Pericentrin-mediated SAS-6 recruitment promotes centriole assembly

Daisuke Ito (1) , Sihem Zitouni (1) , Swadhin Chandra Jana (1) , Paulo Duarte (1) , Jaroslaw Surkont (1) , Zita Carvalho-Santos (1) , José Pereira-Leal (1, 2) , Miguel Godinho Ferreira (3) , Mónica Bettencourt-Dias (1)

1 IGC - Instituto Gulbenkian de Ciência [Oeiras]
2 Ophiomics Precision Medicine - Ophiomics
3 IRCAN - Institut de Recherche sur le Cancer et le Vieillissement

The centrosome is composed of two centrioles surrounded by a microtubulenucleating pericentriolar material (PCM). Although centrioles are known to regulate PCM assembly, it is less known whether and how the PCM contributes to centriole assembly. Here we investigate the interaction between centriole components and the PCM by taking advantage of fission yeast, which has a centriole-free, PCM-containing centrosome, the SPB. Surprisingly, we observed that several ectopically-expressed animal centriole components such as SAS-6 are recruited to the SPB. We revealed that a conserved PCM component, Pcp1/pericentrin, interacts with and recruits SAS-6. This interaction is conserved and important for centriole assembly, particularly its elongation. We further explored how yeasts kept this interaction even after centriole loss and showed that the conserved calmodulin-binding region of Pcp1/pericentrin is critical for SAS-6 interaction. Our work suggests that the PCM not only recruits and concentrates microtubule-nucleators, but also the centriole assembly machinery, promoting biogenesis close by.

Domaines: Sciences du Vivant [q-bio]; Organisation et fonctions cellulaires [q-bio.SC]

Daisuke Ito, Sihem Zitouni, Swadhin Chandra Jana, Paulo Duarte, Jaroslaw Surkont, et al.. Pericentrin-mediated SAS-6 recruitment promotes centriole assembly. eLife, 2019, 8, ⟨10.7554/eLife.41418⟩. ⟨hal-02394919⟩