ArticleNature communications2020
The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Insights into Microtubule Nucleation at the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.Nature communications · 2025Article
- Structure of the native γ-tubulin ring complex capping spindle microtubules.Nature structural & molecular biology · 2024Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Bending-torsional elasticity and energetics of the plus-end microtubule tip.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Modular assembly of the principal microtubule nucleator γ-TuRC.Nature communications · 2022Article
- Reconstitution of the recombinant human γ-tubulin ring complex.Open biology · 2021Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
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Abstract
The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is achieved and regulated by a minimal microtubule nucleation system, we here determined the cryo-electron microscopy structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. Compared to the vertebrate γ-tubulin ring complex (γ-TuRC), we observed a vastly remodeled interface between the SPC/GCP-γ-tubulin spokes, which stabilizes the complex and defines the γ-tubulin arrangement. The relative positioning of γ-tubulin subunits indicates that a conformational rearrangement of the complex is required for microtubule nucleation activity, which follows opposing directionality as predicted for the vertebrate γ-TuRC. Collectively, our data suggest that the assembly and regulation mechanisms of γ-tubulin complexes fundamentally differ between the microtubule nucleation systems in lower and higher eukaryotes.
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