Evidence map›Paper›PMID 32413312›Full record

ArticleBiophysical journal2020

Microtubule Simulations Provide Insight into the Molecular Mechanism Underlying Dynamic Instability.

Dudu Tong, Gregory A Voth

Abstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  7. Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Unveiling the catalytic mechanism of GTP hydrolysis in microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Review
  10. Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  11. Article
  12. Article
  13. 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
  14. Structural transitions in the GTP cap visualized by cryo-electron microscopy of catalytically inactive microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. 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

2 authors.

Dudu TongDepartment of Chemistry, Chicago Center for Theoretical Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois.
Gregory A VothDepartment of Chemistry, Chicago Center for Theoretical Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois. Electronic address: gavoth@uchicago.edu.

Funding

New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
NIGMS NIH HHS R01 GM063796
6 · The paper itself

Abstract

The dynamic instability of microtubules (MTs), which refers to their ability to switch between polymerization and depolymerization states, is crucial for their function. It has been proposed that the growing MT ends are protected by a "GTP cap" that consists of GTP-bound tubulin dimers. When the speed of GTP hydrolysis is faster than dimer recruitment, the loss of this GTP cap will lead the MT to undergo rapid disassembly. However, the underlying atomistic mechanistic details of the dynamic instability remains unclear. In this study, we have performed long-time atomistic molecular dynamics simulations (1 μs for each system) for MT patches as well as a short segment of a closed MT in both GTP- and GDP-bound states. Our results confirmed that MTs in the GDP state generally have weaker lateral interactions between neighboring protofilaments (PFs) and less cooperative outward bending conformational change, where the difference between bending angles of neighboring PFs tends to be larger compared with GTP ones. As a result, when the GDP state tubulin dimer is exposed at the growing MT end, these factors will be more likely to cause the MT to undergo rapid disassembly. We also compared simulation results between the special MT seam region and the remaining material and found that the lateral interactions between MT PFs at the seam region were comparatively much weaker. This finding is consistent with the experimental suggestion that the seam region tends to separate during the disassembly process of an MT.

Indexed as

MicrotubulesTubulinGuanosine DiphosphateGuanosine TriphosphateMolecular Dynamics SimulationGuanosine DiphosphateGuanosine TriphosphateTubulin

Identifiers

PMID32413312
PMCPMC7300308

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.