Evidence map›Paper›PMID 29021343›Full record

ArticleMolecular biology of the cell2017

Tubulin isoform composition tunes microtubule dynamics.

Annapurna Vemu, Joseph Atherton, Jeffrey O Spector, Carolyn A Moores, Antonina Roll-Mecak

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

116 citing papers in PubMed, 184 citations in OpenAlex.

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  13. The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 2026
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56 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Annapurna VemuCell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Lung and Blood Institute, Bethesda, MD 20892.
Joseph AthertonInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London WC1E 7HX, United Kingdom.
Jeffrey O SpectorCell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Lung and Blood Institute, Bethesda, MD 20892.
Carolyn A MooresInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London WC1E 7HX, United Kingdom.
Antonina Roll-MecakCell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Lung and Blood Institute, Bethesda, MD 20892 Antonina@mail.nih.gov.
Institute of Structural and Molecular Biology · GBNational Institute of Neurological Disorders and Stroke · USNational Heart Lung and Blood Institute · US

Funding

Readout of the tubulin code by cellular effectorsZIANS003164 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2017 to 2025
$11.7M
Medical Research Council MR/J000973/1Medical Research Council MR/R000352/1
6 · The paper itself

Abstract

Microtubules polymerize and depolymerize stochastically, a behavior essential for cell division, motility, and differentiation. While many studies advanced our understanding of how microtubule-associated proteins tune microtubule dynamics in trans, we have yet to understand how tubulin genetic diversity regulates microtubule functions. The majority of in vitro dynamics studies are performed with tubulin purified from brain tissue. This preparation is not representative of tubulin found in many cell types. Here we report the 4.2-Å cryo-electron microscopy (cryo-EM) structure and in vitro dynamics parameters of α1B/βI+βIVb microtubules assembled from tubulin purified from a human embryonic kidney cell line with isoform composition characteristic of fibroblasts and many immortalized cell lines. We find that these microtubules grow faster and transition to depolymerization less frequently compared with brain microtubules. Cryo-EM reveals that the dynamic ends of α1B/βI+βIVb microtubules are less tapered and that these tubulin heterodimers display lower curvatures. Interestingly, analysis of EB1 distributions at dynamic ends suggests no differences in GTP cap sizes. Last, we show that the addition of recombinant α1A/βIII tubulin, a neuronal isotype overexpressed in many tumors, proportionally tunes the dynamics of α1B/βI+βIVb microtubules. Our study is an important step toward understanding how tubulin isoform composition tunes microtubule dynamics.

Indexed as

Cryoelectron MicroscopyHEK293 CellsHumansMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein IsoformsProtein Structural ElementsTubulinMicrotubule-Associated ProteinsProtein IsoformsTubulin

Identifiers

PMID29021343
PMCPMC5706985
OpenAlexW2762278743

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.