Centrosomal organization of Cep152 provides flexibility in Plk4 and procentriole positioning

J Cell Biol. 2023 Dec 4;222(12):e202301092. doi: 10.1083/jcb.202301092. Epub 2023 Sep 14.

Abstract

Centriole duplication is a high-fidelity process driven by Polo-like kinase 4 (Plk4) and a few conserved initiators. Dissecting how Plk4 and its receptors organize within centrosomes is critical to understand the centriole duplication process and biochemical and architectural differences between centrosomes of different species. Here, at nanoscale resolution, we dissect centrosomal localization of Plk4 in G1 and S phase in its catalytically active and inhibited state during centriole duplication and amplification. We build a precise distribution map of Plk4 and its receptor Cep152, as well as Cep44, Cep192, and Cep152-anchoring factors Cep57 and Cep63. We find that Cep57, Cep63, Cep44, and Cep192 localize in ninefold symmetry. However, during centriole maturation, Cep152, which we suggest is the major Plk4 receptor, develops a more complex pattern. We propose that the molecular arrangement of Cep152 creates flexibility for Plk4 and procentriole placement during centriole initiation. As a result, procentrioles form at variable positions in relation to the mother centriole microtubule triplets.

Publication types

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

MeSH terms

  • Cell Cycle / genetics
  • Cell Cycle Proteins* / genetics
  • Centrioles* / genetics
  • Centrosome*
  • Humans
  • Microtubules / genetics
  • Protein Serine-Threonine Kinases* / genetics
  • S Phase

Substances

  • CEP152 protein, human
  • PLK4 protein, human
  • Cell Cycle Proteins
  • Protein Serine-Threonine Kinases