Conserved molecular interactions in centriole-to-centrosome conversion
Abstract
Centrioles are required to assemble centrosomes for cell division and cilia for motility and signalling. New centrioles assemble perpendicularly to pre-existing ones in G1–S and elongate throughout S and G2. Fully elongated daughter centrioles are converted into centrosomes during mitosis to be able to duplicate and organize pericentriolar material in the next cell cycle. Here we show that centriole-to-centrosome conversion requires sequential loading of Cep135, Ana1 (Cep295) and Asterless (Cep152) onto daughter centrioles during mitotic progression in both Drosophila melanogaster and human. This generates a molecular network spanning from the inner- to outermost parts of the centriole. Ana1 forms a molecular strut within the network, and its essential role can be substituted by an engineered fragment providing an alternative linkage between Asterless and Cep135. This conserved architectural framework is essential for loading Asterless or Cep152, the partner of the master regulator of centriole duplication, Plk4. Our study thus uncovers the molecular basis for centriole-to-centrosome conversion that renders daughter centrioles competent for motherhood.
Additional Information
© 2016 Nature Publishing Group. Received 25 February 2015. Accepted 21 October 2015. Published 23 November 2015. J.F., Z.L., S.S. and N.S.D. are supported by a Programme Grant to D.M.G. from Cancer Research UK. H.R. is supported by an MRC Programme Grant to D.M.G. J.F. thanks the British Academy and the Royal Society for the Newton International Fellowship and Z.L. thanks the Federation of European Biochemical Societies for the Long-Term postdoctoral Fellowship. The authors thank N. Lawrence and A. Sossick for assistance with 3D-SIM. Author Contributions: J.F. designed and performed experiments; Z.L. carried out biochemical analysis; H.R. carried out studies on mutant Drosophila; M.G., M.G.R. and G.C. performed electron microscopy; M.M., C.M., J.C.-C., S.S. and N.S.D. contributed material support; J.F. and D.M.G. analysed results and wrote manuscript. Z.L. and H.R. commented on the manuscript. The authors declare no competing financial interests.Attached Files
Accepted Version - emss-65742.pdf
Supplemental Material - 41556_2016_Article_BFncb3274_Fig10_ESM.jpg
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Supplemental Material - 41556_2016_BFncb3274_MOESM12_ESM.pdf
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Additional details
- PMCID
- PMC4719191
- Eprint ID
- 104837
- DOI
- 10.1038/ncb3274
- Resolver ID
- CaltechAUTHORS:20200807-170349570
- Cancer Research UK
- Medical Research Council (UK)
- British Academy
- Royal Society
- Federation of European Biochemical Societies
- Created
-
2020-08-11Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field