A molecular mechanism for the procentriole recruitment of Ana2

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Animals
  • Cell Cycle / genetics
  • Cell Cycle Proteins / genetics*
  • Cell Line
  • Centrioles / genetics*
  • Drosophila Proteins / genetics*
  • Drosophila melanogaster / genetics
  • Intracellular Signaling Peptides and Proteins / genetics
  • Microtubule-Associated Proteins / genetics
  • Phosphorylation / genetics
  • Protein Binding / genetics
  • Protein Serine-Threonine Kinases / genetics*

Substances

  • Ana2 protein, Drosophila
  • Cell Cycle Proteins
  • Drosophila Proteins
  • Intracellular Signaling Peptides and Proteins
  • Microtubule-Associated Proteins
  • Sas-6 protein, Drosophila
  • Protein Serine-Threonine Kinases
  • Sak protein, Drosophila