Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors
The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuS...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
5. Januar 2025
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| In: |
Nature Communications
Year: 2025, Volume: 16, Pages: 1-19 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-024-55778-7 |
| Online Access: | Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-024-55778-7 Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-024-55778-7 |
| Author Notes: | Anjun Zheng, Bram J. A. Vermeulen, Martin Würtz, Annett Neuner, Nicole Lübbehusen, Matthias P. Mayer, Elmar Schiebel & Stefan Pfeffer |
| Summary: | The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 Å resolution, revealing how the γ-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal α-helix of Stu2 and thereby position the α/β-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in γ-TuSC oligomerisation and the recruitment of microtubule polymerases to the γ-TuRC. |
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| Item Description: | Gesehen am 04.04.2025 |
| Physical Description: | Online Resource |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-024-55778-7 |