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J Cell Biol. 2020 Feb 3;219(2). pii: e201905172. doi: 10.1083/jcb.201905172.

A molecular mechanism for the procentriole recruitment of Ana2.

Author information

1
Department of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ.
2
National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD.
#
Contributed equally

Abstract

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.

PMID:
31841145
DOI:
10.1083/jcb.201905172

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