ArticleThe Journal of biological chemistry2010
GDP-tubulin incorporation into growing microtubules modulates polymer stability.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation.The Journal of cell biology · 2021Article
- Microtubule Plus End Dynamics - Do We Know How Microtubules Grow?: Cells boost microtubule growth by promoting distinct structural transitions at growing microtubule ends.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Microtubule aging probed by microfluidics-assisted tubulin washout.Molecular biology of the cell · 2016Article
- A stable microtubule array drives fission yeast polarity reestablishment upon quiescence exit.The Journal of cell biology · 2015Article
- Random hydrolysis controls the dynamic instability of microtubules.Biophysical journal · 2012Article
- Article
- New insights into microtubule elongation mechanisms.Communicative & integrative biology · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubule growth proceeds through the endwise addition of nucleotide-bound tubulin dimers. The microtubule wall is composed of GDP-tubulin subunits, which are thought to come exclusively from the incorporation of GTP-tubulin complexes at microtubule ends followed by GTP hydrolysis within the polymer. The possibility of a direct GDP-tubulin incorporation into growing polymers is regarded as hardly compatible with recent structural data. Here, we have examined GTP-tubulin and GDP-tubulin incorporation into polymerizing microtubules using a minimal assembly system comprised of nucleotide-bound tubulin dimers, in the absence of free nucleotide. We find that GDP-tubulin complexes can efficiently co-polymerize with GTP-tubulin complexes during microtubule assembly. GDP-tubulin incorporation into microtubules occurs with similar efficiency during bulk microtubule assembly as during microtubule growth from seeds or centrosomes. Microtubules formed from GTP-tubulin/GDP-tubulin mixtures display altered microtubule dynamics, in particular a decreased shrinkage rate, apparently due to intrinsic modifications of the polymer disassembly properties. Thus, although microtubules polymerized from GTP-tubulin/GDP-tubulin mixtures or from homogeneous GTP-tubulin solutions are both composed of GDP-tubulin subunits, they have different dynamic properties, and this may reveal a novel form of microtubule "structural plasticity."
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