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A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell

Silvia Martini1, Khalil Davis1, Rupert Faraway2,3

  • 1Protein Phosphorylation Laboratory, The Francis Crick Institute, London, UK.

Nature Communications
|November 27, 2021
PubMed

Insights

Protein kinase C epsilon (PKCε) controls cell division through SERBP1, a protein that regulates translation and forms M-bodies. This pathway is essential for genome protection during mitosis, independent of Aurora B.

Area of Science:

  • Molecular and Cellular Biology
  • Cancer Research
  • Cell Cycle Regulation

Background:

  • The PKCε-regulated pathway protects transformed cells during mitosis.
  • Aurora B is crucial for this pathway, but its sufficiency and other PKCε targets remain unclear.

Purpose of the Study:

  • To investigate other PKCε cell cycle targets involved in genome protection.
  • To elucidate the role of SERBP1 in mitosis and its relationship with PKCε and Aurora B.

Main Methods:

  • Developed a UV-photocrosslinkable amino acid trapping strategy targeting the PKCε kinase domain.
  • Validated SERBP1 as a PKCε substrate and analyzed its role in mitotic events.

Main Results:

  • Identified SERBP1 as a PKCε substrate, controlling mitotic events via translational regulation.
  • PKCε represses translation, affecting SERBP1 binding to the 40S ribosomal subunit and promoting M-body formation.
  • SERBP1 is essential for chromosome segregation and cell division, correlating with M-body assembly, independent of Aurora B.

Conclusions:

  • SERBP1 is a key mediator in the PKCε-controlled genome protection pathway.
  • Aurora B collaborates with translational regulation mediated by SERBP1 for successful mitosis.

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