Evidence map›Paper›PMID 29185983›Full record

ArticleeLife2017

NuMA recruits dynein activity to microtubule minus-ends at mitosis.

Christina L Hueschen, Samuel J Kenny, Ke Xu, Sophie Dumont

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.2field-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

70 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
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  10. Review
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  12. Article
  13. Kinesin Spindle Protein (KIF11) in Mitosis and Cancer.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Molecular design principles for bipolar spindle organization by two opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

10 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

4 authors at 2 institutions in 1 country.

Christina L HueschenDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-3437-2895
Samuel J KennyDepartment of Chemistry, University of California, Berkeley, Berkeley, United States.
Ke XuDepartment of Chemistry, University of California, Berkeley, Berkeley, United States.ORCID 0000-0002-2788-194X
Sophie DumontDepartment of Cell and Tissue Biology, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-8283-1523
University of California, Berkeley · USUniversity of California, San Francisco · US

Funding

Rewiring cellular architecture to probe mechanical signal processing at kinetochoresDP2GM119177 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DUMONT, SOPHIE · 2015 to 2015
$2.4M
NIGMS NIH HHS DP2 GM119177
6 · The paper itself

Abstract

To build the spindle at mitosis, motors exert spatially regulated forces on microtubules. We know that dynein pulls on mammalian spindle microtubule minus-ends, and this localized activity at ends is predicted to allow dynein to cluster microtubules into poles. How dynein becomes enriched at minus-ends is not known. Here, we use quantitative imaging and laser ablation to show that NuMA targets dynactin to minus-ends, localizing dynein activity there. NuMA is recruited to new minus-ends independently of dynein and more quickly than dynactin; both NuMA and dynactin display specific, steady-state binding at minus-ends. NuMA localization to minus-ends involves a C-terminal region outside NuMA's canonical microtubule-binding domain and is independent of minus-end binders γ-TuRC, CAMSAP1, and KANSL1/3. Both NuMA's minus-end-binding and dynein-dynactin-binding modules are required to rescue focused, bipolar spindle organization. Thus, NuMA may serve as a mitosis-specific minus-end cargo adaptor, targeting dynein activity to minus-ends to cluster spindle microtubules into poles.

Indexed as

MitosisAntigens, NuclearCell Cycle ProteinsCell LineDyneinsHumansMicrotubulesNuclear Matrix-Associated ProteinsProtein BindingSpindle ApparatusAntigens, NuclearCell Cycle ProteinsDyneinsNuclear Matrix-Associated ProteinsNUMA1 protein, humancell biologydyneinhumanmicrotubuleminus-endmitosisPotorous tridactylusspindle

Identifiers

PMID29185983
PMCPMC5706958
OpenAlexW2768851671

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.