A molecular mechanism for the procentriole recruitment of Ana2

During centriole duplication, a preprocentriole forms at a single site on the mother centriole through a process that includes the hierarchical recruitment of a conserved set of proteins, including the Polo-like kinase 4 (Plk4), Ana2/STIL, and the cartwheel protein Sas6. Ana2/STIL is critical for pr...

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Veröffentlicht in:The Journal of cell biology 2020-02, Vol.219 (2)
Hauptverfasser: McLamarrah, Tiffany A, Speed, Sarah K, Ryniawec, John M, Buster, Daniel W, Fagerstrom, Carey J, Galletta, Brian J, Rusan, Nasser M, Rogers, Gregory C
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Sprache:eng
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Zusammenfassung:During centriole duplication, a preprocentriole forms at a single site on the mother centriole through a process that includes the hierarchical recruitment of a conserved set of proteins, including the Polo-like kinase 4 (Plk4), Ana2/STIL, and the cartwheel protein Sas6. Ana2/STIL is critical for procentriole assembly, and its recruitment is controlled by the kinase activity of Plk4, but how this works remains poorly understood. A structural motif called the G-box in the centriole outer wall protein Sas4 interacts with a short region in the N terminus of Ana2/STIL. Here, we show that binding of Ana2 to the Sas4 G-box enables hyperphosphorylation of the Ana2 N terminus by Plk4. Hyperphosphorylation increases the affinity of the Ana2-G-box interaction, and, consequently, promotes the accumulation of Ana2 at the procentriole to induce daughter centriole formation.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201905172