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Direct binding of SAS-6 to ZYG-1 recruits SAS-6 to the mother centriole for cartwheel assembly.
- Source :
-
Developmental cell [Dev Cell] 2013 May 13; Vol. 25 (3), pp. 284-98. - Publication Year :
- 2013
-
Abstract
- Assembly of SAS-6 dimers to form the centriolar cartwheel requires the ZYG-1/Plk4 kinase. Here, we show that ZYG-1 recruits SAS-6 to the mother centriole independently of its kinase activity; kinase activity is subsequently required for cartwheel assembly. We identify a direct interaction between ZYG-1 and the SAS-6 coiled coil that explains its kinase activity-independent function in SAS-6 recruitment. Perturbing this interaction, or the interaction between an adjacent segment of the SAS-6 coiled coil and SAS-5, prevented SAS-6 recruitment and cartwheel assembly. SAS-6 mutants with alanine substitutions in a previously described ZYG-1 target site or in 37 other residues, either phosphorylated by ZYG-1 in vitro or conserved in closely related nematodes, all supported cartwheel assembly. We propose that ZYG-1 binding to the SAS-6 coiled coil recruits the SAS-6-SAS-5 complex to the mother centriole, where a ZYG-1 kinase activity-dependent step, whose target is unlikely to be SAS-6, triggers cartwheel assembly.<br /> (Copyright © 2013 Elsevier Inc. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Animals, Genetically Modified embryology
Animals, Genetically Modified genetics
Animals, Genetically Modified metabolism
Caenorhabditis elegans embryology
Caenorhabditis elegans genetics
Caenorhabditis elegans Proteins genetics
Cell Cycle Proteins genetics
Centrioles genetics
Conserved Sequence
Embryo, Nonmammalian metabolism
Enzyme Activation
Male
Molecular Sequence Data
Multiprotein Complexes genetics
Multiprotein Complexes metabolism
Mutation
Phosphorylation
Protein Binding
Protein Interaction Mapping
Protein Kinases genetics
Protein Multimerization
RNA Interference
Transgenes
Caenorhabditis elegans metabolism
Caenorhabditis elegans Proteins metabolism
Cell Cycle Proteins metabolism
Centrioles metabolism
Protein Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1878-1551
- Volume :
- 25
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Developmental cell
- Publication Type :
- Academic Journal
- Accession number :
- 23673331
- Full Text :
- https://doi.org/10.1016/j.devcel.2013.03.011