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Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC

The γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole lumen. In the pericentriolar material, the γ-TuRC is involved in microtubule organization, while the funct...

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Hauptverfasser: Gao, Qi (VerfasserIn) , Hofer, Florian W. (VerfasserIn) , Filbeck, Sebastian (VerfasserIn) , Vermeulen, Bram J. A. (VerfasserIn) , Würtz, Martin (VerfasserIn) , Neuner, Annett (VerfasserIn) , Kaplan, Charlotte (VerfasserIn) , Zezlina, Maja (VerfasserIn) , Sala, Cornelia (VerfasserIn) , Shin, Hyesu (VerfasserIn) , Gruss, Oliver J. (VerfasserIn) , Schiebel, Elmar (VerfasserIn) , Pfeffer, Stefan (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 12 March 2025
In: Nature Communications
Year: 2025, Jahrgang: 16, Pages: 1-23
ISSN:2041-1723
DOI:10.1038/s41467-025-57729-2
Online-Zugang:Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-025-57729-2
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-025-57729-2
Volltext
Verfasserangaben:Qi Gao, Florian W. Hofer, Sebastian Filbeck, Bram J. A. Vermeulen, Martin Würtz, Annett Neuner, Charlotte Kaplan, Maja Zezlina, Cornelia Sala, Hyesu Shin, Oliver J. Gruss, Elmar Schiebel & Stefan Pfeffer
Beschreibung
Zusammenfassung:The γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole lumen. In the pericentriolar material, the γ-TuRC is involved in microtubule organization, while the function of the centriole lumenal pool remains unclear. The conformational landscape of the γ-TuRC, which is crucial for its activity, and its centrosomal anchoring mechanisms, which determine γ-TuRC activity and turnover, are not understood. Using cryo-electron tomography, we analyze γ-TuRCs in human cells and purified centrosomes. Pericentriolar γ-TuRCs simultaneously associate with the essential adapter NEDD1 and the microcephaly protein CDK5RAP2. NEDD1 forms a tetrameric structure at the γ-TuRC base through interactions with four GCP3/MZT1 modules and GCP5/6-specific extensions, while multiple copies of CDK5RAP2 engage the γ-TuRC in two distinct binding patterns to promote γ-TuRC closure and activation. In the centriole lumen, the microtubule branching factor Augmin tethers a condensed cluster of γ-TuRCs to the centriole wall with defined directional orientation. Centriole-lumenal γ-TuRC-Augmin is protected from degradation during interphase and released in mitosis to aid chromosome alignment. This study provides a unique view on γ-TuRC structure and molecular organization at centrosomes and identifies an important cellular function of centriole-lumenal γ-TuRCs.
Beschreibung:Gesehen am 12.08.2025
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-025-57729-2

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