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• W2111920698 abstract "γ-tubulin is an essential part of a multiprotein complex that nucleates the minus end of microtubules. Although the function of γ-tubulin in nucleating cytoplasmic and mitotic microtubules from organizing centers such as the centrosome and spindle pole body is well documented [1Jeng R. Stearns T. Gamma-tubulin complexes size does matter.Trends Cell Biol. 1999; 9: 339-342Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar, 2Schiebel E. γ-tubulin complexes binding to the centrosome, regulation and microtubule nucleation.Curr. Opin. Cell Biol. 2000; 12: 113-118Crossref PubMed Scopus (137) Google Scholar, 3Wiese C. Zheng Y. γ-tubulin complexes and their interaction with microtubule-organising centers.Curr. Opin. Struct. Biol. 1999; 9: 250-259Crossref PubMed Scopus (96) Google Scholar], its role in microtubule nucleation in the eukaryotic flagellum is unclear. Here, we have used Trypanosoma brucei to investigate possible functions of γ-tubulin in the formation of the 9 + 2 flagellum axoneme. T. brucei possesses a single flagellum and forms a new flagellum during each cell cycle. We have used an inducible RNA interference (RNAi) approach to ablate expression of γ-tubulin, and, after induction, we observe that the new flagellum is still formed but is paralyzed, while the old flagellum is unaffected. Electron microscopy reveals that the paralyzed flagellum lacks central pair microtubules but that the outer doublet microtubules are formed correctly. These differences in microtubule nucleation mechanisms during flagellum growth provide insights into spatial and temporal regulation of γ-tubulin-dependent processes within cells and explanations for the organization and evolution of axonemal structures such as the 9 + 0 axonemes of sensory cells and primary cilia." @default.
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• W2111920698 date "2003-04-01" @default.
• W2111920698 modified "2023-10-18" @default.
• W2111920698 title "γ-Tubulin Functions in the Nucleation of a Discrete Subset of Microtubules in the Eukaryotic Flagellum" @default.
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• W2111920698 doi "https://doi.org/10.1016/s0960-9822(03)00174-x" @default.
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