The structure of the γ-TuRC: a 25-years-old molecular puzzle
The nucleation of microtubules from αβ-tubulin dimers is an essential cellular process dependent on γ-tubulin complexes. Mechanistic understanding of the nucleation reaction was hampered by the lack of γ-tubulin complex structures at sufficiently high resolution. The recent technical developments in...
Gespeichert in:
| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2021
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| In: |
Current opinion in structural biology
Year: 2021, Jahrgang: 66, Pages: 15-21 |
| DOI: | 10.1016/j.sbi.2020.08.008 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.sbi.2020.08.008 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0959440X20301433 
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| Verfasserangaben: | Erik Zupa, Peng Liu, Martin Würtz, Elmar Schiebel and Stefan Pfeffer |
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| 520 | |a The nucleation of microtubules from αβ-tubulin dimers is an essential cellular process dependent on γ-tubulin complexes. Mechanistic understanding of the nucleation reaction was hampered by the lack of γ-tubulin complex structures at sufficiently high resolution. The recent technical developments in cryo-electron microscopy have allowed resolving the vertebrate γ-tubulin ring complex (γ-TuRC) structure at near-atomic resolution. These studies clarified the arrangement and stoichiometry of gamma-tubulin complex proteins in the γ-TuRC, characterized the surprisingly versatile integration of the small proteins MZT1/2 into the complex, and identified actin as an integral component of the γ-TuRC. In this review, we summarize the structural insights into the molecular architecture, the assembly pathway, and the regulation of the microtubule nucleation reaction. | ||
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