ArticleDevelopmental cell2020
Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure.
Article in Developmental cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
87 citing papers in PubMed, 136 citations in OpenAlex.
- Towards a systems-level view of the microtubule cytoskeleton and its functions in physiology and disease.Nature reviews. Molecular cell biology · 2026Review
- Noncentrosomal Microtubule Assembly and Its Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.Science advances · 2026Article
- Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.Nature communications · 2026Article
- Mutation of Tubgcp6 induces hematopoietic stem and progenitor cell exhaustion in zebrafish.Communications biology · 2026Article
- The γ-Tubulin Ring Complex promotes mitotic spindle integrity and acts as a microtubule minus-end cap during mitosis.bioRxiv : the preprint server for biology · 2026Article
- Human NLRP3 inflammasome activation leads to formation of condensate at the microtubule organizing center.Science advances · 2026Article
- Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.Nature communications · 2026Article
- Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Journal of molecular biology · 2026Article
- Orchestrating homolog segregation in meiosis I: molecular logic and regulatory networks with emphasis on male metaphase I.Cell communication and signaling : CCS · 2026Review
- 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
- Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding.Nature communications · 2025Article
- How augmin establishes the angle of the microtubule branch site.Nature communications · 2025Article
- Tubulin autoregulation factors SCAPER and TTC5 recruit γ-tubulin to non-centrosomal MTOCs for neuronal microtubule nucleation and axon regeneration.bioRxiv : the preprint server for biology · 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
27 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
The γ-tubulin ring complex (γTuRC) is the major microtubule nucleator in cells. The mechanism of its regulation is not understood. We purified human γTuRC and measured its nucleation properties in a total internal reflection fluorescence (TIRF) microscopy-based real-time nucleation assay. We find that γTuRC stably caps the minus ends of microtubules that it nucleates stochastically. Nucleation is inefficient compared with microtubule elongation. The 4 Å resolution cryoelectron microscopy (cryo-EM) structure of γTuRC, combined with crosslinking mass spectrometry analysis, reveals an asymmetric conformation with only part of the complex in a "closed" conformation matching the microtubule geometry. Actin in the core of the complex, and MZT2 at the outer perimeter of the closed part of γTuRC appear to stabilize the closed conformation. The opposite side of γTuRC is in an "open," nucleation-incompetent conformation, leading to a structural asymmetry explaining the low nucleation efficiency of purified human γTuRC. Our data suggest possible regulatory mechanisms for microtubule nucleation by γTuRC closure.
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Registered trials
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.