Evidence map›Paper›PMID 24421324›Full record

ArticleThe EMBO journal2014

γ-Tubulin Ring Complexes and EB1 play antagonistic roles in microtubule dynamics and spindle positioning.

Anaïs Bouissou, Christel Vérollet, Hélène de Forges, Laurence Haren, Yohanns Bellaïche, Franck Perez, Andreas Merdes, Brigitte Raynaud-Messina

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Anaïs BouissouCentre Biologie du Développement, UMR 5547 CNRS-UPS Toulouse 3, Toulouse Cedex 04, France.
Christel Vérollet
Hélène de Forges
Laurence Haren
Yohanns Bellaïche
Franck Perez
Andreas Merdes
Brigitte Raynaud-Messina
Centre National de la Recherche Scientifique · FRInstitut de Pharmacologie et de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

γ-Tubulin is critical for microtubule (MT) assembly and organization. In metazoa, this protein acts in multiprotein complexes called γ-Tubulin Ring Complexes (γ-TuRCs). While the subunits that constitute γ-Tubulin Small Complexes (γ-TuSCs), the core of the MT nucleation machinery, are essential, mutation of γ-TuRC-specific proteins in Drosophila causes sterility and morphological abnormalities via hitherto unidentified mechanisms. Here, we demonstrate a role of γ-TuRCs in controlling spindle orientation independent of MT nucleation activity, both in cultured cells and in vivo, and examine a potential function for γ-TuRCs on astral MTs. γ-TuRCs locate along the length of astral MTs, and depletion of γ-TuRC-specific proteins increases MT dynamics and causes the plus-end tracking protein EB1 to redistribute along MTs. Moreover, suppression of MT dynamics through drug treatment or EB1 down-regulation rescues spindle orientation defects induced by γ-TuRC depletion. Therefore, we propose a role for γ-TuRCs in regulating spindle positioning by controlling the stability of astral MTs.

Indexed as

AnimalsAnimals, Genetically ModifiedCells, CulturedDrosophilaHeLa CellsHumansMicrotubule-Associated ProteinsMicrotubulesMultiprotein ComplexesSpindle ApparatusTubulinEB1 microtubule binding proteinsMicrotubule-Associated ProteinsMultiprotein ComplexesTubulin

Identifiers

PMID24421324
PMCPMC3989606
OpenAlexW2052756081

What OpenQuestion holds

Textmetadata
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.