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KMID : 0624620110440080529
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BMB Reports
2011 Volume.44 No. 8 p.529 ~ p.534
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Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase
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Yoon In-Soo
Chung Ji-Hyung
Hahm Soo-Hyun
Park Min-Ju
Lee You-Ri
Ko Sung-Il
Kang Lin-Woo
Kim Tae-Sung
Kim Joon
Han Ye-Sun
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Abstract
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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.
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KEYWORD
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Cdk1/cdc2, Cell cycle, Phosphorylation, RpS3
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