ArticleThe Journal of cell biology2016
MOZART1 and γ-tubulin complex receptors are both required to turn γ-TuSC into an active microtubule nucleation template.
Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 55 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
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- Phosphorylation remodels the mitotic centrosome matrix to generate bipartite γ-tubulin complex docking sites.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors.Nature communications · 2025Article
- Expansion microscopy reveals characteristic ultrastructural features of pathogenic budding yeast species.Journal of cell science · 2024Article
- Structure of the native γ-tubulin ring complex capping spindle microtubules.Nature structural & molecular biology · 2024Article
- The centrosomal recruitment of γ-tubulin and its microtubule nucleation activity is α-fodrin guided.Cell cycle (Georgetown, Tex.) · 2023Article
- Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG.Nature communications · 2023Article
- A phylogenetically-restricted essential cell cycle progression factor in the human pathogen Candida albicans.Nature communications · 2022Article
- Modular assembly of the principal microtubule nucleator γ-TuRC.Nature communications · 2022Article
- Human centrosome organization and function in interphase and mitosis.Seminars in cell & developmental biology · 2021Review
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- Biochemical reconstitutions reveal principles of human γ-TuRC assembly and function.The Journal of cell biology · 2021Article
- Reconstitution of the recombinant human γ-tubulin ring complex.Open biology · 2021Article
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.Science advances · 2020Article
- The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.Nature communications · 2020Article
- MZT Proteins Form Multi-Faceted Structural Modules in the γ-Tubulin Ring Complex.Cell reports · 2020Article
- Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure.Developmental cell · 2020Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MOZART1/Mzt1 is required for the localization of γ-tubulin complexes to microtubule (MT)-organizing centers from yeast to human cells. Nevertheless, the molecular function of MOZART1/Mzt1 is largely unknown. Taking advantage of the minimal MT nucleation system of Candida albicans, we reconstituted the interactions of Mzt1, γ-tubulin small complex (γ-TuSC), and γ-tubulin complex receptors (γ-TuCRs) Spc72 and Spc110 in vitro. With affinity measurements, domain deletion, and swapping, we show that Spc110 and Mzt1 bind to distinct regions of the γ-TuSC. In contrast, both Mzt1 and γ-TuSC interact with the conserved CM1 motif of Spc110/Spc72. Spc110/Spc72 and Mzt1 constitute "oligomerization chaperones," cooperatively promoting and directing γ-TuSC oligomerization into MT nucleation-competent rings. Consistent with the functions of Mzt1, human MOZART1 directly interacts with the CM1-containing region of the γ-TuCR CEP215. MOZART1 depletion in human cells destabilizes the large γ-tubulin ring complex and abolishes CEP215
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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.