Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1793, Issue 2, Pages 395-405Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2008.10.017
Keywords
PKC delta; rpS3; Src; Endonuclease activity
Categories
Funding
- DNA Repair [2006-02293]
- Proteomics [FPR05C2-390]
- National Research Foundation of Korea [2006-02304, 13-2008-00-024-00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 PKC delta 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 PKC delta-dependent phosphorylation. (c) 2008 Elsevier B.V. All rights reserved.
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