ArticleThe Journal of biological chemistry2016
Functional Analysis of γ-Tubulin Complex Proteins Indicates Specific Lateral Association via Their N-terminal Domains.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Mutation of Tubgcp6 induces hematopoietic stem and progenitor cell exhaustion in zebrafish.Communications biology · 2026Article
- Altered development and network connectivity in a human neuronal model of 15q11.2 deletion-related neurodevelopmental disorders.Translational psychiatry · 2025Article
- Versatile gamma-tubulin complexes contribute to the dynamic organization of MTOCs during Drosophila spermatogenesis.Communications biology · 2024Article
- γ-tubulin complex controls the nucleation of tubulin-based structures in Apicomplexa.Molecular biology of the cell · 2024Article
- Comprehensive serum proteomics profiles and potential protein biomarkers for the early detection of advanced adenoma and colorectal cancer.World journal of gastrointestinal oncology · 2024Article
- CRB3 navigates Rab11 trafficking vesicles to promote γTuRC assembly during ciliogenesis.eLife · 2023Article
- Actin filaments form a size-dependent diffusion barrier around centrosomes.EMBO reports · 2023Article
- 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
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- Aurora A site specific TACC3 phosphorylation regulates astral microtubule assembly by stabilizing γ-tubulin ring complex.BMC molecular and cell biology · 2019Article
- Tubgcp3 Is Required for Retinal Progenitor Cell Proliferation During Zebrafish Development.Frontiers in molecular neuroscience · 2019Article
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
- Assembly and regulation of γ-tubulin complexes.Open biology · 2018Review
- Regulation of microtubule nucleation mediated by γ-tubulin complexes.Protoplasma · 2017Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are nucleated from multiprotein complexes containing γ-tubulin and associated γ-tubulin complex proteins (GCPs). Small complexes (γTuSCs) comprise two molecules of γ-tubulin bound to the C-terminal domains of GCP2 and GCP3. γTuSCs associate laterally into helical structures, providing a structural template for microtubule nucleation. In most eukaryotes γTuSCs associate with additional GCPs (4, 5, and 6) to form the core of the so-called γ-tubulin ring complex (γTuRC). GCPs 2-6 constitute a family of homologous proteins. Previous structural analysis and modeling of GCPs suggest that all family members can potentially integrate into the helical structure. Here we provide experimental evidence for this model. Using chimeric proteins in which the N- and C-terminal domains of different GCPs are swapped, we show that the N-terminal domains define the functional identity of GCPs, whereas the C-terminal domains are exchangeable. FLIM-FRET experiments indicate that GCP4 and GCP5 associate laterally within the complex, and their interaction is mediated by their N-terminal domains as previously shown for γTuSCs. Our results suggest that all GCPs are incorporated into the helix via lateral interactions between their N-terminal domains, whereas the C-terminal domains mediate longitudinal interactions with γ-tubulin. Moreover, we show that binding to γ-tubulin is not essential for integrating into the helical complex.
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