
doi: 10.1038/ncb3329
pmid: 26999736
Centrioles are critical for the formation of centrosomes, cilia and flagella in eukaryotes. They are thought to assemble around a nine-fold symmetric cartwheel structure established by SAS-6 proteins. Here, we have engineered Chlamydomonas reinhardtii SAS-6-based oligomers with symmetries ranging from five- to ten-fold. Expression of a SAS-6 mutant that forms six-fold symmetric cartwheel structures in vitro resulted in cartwheels and centrioles with eight- or nine-fold symmetries in vivo. In combination with Bld10 mutants that weaken cartwheel-microtubule interactions, this SAS-6 mutant produced six- to eight-fold symmetric cartwheels. Concurrently, the microtubule wall maintained eight- and nine-fold symmetries. Expressing SAS-6 with analogous mutations in human cells resulted in nine-fold symmetric centrioles that exhibited impaired length and organization. Together, our data suggest that the self-assembly properties of SAS-6 instruct cartwheel symmetry, and lead us to propose a model in which the cartwheel and the microtubule wall assemble in an interdependent manner to establish the native architecture of centrioles.
Models, Molecular, Algal Proteins, Blotting, Western, Green Fluorescent Proteins, Molecular Conformation, Cell Cycle Proteins, Crystallography, X-Ray, Microscopy, Atomic Force, Microtubules, Protein Structure, Tertiary, Microscopy, Electron, Microscopy, Fluorescence, Cell Line, Tumor, Mutation, Humans, RNA Interference, Protein Multimerization, Chlamydomonas reinhardtii, Centrioles
Models, Molecular, Algal Proteins, Blotting, Western, Green Fluorescent Proteins, Molecular Conformation, Cell Cycle Proteins, Crystallography, X-Ray, Microscopy, Atomic Force, Microtubules, Protein Structure, Tertiary, Microscopy, Electron, Microscopy, Fluorescence, Cell Line, Tumor, Mutation, Humans, RNA Interference, Protein Multimerization, Chlamydomonas reinhardtii, Centrioles
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