Evidence map›Paper›PMID 37749104›Full record

ArticleNature communications2023

Structural insights into the mechanism of GTP initiation of microtubule assembly.

Ju Zhou, Anhui Wang, Yinlong Song, Nan Liu, Jia Wang, Yan Li, Xin Liang, Guohui Li, Huiying Chu, Hong-Wei Wang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  4. Review
  5. Article
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  8. Article
  9. Article
  10. Article
  11. Article
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  13. Form and function in biological filaments: a physicist's review.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  14. Review
  15. Article
  16. 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
  17. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    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

10 authors at 4 institutions in 3 countries.

Ju Zhou *State Key Laboratory of Membrane Biology, Tsinghua University, Beijing, 100084, China.
Anhui Wang *Laboratory of Molecular Modeling and Design, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Science, 457 Zhongshan Road, Dalian, 116023, China.
Yinlong SongTsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Nan LiuState Key Laboratory of Membrane Biology, Tsinghua University, Beijing, 100084, China.
Jia WangState Key Laboratory of Membrane Biology, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0002-5978-4191
Yan LiLaboratory of Molecular Modeling and Design, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Science, 457 Zhongshan Road, Dalian, 116023, China.
Xin LiangTsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0001-7915-8094
Guohui LiLaboratory of Molecular Modeling and Design, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Science, 457 Zhongshan Road, Dalian, 116023, China.ORCID http://orcid.org/0000-0001-8223-705X
Huiying ChuLaboratory of Molecular Modeling and Design, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Science, 457 Zhongshan Road, Dalian, 116023, China. chuhy2009@dicp.ac.cn.ORCID http://orcid.org/0000-0002-0018-6189
Hong-Wei WangState Key Laboratory of Membrane Biology, Tsinghua University, Beijing, 100084, China. hongweiwang@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-9494-8780
Center for Life Sciences · CNDalian Institute of Chemical Physics · CNKing Center · USUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the dynamic assembly of microtubules (MT) plays an important role in numerous cellular processes. The underlying mechanism of GTP triggering MT assembly is still unknown. Here, we present cryo-EM structures of tubulin heterodimer at their GTP- and GDP-bound states, intermediate assembly states of GTP-tubulin, and final assembly stages of MT. Both GTP- and GDP-tubulin heterodimers adopt similar curved conformations with subtle flexibility differences. In head-to-tail oligomers of tubulin heterodimers, the inter-dimer interface of GDP-tubulin exhibits greater flexibility, particularly in tangential bending. Cryo-EM of the intermediate assembly states reveals two types of tubulin lateral contacts, "Tube-bond" and "MT-bond". Further, molecular dynamics (MD) simulations show that GTP triggers lateral contact formation in MT assembly in multiple sequential steps, gradually straightening the curved tubulin heterodimers. Therefore, we propose a flexible model of GTP-initiated MT assembly, including the formation of longitudinal and lateral contacts, to explain the nucleation and assembly of MT.

Indexed as

CognitionTubulinGuanosine TriphosphateMicrotubulesGuanosine TriphosphateTubulin

Identifiers

PMID37749104
PMCPMC10519996
OpenAlexW4387012361

What OpenQuestion holds

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LicenceCC BY
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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.