Evidence map›Paper›PMID 29937387›Full record

ArticleDevelopmental cell2018

CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain.

Amol Aher, Maurits Kok, Ashwani Sharma, Ankit Rai, Natacha Olieric, Ruddi Rodriguez-Garcia, Eugene A Katrukha, Tobias Weinert, Vincent Olieric, Lukas C Kapitein and 3 more

Abstract read
In one paragraph

Article in Developmental cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Review
  2. Article
  3. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
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5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Amol AherCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Maurits KokDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629 HZ Delft, the Netherlands.
Ashwani SharmaLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland.
Ankit RaiCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Natacha OliericLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland.
Ruddi Rodriguez-GarciaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Eugene A KatrukhaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Tobias WeinertLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland.
Vincent OliericSwiss Light Source, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland.
Lukas C KapiteinCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands.
Michel O SteinmetzLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland; University of Basel, Biozentrum, 4056 Basel, Switzerland.
Marileen DogteromDepartment of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, van der Maasweg 9, 2629 HZ Delft, the Netherlands.
Anna AkhmanovaCell Biology, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands. Electronic address: a.akhmanova@uu.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dynamic instability of microtubules plays a key role in controlling their organization and function, but the cellular mechanisms regulating this process are poorly understood. Here, we show that cytoplasmic linker-associated proteins (CLASPs) suppress transitions from microtubule growth to shortening, termed catastrophes, including those induced by microtubule-destabilizing agents and physical barriers. Mammalian CLASPs encompass three TOG-like domains, TOG1, TOG2, and TOG3, none of which bind to free tubulin. TOG2 is essential for catastrophe suppression, whereas TOG3 mildly enhances rescues but cannot suppress catastrophes. These functions are inhibited by the C-terminal domain of CLASP2, while the TOG1 domain can release this auto-inhibition. TOG2 fused to a positively charged microtubule-binding peptide autonomously accumulates at growing but not shrinking ends, suppresses catastrophes, and stimulates rescues. CLASPs suppress catastrophes by stabilizing growing microtubule ends, including incomplete ones, preventing their depolymerization and promoting their recovery into complete tubes. TOG2 domain is the key determinant of these activities.

Indexed as

AnimalsBinding SitesCell LineCell ProliferationChlorocebus aethiopsCOS CellsHEK293 CellsHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein DomainsSpindle ApparatusTubulinCLASP1 protein, humanCLASP2 protein, humanMicrotubule-Associated ProteinsTubulinCLASPCLIP-170EB1EB3microfabricated barriersmicrotubule dynamicssingle-molecule biophysicsTOG domaintubulinX-ray crystallography

Identifiers

PMID29937387
PMCPMC6035287

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Registered trials

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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.