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- W3087315217 abstract "Abstract The formation of cellular microtubule networks is regulated by the γ -tubulin ring complex ( γ -TuRC). This ∼2.3 MDa assembly of >31 proteins includes γ -tubulin and GCP2-6, as well as MZT1 and an actin-like protein in a “lumenal bridge”. The challenge of reconstituting the γ -TuRC has limited dissections of its assembly and function. Here, we report a complete biochemical reconstitution of the human γ -TuRC ( γ -TuRC-GFP), a ∼35S complex that nucleates microtubules in vitro . We extend our approach to generate a stable subcomplex, γ -TuRC mini -GFP, which lacks MZT1 and actin. Using mutagenesis, we show that γ -TuRC mini -GFP nucleates microtubules in a guanine nucleotide-dependent manner and proceeds with similar kinetics as reported for native γ -TuRCs. Electron microscopy reveals that γ -TuRC-GFP resembles the native γ -TuRC architecture, while γ -TuRC mini -GFP adopts a partial cone shape presenting only 8-10 γ -tubulin subunits and lacks a well-ordered lumenal bridge. Our structure-function analysis suggests that the lumenal bridge facilitates the self-assembly of regulatory interfaces around a microtubule-nucleating “core” in the γ -TuRC." @default.
- W3087315217 created "2020-09-25" @default.
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- W3087315217 date "2020-09-21" @default.
- W3087315217 modified "2023-10-18" @default.
- W3087315217 title "Biochemical reconstitutions reveal principles of human γ-TuRC assembly and function" @default.
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- W3087315217 doi "https://doi.org/10.1101/2020.09.21.306845" @default.
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