a tail domain and associated subunits can cause MT sliding. Single molecule imaging reveals that motors pause and frequently reverse direction when encountering an anti-parallel MT overlap, suggesting that the two motor domains can bind both MTs simultaneously. In the mitotic spindle, inward microtubule sliding by dynein counteracts outward sliding generated by kinesin-5, and we show that a tailless, dimeric motor is sufficient to drive this activity in mammalian cells. Our results identify an unexpected mechanism for dynein-driven microtubule sliding, which differs from filament sliding mechanisms described for other motor proteins. DOI:http://dx.doi.org/10.7554/eLife.00943.001.

Indexed as

CytoplasmDimerizationDyneinsMicrotubulesDyneinscytoskeletondyneinEg5HumanmicrotubulemitosisS. cerevisiaespindle

Identifiers

PMID24015359
PMCPMC3762337
OpenAlexW2154235253

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.