Cep68 act as an important linker protein of centrosomes and centriole disengagement

 

In cell cycle, two centrosomes and two centrioles (parental centriole and daughter centriole), the components of centrosomes, need to be disengaged at different stages. The mechanism of this process is intrcate and has not been fully understood. Pagan et al. indentified the important roles of Cep68 and other related factors during the disengagement of centrosomes and entrioles. The article was published on Nature Cell Biology, recently.

 

Several proteins including Cep68, rootletin, LRCC45, centlein, and c-Nap1, have been reported as as intercentrosomal linker proteins. The loss of these proteins leads to separation of centrosoms in interphase. In this study, Cep68 is proved to be degraded by the Skp1-Cul1-F-box protein (SCF^βTrCP) unbiquitin ligase complex, which has been shown to facilitate centrosome duplication. Following the recognition by βTrCP, Cep68 is degraded by PLK1 phosphorylation on Ser 332 of Cep68. On the other hand, Cep68 is also an important protein in regulating centriole disengagement. Researchers found Cep68 forms a complex with two centriole engagement-related pericentriolar material (PCM) proteins, Cep215 and pericentrin (PCNT). As Cep68 and PCNT bind to different site of Cep215, they suggested Cep215 is removed from PCM by Cep68 degradation and PCNT cleavage, either to promote or to inhibit centriole disengagement, respectively. The findings provide an in-depth mechanism of centrosomes and centriole disengagement during cell cycle.

 

Reference:
Nat Cell Biol. 2015 Jan;17(1):31-43.

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