title: 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.
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Jingyan
authors.identifier: http://orcid.org/0000-0002-5896-8132
authors.initials: J
authors.lastname: Fu
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Zoltan
authors.identifier: http://orcid.org/0000-0002-2067-0832
authors.initials: Z
authors.lastname: Lipinszki
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Hélène
authors.initials: H
authors.lastname: Rangone
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Mingwei
authors.initials: M
authors.lastname: Min
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Charlotte
authors.initials: C
authors.lastname: Mykura
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Jennifer
authors.initials: J
authors.lastname: Chao-Chu
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Sandra
authors.initials: S
authors.lastname: Schneider
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: Nikola S
authors.initials: NS
authors.lastname: Dzhindzhev
authors.affiliation: Department of Life Sciences, University of Siena, Via A. Moro 4, 53100 Siena, Italy.
authors.forename: Marco
authors.initials: M
authors.lastname: Gottardo
authors.affiliation: Department of Life Sciences, University of Siena, Via A. Moro 4, 53100 Siena, Italy.
authors.forename: Maria Giovanna
authors.initials: MG
authors.lastname: Riparbelli
authors.affiliation: Department of Life Sciences, University of Siena, Via A. Moro 4, 53100 Siena, Italy.
authors.forename: Giuliano
authors.initials: G
authors.lastname: Callaini
authors.affiliation: Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
authors.forename: David M
authors.initials: DM
authors.lastname: Glover
mesh_terms: D000818:Animals; D002453:Cell Cycle / Q000235:genetics / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002502:Centrioles / Q000378:metabolism*; D018385:Centrosome / Q000378:metabolism*; D029721:Drosophila Proteins / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D008938:Mitosis / Q000502:physiology*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism
chemical_list: D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; D017346:Protein Serine-Threonine Kinases