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000207425 1001_ $$0P:(DE-H253)PIP1016655$$aShimanovskaya, Ekaterina$$b0$$eCorresponding Author
000207425 245__ $$aStructure of the C. Elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases
000207425 260__ $$aLondon [u.a.]$$bElsevier Science$$c2014
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000207425 520__ $$aPlk4 family kinases control centriole assembly. Plk4s target mother centrioles through an interaction between their cryptic polo box (CPB) and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. Here, we report a crystal structure for the CPB of C. elegans ZYG-1, which forms a Z-shaped dimer containing an intermolecular β sheet with an extended basic surface patch. Biochemical and in vivo analysis revealed that electrostatic interactions dock the ZYG-1 CPB basic patch onto the SPD-2-derived acidic region to promote ZYG-1 targeting and new centriole assembly. Analysis of a different crystal form of the Drosophila Plk4 (DmPlk4) CPB suggests that it also forms a Z-shaped dimer. Comparison of the ZYG-1 and DmPlk4 CPBs revealed structural changes in the ZYG-1 CPB that confer selectivity for binding SPD-2 over Asterless-derived acidic regions. Overall, our findings suggest a conserved mechanism for centriolar docking of Plk4 homologs that initiate daughter centriole assembly.
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000207425 7001_ $$0P:(DE-HGF)0$$aViscardi, Valeria$$b1
000207425 7001_ $$0P:(DE-HGF)0$$aLesigang, Johannes$$b2
000207425 7001_ $$0P:(DE-HGF)0$$aLettman, Molly M.$$b3
000207425 7001_ $$0P:(DE-HGF)0$$aQiao, Renping$$b4
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000207425 7001_ $$0P:(DE-HGF)0$$aRound, Adam$$b6
000207425 7001_ $$0P:(DE-HGF)0$$aOegema, Karen$$b7
000207425 7001_ $$0P:(DE-H253)PIP1016609$$aDong, Gang$$b8
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