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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 the Drosophila Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer in vitro that likely precludes an interaction with PB3. Here, we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers in vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although Drosophila PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD in vitro Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.

SUBMITTER: Cottee MA 

PROVIDER: S-EPMC5374404 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies.

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]

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