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 that the microtubules at the tip are highly crosslinked with each other and stabilized by luminal proteins, plugs, and cap proteins at the plus ends. In the tip region, the central pair lacks typical projections and twists significantly. By analyzing 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 explained the potential functions of CEP104/FAP256. These data provide new insights into the function of the ciliary tip and the mechanisms of ciliary assembly and length regulation.
CEP104/FAP256 and associated cap complex maintain stability of the ciliary tip
Disclosures: The authors declare no competing interests exist.
- Award Id(s): PJT-156354
- Award Id(s): RGPIN-2022-04774
- Award Id(s): R01GM135444,R01GM139856
Thibault Legal, Mireya Parra, Maxwell Tong, Corbin S. Black, Ewa Joachimiak, Melissa Valente-Paterno, Karl Lechtreck, Jacek Gaertig, Khanh Huy Bui; CEP104/FAP256 and associated cap complex maintain stability of the ciliary tip. J Cell Biol 6 November 2023; 222 (11): e202301129. doi: https://doi.org/10.1083/jcb.202301129
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