Evidence map›Paper›PMID 23615441›Full record

ArticleMolecular biology of the cell2013

MAP65/Ase1 promote microtubule flexibility.

D Portran, M Zoccoler, J Gaillard, V Stoppin-Mellet, E Neumann, I Arnal, J L Martiel, M Vantard

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  7. The Potential Role ofPlants (Basel, Switzerland) · 2024
    Article
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  18. Article
  19. Are microtubules tension sensors?Nature communications · 2019
    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 2 institutions in 1 country.

D PortranLaboratoire de Physiologie Cellulaire et Végétale, Institut de Recherches en Technologies et Sciences pour le Vivant, UMR CNRS, CEA, INRA, Université Joseph Fourier, 38054 Grenoble, France.
M Zoccoler
J Gaillard
V Stoppin-Mellet
E Neumann
I Arnal
J L Martiel
M Vantard
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules (MTs) are dynamic cytoskeletal elements involved in numerous cellular processes. Although they are highly rigid polymers with a persistence length of 1-8 mm, they may exhibit a curved shape at a scale of few micrometers within cells, depending on their biological functions. However, how MT flexural rigidity in cells is regulated remains poorly understood. Here we ask whether MT-associated proteins (MAPs) could locally control the mechanical properties of MTs. We show that two major cross-linkers of the conserved MAP65/PRC1/Ase1 family drastically decrease MT rigidity. Their MT-binding domain mediates this effect. Remarkably, the softening effect of MAP65 observed on single MTs is maintained when MTs are cross-linked. By reconstituting physical collisions between growing MTs/MT bundles, we further show that the decrease in MT stiffness induced by MAP65 proteins is responsible for the sharp bending deformations observed in cells when they coalign at a steep angle to create bundles. Taken together, these data provide new insights into how MAP65, by modifying MT mechanical properties, may regulate the formation of complex MT arrays.

Indexed as

AlgorithmsAnimalsArabidopsisArabidopsis ProteinsBrainCattleGreen Fluorescent ProteinsKineticsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalModels, ChemicalModels, MolecularPliabilityRecombinant Fusion ProteinsArabidopsis ProteinsGreen Fluorescent ProteinsMAP65-1 protein, ArabidopsisMAP65-4 protein, ArabidopsisMicrotubule-Associated ProteinsRecombinant Fusion ProteinsTubulin

Identifiers

PMID23615441
PMCPMC3681700
OpenAlexW2149359374

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.