Evidence map›Paper›PMID 27916523›Full record

ArticleCurrent biology : CB2016

Localized Mechanical Stress Promotes Microtubule Rescue.

Hélène de Forges, Antoine Pilon, Isabelle Cantaloube, Antoine Pallandre, Anne-Marie Haghiri-Gosnet, Franck Perez, Christian Poüs

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Current biology : CB, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.1field-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

47 citing papers in PubMed, 103 citations in OpenAlex.

  1. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Article
  7. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  8. A tubulin-MAPKKK pathway engages tubulin isotype interaction for neuroprotection.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
  11. Article
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  13. Article
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  15. Article
  16. Phase separation of +TIP networks regulates microtubule dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Theory of tip structure-dependent microtubule catastrophes and damage-induced microtubule rescues.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Hélène de ForgesInstitut Curie, PSL Research University, CNRS UMR 144, rue d'Ulm, 75246 Paris Cedex 05, France.
Antoine PilonINSERM UMR-S 1193, Univ. Paris-Sud, Université Paris-Saclay, rue Jean-Baptiste Clément, 92296 Châtenay-Malabry, France; Biochimie, APHP, Hôpitaux Universitaires de l'Est Parisien, Site St Antoine, rue du Faubourg Saint Antoine, 75571 Paris Cedex 12, France.
Isabelle CantaloubeINSERM UMR-S 1193, Univ. Paris-Sud, Université Paris-Saclay, rue Jean-Baptiste Clément, 92296 Châtenay-Malabry, France.
Antoine PallandreCNRS UPR 20, Laboratoire de Photonique et Nanostructures, route de Nozay, F-91460 Marcoussis, France; Univ. Paris-Sud, Université Paris-Saclay, Faculté de Pharmacie, rue Jean-Baptiste Clément, 92296 Châtenay-Malabry, France.
Anne-Marie Haghiri-GosnetCNRS UPR 20, Laboratoire de Photonique et Nanostructures, route de Nozay, F-91460 Marcoussis, France.
Franck PerezInstitut Curie, PSL Research University, CNRS UMR 144, rue d'Ulm, 75246 Paris Cedex 05, France. Electronic address: franck.perez@curie.fr.
Christian PoüsINSERM UMR-S 1193, Univ. Paris-Sud, Université Paris-Saclay, rue Jean-Baptiste Clément, 92296 Châtenay-Malabry, France; Biochimie-Hormonologie, APHP, Hôpitaux Universitaires Paris-Sud, Site Antoine Béclère, rue de la Porte de Trivaux, 92141 Clamart, France. Electronic address: christian.pous@u-psud.fr.
Université Paris-Sud · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule dynamics rely on the properties of tubulin and are regulated by microtubule-associated proteins. GTP-tubulin assembles into hollow polymers, which can depolymerize upon GTP hydrolysis. Depolymerizing microtubules may stop shrinking and resume growth. Such rescues are regulated by microtubule-associated proteins like CLIP-170 and the CLASPs [1, 2]. Microtubule domains prone to rescues contain discrete regions (previously termed "GTP islands") that retain a GTP-tubulin-like conformation in the main body of the microtubule [3]. However, the exact nature of these domains and the mechanisms controlling their occurrence and distribution are largely unknown. Here we show that collisions between growing microtubules and mechanical obstacles (including other microtubules) in vitro result in the higher abundance of GTP-like islands in stressed microtubule regions. Furthermore, these islands were found to be efficiently generated by both lateral contacts and mechanical constraints applied to the main body of the microtubules. They were also particularly prominent where shifts in the number of protofilaments occur in the microtubule lattice. GTP-like islands and rescues frequently co-occurred at microtubule intersections in vitro and in living cells, both in crossing and in crossed microtubules. We also observed that CLIP-170 recognizes GTP-like islands in vivo and is retained at microtubule crossings. Therefore, we propose that rescues occur via a two-stage mechanism: (1) lattice defects determine potential rescue-promoting islands in the microtubule structure, and (2) CLIP-170 detects these islands to stimulate microtubule rescue. Our results reveal the interplay between rescue-promoting factors and microtubule architecture and organization to control microtubule dynamics.

Indexed as

AnimalsCell LineGuanosine TriphosphateMicrotubulesMolecular Dynamics SimulationPolymersProtein ConformationGuanosine TriphosphatePolymersCLIP-170cytoskeletonGTP islandsmechanical stressmicrotubule crossingsmicrotubule dynamicsmicrotubule rescue

Identifiers

PMID27916523
OpenAlexW2557808664

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.