Cep78 is a new centriolar protein involved in Plk4-induced centriole overduplication

• Published in: Journal of cell science Vol. 129; no. 14; pp. 2713 - 2718
• Main Authors: Brunk, Kathrin, Zhu, Mei, Bärenz, Felix, Kratz, Anne-Sophie, Haselmann-Weiss, Uta, Antony, Claude, Hoffmann, Ingrid
• Format: Journal Article
• Language: English
• Published: England 15.07.2016
• Subjects: Cell Cycle Proteins - metabolism; Centrioles - metabolism; HeLa Cells; Humans; Interphase; Protein Binding; Protein Transport; Protein-Serine-Threonine Kinases - metabolism; Cep78; Centriole duplication; Plk4; Centrosome
• ISSN: 0021-9533; 1477-9137
• DOI: 10.1242/jcs.184093

Centrioles are core components of centrosomes, the major microtubule-organizing centers of animal cells, and act as basal bodies for cilia formation. Control of centriole number is therefore crucial for genome stability and embryogenesis. Centriole duplication requires the serine/threonine protein kinase Plk4. Here, we identify Cep78 as a human centrosomal protein and a new interaction partner of Plk4. Cep78 is mainly a centriolar protein that localizes to the centriolar wall. Furthermore, we find that Plk4 binds to Cep78 through its N-terminal domain but that Cep78 is not an in vitro Plk4 substrate. Cep78 colocalizes with Plk4 at centrioles and is required for Plk4-induced centriole overduplication. Interestingly, upon depletion of Cep78, newly synthesized Plk4 is not localized to centrosomes. Our results suggest that the interaction between Cep78 and the N-terminal catalytic domain of Plk4 is a new and important element in the centrosome overduplication process.