Aggregation of Ribosomal Protein S6 at Nucleolus Is Cell Cycle-Controlled and Its Function in Pre-rRNA Processing Is Phosphorylation Dependent

作者：Zhang, Duo; Chen, Hui-Peng; Duan, Hai-Feng; Gao, Li-Hua; Shao, Yong; Chen, Ke-Yan; Wang, You-Liang; Lan, Feng-Hua^*; Hu, Xian-Wen^*

来源：Journal of Cellular Biochemistry, 2016, 117(7): 1649-1657.

DOI：10.1002/jcb.25458

• RIBOSOMAL PROTEIN S6
• 40S RIBOSOMAL SUBUNIT
• PHOSPHORYLATION
• CELL CYCLE
• PRE-rRNA

Ribosomal protein S6 (rpS6) has long been regarded as one of the primary r-proteins that functions in the early stage of 40S subunit assembly, but its actual role is still obscure. The correct forming of 18S rRNA is a key step in the nuclear synthesis of 40S subunit. In this study, we demonstrate that rpS6 participates in the processing of 30S pre-rRNA to 18S rRNA only when its C-terminal five serines are phosphorylated, however, the process of entering the nucleus and then targeting the nucleolus does not dependent its phosphorylation. Remarkably, we also find that the aggregation of rpS6 at the nucleolus correlates to the phasing of cell cycle, beginning to concentrate in the nucleolus at later S phase and disaggregate at M phase.

• 出版日期2016-7
• 单位北京中医药大学; 中国人民解放军南京军区福州总医院; 厦门大学