Evidence map›Paper›PMID 27146111›Full record

ArticleMolecular biology of the cell2016

GDP-to-GTP exchange on the microtubule end can contribute to the frequency of catastrophe.

Felipe-Andrés Piedra, Tae Kim, Emily S Garza, Elisabeth A Geyer, Alexander Burns, Xuecheng Ye, Luke M Rice

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. 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. Article
  10. Article
  11. Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases.International journal of molecular sciences · 2020
    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

7 authors at 1 institution in 1 country.

Felipe-Andrés PiedraDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Tae KimDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Emily S GarzaDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Elisabeth A GeyerDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Alexander BurnsDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Xuecheng YeDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390.
Luke M RiceDepartments of Biophysics and Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390 Luke.Rice@UTSouthwestern.edu.
Southwestern Medical Center · US

Funding

Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

Microtubules are dynamic polymers of αβ-tubulin that have essential roles in chromosome segregation and organization of the cytoplasm. Catastrophe-the switch from growing to shrinking-occurs when a microtubule loses its stabilizing GTP cap. Recent evidence indicates that the nucleotide on the microtubule end controls how tightly an incoming subunit will be bound (trans-acting GTP), but most current models do not incorporate this information. We implemented trans-acting GTP into a computational model for microtubule dynamics. In simulations, growing microtubules often exposed terminal GDP-bound subunits without undergoing catastrophe. Transient GDP exposure on the growing plus end slowed elongation by reducing the number of favorable binding sites on the microtubule end. Slower elongation led to erosion of the GTP cap and an increase in the frequency of catastrophe. Allowing GDP-to-GTP exchange on terminal subunits in simulations mitigated these effects. Using mutant αβ-tubulin or modified GTP, we showed experimentally that a more readily exchangeable nucleotide led to less frequent catastrophe. Current models for microtubule dynamics do not account for GDP-to-GTP exchange on the growing microtubule end, so our findings provide a new way of thinking about the molecular events that initiate catastrophe.

Indexed as

Cell SizeComputer SimulationGuanosine DiphosphateGuanosine TriphosphateMicrotubulesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTubulinGuanosine DiphosphateGuanosine TriphosphateSaccharomyces cerevisiae ProteinsTubulin

Identifiers

PMID27146111
PMCPMC5221584
OpenAlexW2345508708

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.