Insights into the assembly and activation of the microtubule nucleator γ-TuRC

Here, we present the cryo-EM structure of γ-TuRC from Xenopus laevis at 4.8 Å global resolution, revealing a 14-spoked arrangement of GCPs and γ-tubulins in a partially flexible open left-handed spiral with a uniform sequence of GCP variants (Fig. 1a). Via specific interactions with other GCP prote...

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Hauptverfasser: Liu, Peng (VerfasserIn) , Župa, Erik (VerfasserIn) , Neuner, Annett (VerfasserIn) , Böhler, Anna (VerfasserIn) , Flemming, Dirk (VerfasserIn) , Ruppert, Thomas (VerfasserIn) , Pfeffer, Stefan (VerfasserIn) , Schiebel, Elmar (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2020
In: Nature
Year: 2019, Jahrgang: 578, Pages: 467-471
ISSN:1476-4687
DOI:10.1038/s41586-019-1896-6
Online-Zugang:Resolving-System, Volltext: https://doi.org/10.1038/s41586-019-1896-6
Verlag: https://www.nature.com/articles/s41586-019-1896-6
Volltext
Verfasserangaben:Peng Liu, Erik Zupa, Annett Neuner, Anna Böhler, Justus Loerke, Dirk Flemming, Thomas Ruppert, Till Rudack, Christoph Peter, Christian Spahn, Oliver J. Gruss, Stefan Pfeffer & Elmar Schiebel
Beschreibung
Zusammenfassung:Here, we present the cryo-EM structure of γ-TuRC from Xenopus laevis at 4.8 Å global resolution, revealing a 14-spoked arrangement of GCPs and γ-tubulins in a partially flexible open left-handed spiral with a uniform sequence of GCP variants (Fig. 1a). Via specific interactions with other GCP proteins, the GCP6-specific insertion domain scaffolds the assembly of the γ-TuRC. Unexpectedly, we identified Actin as a bona fide structural component of γ-TuRC with functional relevance in MT nucleation. The γ-TuRC spiral geometry is suboptimal for MT nucleation and a controlled conformational rearrangement of the γ-TuRC is required for its activation. Collectively, our cryo-EM reconstruction provides unprecedented insights into the molecular organization, the assembly and the activation mechanism of vertebrate γ-TuRC and will serve as an important framework for the mechanistic understanding of fundamental biological processes associated with MT nucleation, e.g. meiotic and mitotic spindle formation and centriole biogensis4.
Beschreibung:Published online: 19 December 2019
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Beschreibung:Online Resource
ISSN:1476-4687
DOI:10.1038/s41586-019-1896-6