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A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies

DOI: 10.1242/bio.024661 DOI Help

Authors: Matthew A. Cottee (University of Oxford) , Steven Johnson (University of Oxford) , Jordan W. Raff (University of Oxford) , Susan M. Lea (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biology Open

State: Published (Approved)
Published: February 2017
Diamond Proposal Number(s): 9306

Open Access Open Access

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.

Journal Keywords: centriole duplication; centrosome; cartwheel

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Other Facilities: European Synchrotron Radiation Facility


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