ArticleNature structural & molecular biology2011
Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 85 citations in OpenAlex.
- 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
- Network-based analysis predicts interacting genetic modifiers from a meta-mapping study of spike-wave discharge in mice.Genes, brain, and behavior · 2024Article
- The AP-2 complex interacts with γ-TuRC and regulates the proliferative capacity of neural progenitors.Life science alliance · 2024Article
- Analysis of Predicted Amino Acid Sequences of Diatom Microtubule Center Components.International journal of molecular sciences · 2023Article
- A germline-specific role for unconventional components of the γ-tubulin complex in Caenorhabditis elegans.Journal of cell science · 2023Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Bi-Allelic c.1746G>T; p.Leu582= Variants inMolecular syndromology · 2022Article
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.eLife · 2021Article
- Article
- Reconstitution of the recombinant human γ-tubulin ring complex.Open biology · 2021Article
- Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.Science advances · 2020Article
- Review
- Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure.Developmental cell · 2020Article
- Article
- Article
- Bi-allelic Pathogenic Variants in TUBGCP2 Cause Microcephaly and Lissencephaly Spectrum Disorders.American journal of human genetics · 2019Article
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
- Potential mechanism and drug candidates for sepsis-induced acute lung injury.Experimental and therapeutic medicine · 2018Article
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
Abstract
Microtubule nucleation in all eukaryotes involves γ-tubulin small complexes (γTuSCs) that comprise two molecules of γ-tubulin bound to γ-tubulin complex proteins (GCPs) GCP2 and GCP3. In many eukaryotes, multiple γTuSCs associate with GCP4, GCP5 and GCP6 into large γ-tubulin ring complexes (γTuRCs). Recent cryo-EM studies indicate that a scaffold similar to γTuRCs is formed by lateral association of γTuSCs, with the C-terminal regions of GCP2 and GCP3 binding γ-tubulin molecules. However, the exact role of GCPs in microtubule nucleation remains unknown. Here we report the crystal structure of human GCP4 and show that its C-terminal domain binds directly to γ-tubulin. The human GCP4 structure is the prototype for all GCPs, as it can be precisely positioned within the γTuSC envelope, revealing the nature of protein-protein interactions and conformational changes regulating nucleation activity.
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