ArticleScience advances2020
Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.
Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 58 citations in OpenAlex.
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.Science advances · 2026Article
- 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
- Dissecting the Structural Organization, Recruitment and Activation Mechanisms of Centrosomal γ-TuRCs.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Insights into Microtubule Nucleation at the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Lysine demethylase 4A: from chromatin to centrosomes.The FEBS journal · 2026Article
- 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
- Molecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography.Developmental cell · 2025Article
- Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC.Nature communications · 2025Article
- Cryo-EM structures of γ-TuRC reveal molecular insights into microtubule nucleation.Nature structural & molecular biology · 2024Article
- Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular 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
- CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC.Nature cell biology · 2024Article
- Multifaceted modes of γ-tubulin complex recruitment and microtubule nucleation at mitotic centrosomes.The Journal of cell biology · 2023Article
- Microtubule nucleation for spindle assembly: one molecule at a time.Trends in biochemical sciences · 2023Review
- A nucleotide binding-independent role for γ-tubulin in microtubule capping and cell division.The Journal of cell biology · 2023Article
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- MCRS1 modulates the heterogeneity of microtubule minus-end morphologies in mitotic spindles.Molecular biology of the cell · 2023Article
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6 authors at 2 institutions in 1 country.
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Abstract
The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has evaded in vitro reconstitution and thus detailed structure-function studies. Here, we show that a complex of RuvB-like protein 1 (RUVBL1) and RUVBL2 "RUVBL" controls assembly and composition of γTuRC in human cells. Likewise, RUVBL assembles γTuRC from a minimal set of core subunits in a heterologous coexpression system. RUVBL interacts with γTuRC subcomplexes but is not part of fully assembled γTuRC. Purified, reconstituted γTuRC has nucleation activity and resembles native γTuRC as revealed by its cryo-electron microscopy (cryo-EM) structure at ~4.0-Å resolution. We further use cryo-EM to identify features that determine the intricate, higher-order γTuRC architecture. Our work finds RUVBL as an assembly factor that regulates γTuRC in cells and allows production of recombinant γTuRC for future in-depth mechanistic studies.
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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.