title: A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.
abstract: 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.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Cottee
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
authors.forename: Steven
authors.initials: S
authors.lastname: Johnson
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK jordan.raff@path.ox.ac.uk susan.lea@path.ox.ac.uk.
authors.forename: Jordan W
authors.identifier: http://orcid.org/0000-0002-4689-1297
authors.initials: JW
authors.lastname: Raff
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK jordan.raff@path.ox.ac.uk susan.lea@path.ox.ac.uk.
authors.forename: Susan M
authors.initials: SM
authors.lastname: Lea
keywords: Cartwheel; Centriole duplication; Centrosome