A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.
Cottee MA., Johnson S., Raff JW., Lea SM.
A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of PLK4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of PLK4 and the coiled-coil domain of STIL (HsCCD). We showed previously that theDrosophilaAna2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramerin vitrothat likely precludes an interaction with PB3. Here, we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimersin vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, althoughDrosophilaPB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCDin vitroThus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.