PKCδ-dependent functional switch of rpS3 between translation and DNA repair

Tae Sung Kim, Hag Dong Kim, Joon Kim

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)


Ribosomal protein S3 (rpS3) is critically involved in translation as a component of the 40S ribosomal subunit and participates in the processing of DNA damage, functioning as a damage DNA endonuclease. However, it is not yet known how the function of rpS3 switches between translation and DNA repair. Here we show that PKCδ phosphorylates rpS3 resulting in its mobilization in the nucleus to repair damaged DNA. Phosphorylated rpS3 was only detected in non-ribosomal rpS3 and the repair endonuclease activity of rpS3 was increased by its phosphorylation. In addition, rpS3 knock-down cells showed more sensitivity to genotoxic stress than control cells, and this sensitivity was corrected by overexpressed wild-type rpS3 but not by phosphorylation defective rpS3. In conclusion, we propose that the destiny of rpS3 molecules between translation and DNA repair is regulated by PKCδ-dependent phosphorylation.

Original languageEnglish
Pages (from-to)395-405
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number2
Publication statusPublished - 2009 Feb


  • Endonuclease activity
  • PKCδ
  • Src
  • rpS3

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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