Proteins that control the geometry of ciliary ends

Louka, Panagiota; Vasudevan, Krishna Kumar; Guha, Mayukh; Joachimiak, Ewa; Wloga, Dorota; Tomasi, Raphaël F.‑X.; Baroud, Charles N.; Dupuis‑Williams, Pascale; Galati, Domenico
F.; G. Pearson, Chad; Rice, Luke M.; Moresco, James J.; Jiang, Yu‑Yang; Lechtreck, Karl; Dentler, William; Gaertig, Jacek; R. Yates III, John

doi:10.25376/hra.7872338.v1

Proteins that control the geometry of ciliary ends.pdf (5.41 MB)

Proteins that control the geometry of ciliary ends

journal contribution

posted on 2019-03-25, 09:00 authored by Panagiota Louka, Krishna Kumar Vasudevan, Mayukh Guha, Ewa Joachimiak, Dorota Wloga, Raphaël F.‑X. Tomasi, Charles N. Baroud, Pascale Dupuis‑Williams, Domenico F. Galati, Chad G. Pearson, Luke M. Rice, James J. Moresco, Yu‑Yang Jiang, Karl Lechtreck, William Dentler, Jacek Gaertig, John R. Yates III

We studied three conserved ciliary proteins, FAP256/CEP104, CHE12/Crescerin and ARMC9, in the ciliate Tetrahymena. Using a combination of super-resolution structural illumination and electron microscopy we show that these proteins localize near the plus ends of ciliary microtubules where they control their length and subsequently the structural organization of ciliary ends. Our results show that defects in the geometry of ciliary ends affect the function of cilia.