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

Matthew A. Cottee, Steven Johnson, Jordan W. Raff, Susan M. Lea

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)381-389
Number of pages9
JournalBiology Open
Volume6
Issue number3
DOIs
Publication statusPublished - 15 Mar 2017
Externally publishedYes

Keywords

  • Cartwheel
  • Centriole duplication
  • Centrosome

Cite this