Structure of the C. Elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases

Shimanovskaya, Ekaterina; Lettman, Molly M.; Round, Adam; Lesigang, Johannes; Svergun, Dmitri; Viscardi, Valeria; Qiao, Renping; Dong, Gang; Oegema, Karen

doi:10.1016/j.str.2014.05.009

Journal Article

PUBDB-2015-01335

Structure of the C. Elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases

Shimanovskaya, E. (Corresponding Author)>Extern* ; Viscardi, V. ; Lesigang, J. ; Lettman, M. ; Qiao, R. ; Svergun, D.>Extern*EMBL* ; Round, A. ; Oegema, K. ; Dong, G.>Extern*

2014
Elsevier Science London [u.a.]

Structure 22(8), 1090 - 1104 (2014) [10.1016/j.str.2014.05.009]

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Please use a persistent id in citations: doi:10.1016/j.str.2014.05.009

Abstract: Plk4 family kinases control centriole assembly. Plk4s target mother centrioles through an interaction between their cryptic polo box (CPB) and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. Here, we report a crystal structure for the CPB of C. elegans ZYG-1, which forms a Z-shaped dimer containing an intermolecular β sheet with an extended basic surface patch. Biochemical and in vivo analysis revealed that electrostatic interactions dock the ZYG-1 CPB basic patch onto the SPD-2-derived acidic region to promote ZYG-1 targeting and new centriole assembly. Analysis of a different crystal form of the Drosophila Plk4 (DmPlk4) CPB suggests that it also forms a Z-shaped dimer. Comparison of the ZYG-1 and DmPlk4 CPBs revealed structural changes in the ZYG-1 CPB that confer selectivity for binding SPD-2 over Asterless-derived acidic regions. Overall, our findings suggest a conserved mechanism for centriolar docking of Plk4 homologs that initiate daughter centriole assembly.

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