ArticleMolecular biology of the cell2001
GCP5 and GCP6: two new members of the human gamma-tubulin complex.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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97 citing papers in PubMed, 188 citations in OpenAlex.
- 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
- Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.Nature communications · 2026Article
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- MLL/WDR5 complex recruits centriolar satellite protein Cep72 to regulate microtubule nucleation and spindle formation.Science advances · 2024Article
- Genetic Primary Microcephalies: When Centrosome Dysfunction Dictates Brain and Body Size.Cells · 2023Review
- A germline-specific role for unconventional components of the γ-tubulin complex in Caenorhabditis elegans.Journal of cell science · 2023Article
- Deciphering the RNA-binding protein interaction with the mRNAs encoded from human chromosome 15q11.2 BP1-BP2 microdeletion region.Functional & integrative genomics · 2023Article
- A nucleotide binding-independent role for γ-tubulin in microtubule capping and cell division.The Journal of cell biology · 2023Article
- No signs of neurodegenerative effects in 15q11.2 BP1-BP2 copy number variant carriers in the UK Biobank.Translational psychiatry · 2023Article
- The centrosomal recruitment of γ-tubulin and its microtubule nucleation activity is α-fodrin guided.Cell cycle (Georgetown, Tex.) · 2023Article
- Mitochondrial DNA methylation is a predictor of immunotherapy response and prognosis in breast cancer: scRNA-seq and bulk-seq data insights.Frontiers in immunology · 2023Article
- Novel plasma protein biomarkers from critically ill sepsis patients.Clinical proteomics · 2022Article
- The centriolar satellite protein Cfap53 facilitates formation of the zygotic microtubule organizing center in the zebrafish embryo.Development (Cambridge, England) · 2022Article
- Modular assembly of the principal microtubule nucleator γ-TuRC.Nature communications · 2022Article
- Molecular Evolution of Tubulins in Diatoms.International journal of molecular sciences · 2022Article
- Mining massive genomic data of two Swiss Braunvieh cattle populations reveals six novel candidate variants that impair reproductive success.Genetics, selection, evolution : GSE · 2021Article
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- Micron-scale geometrical features of microtubules as regulators of microtubule organization.eLife · 2021Review
- The Polygenic Nature and Complex Genetic Architecture of Specific Learning Disorder.Brain sciences · 2021Review
- CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.eLife · 2021Article
37 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The gamma-tubulin complex is a large multiprotein complex that is required for microtubule nucleation at the centrosome. Here we report the purification and characterization of the human gamma-tubulin complex and the identification of its subunits. The human gamma-tubulin complex is a ring of ~25 nm, has a subunit structure similar to that reported for gamma-tubulin complexes from other species, and is able to nucleate microtubule polymerization in vitro. Mass spectrometry analysis of the human gamma-tubulin complex components confirmed the presence of four previously identified components (gamma-tubulin and gamma-tubulin complex proteins [GCPs] 2, 3, and 4) and led to the identification of two new components, GCP5 and GCP6. Sequence analysis revealed that the GCPs share five regions of sequence similarity and define a novel protein superfamily that is conserved in metazoans. GCP5 and GCP6, like other components of the gamma-tubulin complex, localize to the centrosome and associate with microtubules, suggesting that the entire gamma-tubulin complex takes part in both of these interactions. Stoichiometry experiments revealed that there is a single copy of GCP5 and multiple copies of gamma-tubulin, GCP2, GCP3, and GCP4 within the gamma-tubulin complex. Thus, the gamma-tubulin complex is conserved in structure and function, suggesting that the mechanism of microtubule nucleation is conserved.
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