ArticleNature structural & molecular biology2015
Ring closure activates yeast γTuRC for species-specific microtubule nucleation.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Towards a systems-level view of the microtubule cytoskeleton and its functions in physiology and disease.Nature reviews. Molecular cell biology · 2026Review
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.Nature communications · 2026Article
- Insights into Microtubule Nucleation at the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Conformational Regulation of Vertebrate γ-Tubulin Ring Complexes by CM1 Proteins.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Molecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography.Developmental cell · 2025Article
- 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
- Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular biology · 2024Article
- Mechanism of how the universal module XMAP215 γ-TuRC nucleates microtubules.bioRxiv : the preprint server for biology · 2024Article
- γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end.The EMBO journal · 2024Article
- Native molecular architectures of centrosomes inbioRxiv : the preprint server for biology · 2024Article
- Microtubule nucleation for spindle assembly: one molecule at a time.Trends in biochemical sciences · 2023Review
- Mechanisms underlying spindle assembly and robustness.Nature reviews. Molecular cell biology · 2023Review
- A germline-specific role for unconventional components of the γ-tubulin complex in Caenorhabditis elegans.Journal of cell science · 2023Article
- MCRS1 modulates the heterogeneity of microtubule minus-end morphologies in mitotic spindles.Molecular biology of the cell · 2023Article
- Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- Microtubule Anchoring: Attaching Dynamic Polymers to Cellular Structures.Frontiers in cell and developmental biology · 2022Review
- γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022Review
13 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
Abstract
The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm the functional importance of the closed γTuSC ring, we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, thus suggesting that this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a strong preference for tubulin from the same species.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.