Ontology highlight
ABSTRACT:
SUBMITTER: Cottee MA
PROVIDER: S-EPMC5374404 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Cottee Matthew A MA Johnson Steven S Raff Jordan W JW Lea Susan M SM
Biology open 20170315 3
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 the <i>Drosophila</i> Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer <i>in vitro</i> that li ...[more]