Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase
- Authors
- Yoon, In-Soo; Chung, Ji Hyung; Hahm, Soo-Hyun; Park, Min Ju; Lee, You Ri; Il Ko, Sung; Kang, Lin-Woo; Kim, Tae-Sung; Kim, Joon; Han, Ye Sun
- Issue Date
- 31-8월-2011
- Publisher
- KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
- Keywords
- Cdk1/cdc2; Cell cycle; Phosphorylation; RpS3
- Citation
- BMB REPORTS, v.44, no.8, pp.529 - 534
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- BMB REPORTS
- Volume
- 44
- Number
- 8
- Start Page
- 529
- End Page
- 534
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/111754
- DOI
- 10.5483/BMBRep.2011.44.8.529
- ISSN
- 1976-6696
- Abstract
- 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. [BMB reports 2011; 44(8): 529-534]
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