Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase

In Soo Yoon, Ji Hyung Chung, Soo Hyun Hahm, Min Ju Park, You Ri Lee, Sung Il Ko, Lin Woo Kang, Tae Sung Kim, Joon Kim, Ye Sun Han

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


Ribosomal protein S3 (rpS3) is a multifunctional protein involved in translation, DNA repair, and apoptosis. The relationship between rpS3 and cyclin-dependent kinases (Cdks) involved in cell cycle regulation is not yet known. Here, we show that rpS3 is phosphorylated by Cdk1 in G2/M phase. Co-immunoprecipitation and GST pull-down assays revealed that Cdk1 interacted with rpS3. An in vitro kinase assay showed that Cdk1 phosphorylated rpS3 protein. Phosphorylation of rpS3 increased in nocodazole-arrested mitotic cells; however, treatment with Cdk1 inhibitor or Cdk1 siRNA significantly attenuated this phosphorylation event. The phosphorylation of a mutant form of rpS3, T221A, was significantly reduced compared with wild-type rpS3. Decreased phosphorylation and nuclear accumulation of T221A was much more pronounced in G2/M phase. These results suggest that the phosphorylation of rpS3 by Cdk1 occurs at Thr221 during G2/M phase and, moreover, that this event is important for nuclear accumulation of rpS3.

Original languageEnglish
Pages (from-to)529-534
Number of pages6
JournalBMB reports
Issue number8
Publication statusPublished - 2011 Aug


  • Cdk1/cdc2
  • Cell cycle
  • Phosphorylation
  • RpS3

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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