Evidence map›Paper›PMID 33544140›Full record

ArticleThe Journal of cell biology2021

GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation.

Rie Ayukawa, Seigo Iwata, Hiroshi Imai, Shinji Kamimura, Masahito Hayashi, Kien Xuan Ngo, Itsushi Minoura, Seiichi Uchimura, Tsukasa Makino, Mikako Shirouzu and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  6. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Bending-torsional elasticity and energetics of the plus-end microtubule tip.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 2 countries.

Rie Ayukawa *Laboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Seigo Iwata *Laboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Hiroshi Imai *Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo, Japan.
Shinji KamimuraDepartment of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo, Japan.
Masahito HayashiLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Kien Xuan NgoLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Itsushi MinouraLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Seiichi UchimuraLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Tsukasa MakinoLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
Mikako ShirouzuLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Hideki ShigematsuLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Ken SekimotoMatière et Systèmes Complexes (MSC), CNRS UMR 7057, Université de Paris, Paris, France.
Benoît GigantUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette, France.
Etsuko MutoLaboratory for Molecular Biophysics, RIKEN Center for Brain Science, Saitama, Japan.
RIKEN Center for Brain Science · JPCentre National de la Recherche Scientifique · FRChuo University · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

DROSOPHILA GENOMICS RESOURCE CENTERP40OD010949 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Andrew Zelhof · 2012 to 2026
$9.4M
NIH HHS P40 OD010949
6 · The paper itself

Abstract

Nucleation of microtubules (MTs) is essential for cellular activities, but its mechanism is unknown because of the difficulty involved in capturing rare stochastic events in the early stage of polymerization. Here, combining rapid flush negative stain electron microscopy (EM) and kinetic analysis, we demonstrate that the formation of straight oligomers of critical size is essential for nucleation. Both GDP and GTP tubulin form single-stranded oligomers with a broad range of curvatures, but upon nucleation, the curvature distribution of GTP oligomers is shifted to produce a minor population of straight oligomers. With tubulin having the Y222F mutation in the β subunit, the proportion of straight oligomers increases and nucleation accelerates. Our results support a model in which GTP binding generates a minor population of straight oligomers compatible with lateral association and further growth to MTs. This study suggests that cellular factors involved in nucleation promote it via stabilization of straight oligomers.

Indexed as

Protein MultimerizationAnimalsDrosophila melanogasterDrosophila ProteinsGuanosine DiphosphateGuanosine TriphosphateMicrotubulesTubulinDrosophila ProteinsGuanosine DiphosphateGuanosine TriphosphateTubulin

Identifiers

PMID33544140
PMCPMC7871348
OpenAlexW3127100265

What OpenQuestion holds

Textmetadata
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.