TY  - JOUR
AU  - Shimanovskaya, Ekaterina
AU  - Viscardi, Valeria
AU  - Lesigang, Johannes
AU  - Lettman, Molly M.
AU  - Qiao, Renping
AU  - Svergun, Dmitri
AU  - Round, Adam
AU  - Oegema, Karen
AU  - Dong, Gang
TI  - Structure of the C. Elegans ZYG-1 Cryptic Polo Box Suggests a Conserved Mechanism for Centriolar Docking of Plk4 Kinases
JO  - Structure
VL  - 22
IS  - 8
SN  - 0969-2126
CY  - London [u.a.]
PB  - Elsevier Science
M1  - PUBDB-2015-01335
SP  - 1090 - 1104
PY  - 2014
N1  - (c) Elsevier Ltd. Post referee full text in progress.
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000340488100004
C6  - pmid:24980795
DO  - DOI:10.1016/j.str.2014.05.009
UR  - https://bib-pubdb1.desy.de/record/207425
ER  -