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Microtubule nucleation by γ-tubulin complexes
Open accessAbstract
Microtubule nucleation is regulated by the γ-tubulin ring complex (γTuRC) and related γ-tubulin complexes, providing spatial and temporal control over the initiation of microtubule growth. Recent structural work has shed light on the mechanism of γTuRC-based microtubule nucleation, confirming the long-standing hypothesis that the γTuRC functions as a microtubule template. The first crystallographic analysis of a non-γ-tubulin γTuRC component (γ-tubulin complex protein 4 (GCP4)) has resulted in a new appreciation of the relationships among all γTuRC proteins, leading to a refined model of their organization and function. The structures have also suggested an unexpected mechanism for regulating γTuRC activity via conformational modulation of the complex component GCP3. New experiments on γTuRC localization extend these insights, suggesting a direct link between its attachment at specific cellular sites and its activation.
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Cites
Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions
Volkmann, N., Amann, K. J., Stoilova-McPhie, S., Egile, C., Winter, D. C., Hazelwood, L., Heuser, J. E., Li, R., Pollard, T. D., & Hanein, D. (2001) · Science · doi:10.1126/science.1063025 · Cited by 258
Evidence for a mixed lattice in microtubules reassembled in vitro
McEwen, B., & Edelstein, S. J. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90300-9 · Cited by 77
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Metadata
- Authors
- Kollman, J. M., Merdes, A., Mourey, L., & Agard, D. A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2011-10-12
- Volume
- 12
- Issue
- 11
- Pages
- 709-721
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2065581527
- Cited by
- 1,583
- References
- 2
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- green
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