ArticleJournal of computer-aided molecular design2012
The state of the guanosine nucleotide allosterically affects the interfaces of tubulin in protofilament.
Article in Journal of computer-aided molecular design, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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
6 citing papers in PubMed, 16 citations in OpenAlex.
- 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
- Microtubule Simulations Provide Insight into the Molecular Mechanism Underlying Dynamic Instability.Biophysical journal · 2020Article
- Multiscale Computational Modeling of Tubulin-Tubulin Lateral Interaction.Biophysical journal · 2019Article
- Microtubule assembly governed by tubulin allosteric gain in flexibility and lattice induced fit.eLife · 2018Article
- Detailed Per-residue Energetic Analysis Explains the Driving Force for Microtubule Disassembly.PLoS computational biology · 2015Article
- Brownian dynamics of subunit addition-loss kinetics and thermodynamics in linear polymer self-assembly.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynamics of microtubules is essential for many microtubule-dependent cellular functions such as the mitosis. It has been recognized for a long time that GTP hydrolysis in αβ-tubulin polymers plays a critical role in this dynamics. However, the effects of the changes in the nature of the guanosine nucleotide at the E-site in β-tubulin on microtubule structure and stability are still not well understood. In the present work, we performed all-atom molecular dynamics simulations of a αβα-tubulin heterotrimer harboring a guanosine nucleotide in three different states at the E-site: GTP, GDP-Pi and GDP. We found that changes in the nucleotide state is associated with significant conformational variations at the α-tubulin N- and β-tubulin M-loops which impact the interactions between tubulin protofilaments. The results also show that GTP hydrolysis reduces αβ-tubulin interdimer contacts in favor of intradimer interface. From an atomistic point view, we propose a role for α-tubulin glutamate residue 254 in catalytic magnesium coordination and identified a water molecule in the nucleotide binding pocket which is most probably required for nucleotide hydrolysis. Finally, the results are discussed with reference to the role of taxol in microtubule stability and the recent tubulin-sT2R crystal structures.
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Registered trials
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