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- W4313457146 abstract "Abstract Cilia are essential organelles that protrude from the cell body. Cilia are made of a microtubule-based structure called the axoneme. In most types of cilia, the ciliary tip is distinct from the rest of the cilium. Here, we used cryo-electron tomography and subtomogram averaging to obtain the structure of the ciliary tip of the ciliate Tetrahymena thermophila . We show the microtubules in the tip are highly cross-linked with each other and stabilised by luminal proteins, plugs and cap proteins at the plus ends. In the tip region, the central pair lacks the typical projections and twists significantly. By analysing cells lacking a ciliary tip-enriched protein CEP104/FAP256 by cryo-electron tomography and proteomics, we discovered candidates for the central pair cap complex and explain potential functions of CEP104/FAP256 . These data provide new insights into the function of the ciliary tip and inform about the mechanisms of ciliary assembly and length regulation." @default.
- W4313457146 created "2023-01-06" @default.
- W4313457146 creator A5021750729 @default.
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- W4313457146 date "2023-01-03" @default.
- W4313457146 modified "2023-10-17" @default.
- W4313457146 title "Molecular architecture of the ciliary tip revealed by cryo-electron tomography" @default.
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- W4313457146 doi "https://doi.org/10.1101/2023.01.03.522627" @default.
- W4313457146 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36711791" @default.
- W4313457146 hasPublicationYear "2023" @default.
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