ArticleThe EMBO journal2024
γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.Nature communications · 2026Article
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- Integrated Protocol for γTuRC Expression and Purification for Microtubule Nucleation and Cryo-EM Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Dissecting the Structural Organization, Recruitment and Activation Mechanisms of Centrosomal γ-TuRCs.Cytoskeleton (Hoboken, N.J.) · 2026Article
- SPC24 boosts tumor progression and correlates with immune infiltrates in pancreatic adenocarcinoma.Frontiers in oncology · 2026Article
- Insights into Microtubule Nucleation at the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching.Nature communications · 2025Article
- Structure of the microtubule-anchoring factor NEDD1 bound to the γ-tubulin ring complex.The Journal of cell biology · 2025Article
- Conformational Regulation of Vertebrate γ-Tubulin Ring Complexes by CM1 Proteins.Cytoskeleton (Hoboken, N.J.) · 2025Article
- NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends.The Journal of cell biology · 2025Article
- Molecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography.Developmental cell · 2025Article
- Cryo-EM structures of γ-TuRC reveal molecular insights into microtubule nucleation.Nature structural & molecular biology · 2024Article
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Authors and funding
11 authors.
Funding
Abstract
The γ-tubulin ring complex (γ-TuRC) is a structural template for de novo microtubule assembly from α/β-tubulin units. The isolated vertebrate γ-TuRC assumes an asymmetric, open structure deviating from microtubule geometry, suggesting that γ-TuRC closure may underlie regulation of microtubule nucleation. Here, we isolate native γ-TuRC-capped microtubules from Xenopus laevis egg extract nucleated through the RanGTP-induced pathway for spindle assembly and determine their cryo-EM structure. Intriguingly, the microtubule minus end-bound γ-TuRC is only partially closed and consequently, the emanating microtubule is locally misaligned with the γ-TuRC and asymmetric. In the partially closed conformation of the γ-TuRC, the actin-containing lumenal bridge is locally destabilised, suggesting lumenal bridge modulation in microtubule nucleation. The microtubule-binding protein CAMSAP2 specifically binds the minus end of γ-TuRC-capped microtubules, indicating that the asymmetric minus end structure may underlie recruitment of microtubule-modulating factors for γ-TuRC release. Collectively, we reveal a surprisingly asymmetric microtubule minus end protofilament organisation diverging from the regular microtubule structure, with direct implications for the kinetics and regulation of nucleation and subsequent modulation of microtubules during spindle assembly.
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