The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP.
Open accessAbstract
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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Cites
Dynamic instability of microtubule growth
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Self-citation[39] Preparation of modified tubulins
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Self-citationMicrotubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study.
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γ-Tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
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Self-citationTubulin-nucleotide interactions during the polymerization and depolymerization of microtubules
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Cited by
Kin I kinesins are microtubule-destabilizing enzymes
Desai, A., Verma, S., Mitchison, T. J., & Walczak, C. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80960-5 · Cited by 708
Self-citationAlushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D., & Nogales, E. (2014) · Cell · doi:10.1016/j.cell.2014.03.053 · Cited by 696
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner
Varga, V., Helenius, J., Tanaka, K., Hyman, A. A., Tanaka, T. U., & Howard, J. (2006) · Nature Cell Biology · doi:10.1038/ncb1462 · Cited by 445
Self-citationMechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins
Zhang, R., Alushin, G. M., Brown, A., & Nogales, E. (2015) · Cell · doi:10.1016/j.cell.2015.07.012 · Cited by 457
Metadata
- Authors
- Hyman, A. A., Salser, S., Drechsel, D. N., Unwin, N., & Mitchison, T. J.
- Venue
- Molecular Biology of the Cell
- Published
- 1992-10
- Volume
- 3
- Issue
- 10
- Pages
- 1155-1167
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W1970611771
- Cited by
- 398
- References
- 32
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Hyman, A. A., Salser, S., Drechsel, D. N., Unwin, N., & Mitchison, T. J. (1992). Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.3.10.1155
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