%0 Journal Article
%A Shimanovskaya, Ekaterina
%A Viscardi, Valeria
%A Lesigang, Johannes
%A Lettman, Molly M.
%A Qiao, Renping
%A Svergun, Dmitri
%A Round, Adam
%A Oegema, Karen
%A Dong, Gang
%T Structure of the C. Elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases
%J Structure
%V 22
%N 8
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M PUBDB-2015-01335
%P 1090 - 1104
%D 2014
%Z (c) Elsevier Ltd. Post referee full text in progress.
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000340488100004
%$ pmid:24980795
%R 10.1016/j.str.2014.05.009
%U https://bib-pubdb1.desy.de/record/207425