ArticleCell reports2020
MZT Proteins Form Multi-Faceted Structural Modules in the γ-Tubulin Ring Complex.
Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 61 citations in OpenAlex.
- Noncentrosomal Microtubule Assembly and Its Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Review
- 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
- Dissecting the Structural Organization, Recruitment and Activation Mechanisms of Centrosomal γ-TuRCs.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.bioRxiv : the preprint server for biology · 2025Article
- MZT2B promotes malignant phenotypes in NSCLC cells by enhancing mitochondrial function and COX5B expression.Cell death & disease · 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
- Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC.Nature communications · 2025Article
- Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.Nature communications · 2025Article
- Global Transcriptomic Analysis of Topical Sodium Alginate Protection against Peptic Damage in an In Vitro Model of Treatment-Resistant Gastroesophageal Reflux Disease.International journal of molecular sciences · 2024Article
- 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
- Structure of the native γ-tubulin ring complex capping spindle microtubules.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
- CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC.Nature cell biology · 2024Article
- The AP-2 complex interacts with γ-TuRC and regulates the proliferative capacity of neural progenitors.Life science alliance · 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
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Microtubule organization depends on the γ-tubulin ring complex (γ-TuRC), a ∼2.3-MDa nucleation factor comprising an asymmetric assembly of γ-tubulin and GCP2-GCP6. However, it is currently unclear how the γ-TuRC-associated microproteins MZT1 and MZT2 contribute to the structure and regulation of the holocomplex. Here, we report cryo-EM structures of MZT1 and MZT2 in the context of the native human γ-TuRC. MZT1 forms two subcomplexes with the N-terminal α-helical domains of GCP3 or GCP6 (GCP-NHDs) within the γ-TuRC "lumenal bridge." We determine the X-ray structure of recombinant MZT1/GCP6-NHD and find it is similar to that within the native γ-TuRC. We identify two additional MZT/GCP-NHD-like subcomplexes, one of which is located on the outer face of the γ-TuRC and comprises MZT2 and GCP2-NHD in complex with a centrosomin motif 1 (CM1)-containing peptide. Our data reveal how MZT1 and MZT2 establish multi-faceted, structurally mimetic "modules" that can expand structural and regulatory interfaces in the γ-TuRC.
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