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Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases.
- Source :
-
Structure (London, England : 1993) [Structure] 2014 Aug 05; Vol. 22 (8), pp. 1090-1104. Date of Electronic Publication: 2014 Jun 26. - Publication Year :
- 2014
-
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.<br /> (Copyright © 2014 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Caenorhabditis elegans Proteins genetics
Centrioles metabolism
Dimerization
Molecular Sequence Data
Protein Binding
Protein Kinases genetics
Protein Structure, Tertiary
Species Specificity
Structure-Activity Relationship
Caenorhabditis elegans genetics
Caenorhabditis elegans Proteins chemistry
Caenorhabditis elegans Proteins metabolism
Centrioles physiology
Models, Molecular
Protein Kinases chemistry
Protein Kinases metabolism
Protein Serine-Threonine Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 22
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 24980795
- Full Text :
- https://doi.org/10.1016/j.str.2014.05.009