Evidence map›Paper›PMID 23437247›Full record

ArticlePloS one2013

MAP65 coordinate microtubule growth during bundle formation.

Virginie Stoppin-Mellet, Vincent Fache, Didier Portran, Jean-Louis Martiel, Marylin Vantard

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Near-atomic cryo-EM structure of PRC1 bound to the microtubule.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. Article
  11. Review
  12. MAP65/Ase1 promote microtubule flexibility.Molecular biology of the cell · 2013
    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

5 authors at 4 institutions in 1 country.

Virginie Stoppin-MelletLaboratoaire de Physiologie Cellulaire & Végétale, Institut de Recherches en Technologies et Sciences pour le Vivant (iRTSV), Centre National de la Recherche Scientifique/Commissariat à l'énergie atomique et aux énergies alternatives/Institut National de la Recherche Agronomique/Université Joseph Fourier (CNRS/CEA/INRA/UJF), Grenoble, France. virginie.stoppin-mellet@cea.fr
Vincent Fache
Didier Portran
Jean-Louis Martiel
Marylin Vantard
Université Joseph Fourier · FRCEA Grenoble · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInstitut de Recherches en Technologies et Sciences pour le Vivant · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules (MTs) are highly dynamical structures that play a crucial role in cell physiology. In cooperation with microtubule-associated proteins (MAPs), MTs form bundles endowing cells with specific mechanisms to control their shape or generate forces. Whether the dynamics of MTs is affected by the lateral connections that MAPs make between MTs during bundle formation is still under debate. Using in vitro reconstitution of MT bundling, we analyzed the dynamics of MT bundles generated by two plant MAP65 (MAP65-1/4), MAP65-1 being the plant ortholog of vertebrate PRC1 and yeast Ase1. MAP65-1/4 limit the amplitude of MT bundle depolymerization and increase the elongation phases. The subsequent sustained elongation of bundles is governed by the coordination of MT growth, so that MT ends come in close vicinity. We develop a model based on the assumption that both MAP65-1/4 block MT depolymerization. Model simulations reveal that rescue frequencies are higher between parallel than between anti-parallel MTs. In consequence the polarity of bundled MTs by MAP65 controls the amplitude of bundle's growth. Our results illustrate how MAP-induced MT-bundling, which is finely tuned by MT polarity, robustly coordinates MT elongation within bundles.

Indexed as

Recombinant Fusion ProteinsAnimalsArabidopsis ProteinsBrainCattleCell PolarityComputer SimulationKineticsMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalProtein MultimerizationTubulinArabidopsis ProteinsMAP65-1 protein, ArabidopsisMAP65-4 protein, ArabidopsisMicrotubule-Associated ProteinsRecombinant Fusion ProteinsTubulin

Identifiers

PMID23437247
PMCPMC3578873
OpenAlexW2017168367

What OpenQuestion holds

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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.