ArticleMolecular biology of the cell1992
Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP.
Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers.
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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.
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182 citing papers in PubMed, 389 citations in OpenAlex.
- Microtubule posttranslational modifications provide unique recognition patterns for associated proteins.The EMBO journal · 2026Article
- Patronin promotes the formation of dynamic microtubule seeds in vivo.Journal of cell science · 2026Article
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- A cryo-EM processing pipeline for microtubules using CryoSPARC.Acta crystallographica. Section D, Structural biology · 2026Article
- Architects of the Developing Brain: Cytoskeleton-Organizing Molecules in Neurodevelopmental Disorders.Cells · 2026Review
- Adaptations in Plasmodium tubulin determine distinct microtubule architectures, mechanics and drug susceptibility.Nature communications · 2026Article
- The kinesin-4 protein KIF27 forms a cytoskeletal scaffold at the transition zone to promote motile cilia structural integrity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Paclitaxel neurotoxicity is triggered by epidermal EG5-dependent microtubule fasciculation and X-ROS formation.Research square · 2025Article
- Development of a Microfluidics-Based Approach for Investigating Microtubule Polymer Mechanics.Journal of visualized experiments : JoVE · 2025Article
- Distinct Network Morphologies from In Situ Polymerization of Microtubules in Giant Polymer-Lipid Hybrid Vesicles.Advanced biology · 2025Article
- Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap.Nature communications · 2025Article
- Role of the cytoskeleton in cellular reprogramming: effects of biophysical and biochemical factors.Frontiers in molecular biosciences · 2025Review
- Modulation of the cytoskeleton for cancer therapy.Frontiers in cell and developmental biology · 2025Article
- Modulation of microtubule dynamics by monovalent ions.PNAS nexus · 2025Article
- Phase separation of microtubule-binding proteins - implications for neuronal function and disease.Journal of cell science · 2024Review
- The GTP-tubulin cap is not the determinant of microtubule end stability in cells.Molecular biology of the cell · 2024Article
- Stable GDP-tubulin islands rescue dynamic microtubules.The Journal of cell biology · 2024Article
- Interface-acting nucleotide controls polymerization dynamics at microtubule plus- and minus-ends.eLife · 2024Article
- Measuring and modeling forces generated by microtubules.Biophysical reviews · 2023Review
- Decoding the hydrodynamic properties of microscale helical propellers from Brownian fluctuations.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
122 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
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Abstract
The role of GTP hydrolysis in microtubule dynamics has been reinvestigated using an analogue of GTP, guanylyl-(alpha, beta)-methylene-diphosphonate (GMPCPP). This analogue binds to the tubulin exchangeable nucleotide binding site (E-site) with an affinity four to eightfold lower than GTP and promotes the polymerization of normal microtubules. The polymerization rate of microtubules with GMPCPP-tubulin is very similar to that of GTP-tubulin. However, in contrast to microtubules polymerized with GTP, GMPCPP-microtubules do not depolymerize rapidly after isothermal dilution. The depolymerization rate of GMPCPP-microtubules is 0.1 s-1 compared with 500 s-1 for GDP-microtubules. GMPCPP also completely suppresses dynamic instability. Contrary to previous work, we find that the beta--gamma bond of GMPCPP is hydrolyzed extremely slowly after incorporation into the microtubule lattice, with a rate constant of 4 x 10(-7) s-1. Because GMPCPP hydrolysis is negligible over the course of a polymerization experiment, it can be used to test the role of hydrolysis in microtubule dynamics. Our results provide strong new evidence for the idea that GTP hydrolysis by tubulin is not required for normal polymerization but is essential for depolymerization and thus for dynamic instability. Because GMPCPP strongly promotes spontaneous nucleation of microtubules, we propose that GTP hydrolysis by tubulin also plays the important biological role of inhibiting spontaneous microtubule nucleation.
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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.