ArticleeLife2015
A mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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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.
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.
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Who cites it
67 citing papers in PubMed, 103 citations in OpenAlex.
- Gain-of-function suppressors restore microtubule dynamics and rescue dominant-negative tubulinopathies.Nature cell biology · 2026Article
- Article
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- An evolution-conserved allosteric network in human tubulin governs paclitaxel efficacy.Nature chemical biology · 2026Article
- Single-molecule microtubule dynamics measurements reveal an intermediate state and clarify the role of nucleotide.Nature communications · 2025Article
- Stu2 performs an essential kinetochore function independent of its microtubule polymerase activity.The Journal of cell biology · 2025Article
- A tubulin-MAPKKK pathway engages tubulin isotype interaction for neuroprotection.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025Article
- Article
- Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- β3 accelerates microtubule plus end maturation through a divergent lateral interface.Molecular biology of the cell · 2025Article
- Evolutionary adaptation to hyperstable microtubules selectively targets tubulins and is empowered by the spindle assembly checkpoint.Cell reports · 2025Article
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- The GTP-tubulin cap is not the determinant of microtubule end stability in cells.Molecular biology of the cell · 2024Article
- β3 accelerates microtubule plus end maturation through a divergent lateral interface.bioRxiv : the preprint server for biology · 2024Article
- Poxvirus A51R proteins regulate microtubule stability and antagonize a cell-intrinsic antiviral response.Cell reports · 2024Article
- Taxol acts differently on different tubulin isotypes.Communications biology · 2023Article
- CLASPs stabilize the pre-catastrophe intermediate state between microtubule growth and shrinkage.The Journal of cell biology · 2023Article
- Investigation of enzalutamide, docetaxel, and cabazitaxel resistance in the castration resistant prostate cancer cell line C4 using genome-wide CRISPR/Cas9 screening.Scientific reports · 2023Article
- Multivalency ensures persistence of a +TIP body at specialized microtubule ends.Nature cell biology · 2023Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Microtubule dynamic instability depends on the GTPase activity of the polymerizing αβ-tubulin subunits, which cycle through at least three distinct conformations as they move into and out of microtubules. How this conformational cycle contributes to microtubule growing, shrinking, and switching remains unknown. Here, we report that a buried mutation in αβ-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized αβ-tubulin. Thus, the mutation weakens the coupling between the conformational and GTPase cycles of αβ-tubulin. By showing that the mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules, our data reveal that the strength of the allosteric response to GDP in the lattice dictates the frequency of catastrophe and the severity of rapid shrinking.
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What OpenQuestion holds
Registered trials
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.