Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases.

@article{Shimanovskaya2014StructureOT,
  title={Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases.},
  author={Ekaterina Shimanovskaya and Valeria Viscardi and Johannes Lesigang and Molly M Lettman and Renping Qiao and Dmitri I. Svergun and Adam Round and Karen Oegema and Gang Dong},
  journal={Structure},
  year={2014},
  volume={22 8},
  pages={1090-1104}
}
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… CONTINUE READING
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