title: Plk4-dependent phosphorylation of STIL is required for centriole duplication.
abstract: Duplication of centrioles, namely the formation of a procentriole next to the parental centriole, is regulated by the polo-like kinase Plk4. Only a few other proteins, including STIL (SCL/TAL1 interrupting locus, SIL) and Sas-6, are required for the early step of centriole biogenesis. Following Plk4 activation, STIL and Sas-6 accumulate at the cartwheel structure at the initial stage of the centriole assembly process. Here, we show that STIL interacts with Plk4 in vivo. A STIL fragment harboring both the coiled-coil domain and the STAN motif shows the strongest binding affinity to Plk4. Furthermore, we find that STIL is phosphorylated by Plk4. We identified Plk4-specific phosphorylation sites within the C-terminal domain of STIL and show that phosphorylation of STIL by Plk4 is required to trigger centriole duplication.
authors.affiliation: Cell Cycle Control and Carcinogenesis, F045, German Cancer Research Center, DKFZ, 69120 Heidelberg, Germany.
authors.forename: Anne-Sophie
authors.initials: AS
authors.lastname: Kratz
authors.affiliation: Cell Cycle Control and Carcinogenesis, F045, German Cancer Research Center, DKFZ, 69120 Heidelberg, Germany.
authors.forename: Felix
authors.initials: F
authors.lastname: Bärenz
authors.affiliation: Cell Cycle Control and Carcinogenesis, F045, German Cancer Research Center, DKFZ, 69120 Heidelberg, Germany.
authors.forename: Kai T
authors.initials: KT
authors.lastname: Richter
authors.affiliation: Cell Cycle Control and Carcinogenesis, F045, German Cancer Research Center, DKFZ, 69120 Heidelberg, Germany Ingrid.Hoffmann@dkfz.de.
authors.forename: Ingrid
authors.initials: I
authors.lastname: Hoffmann
keywords: Centriole duplication; Centrosome; Phosphorylation; Plk4; STIL