生物
磷酸化
细胞生物学
爪蟾
MAPK/ERK通路
有丝分裂
激酶
磷酸化级联
核糖体s6激酶
蛋白激酶A
分子生物学
蛋白质磷酸化
生物化学
P70-S6激酶1
蛋白激酶B
基因
作者
Cong Wu,Shuaishuai Liu,Yu‐Chen Lee,Ruoning Wang,Sheng Sun,Fei Yin,William G. Bornmann,Li-yuan Yu-Lee,Gary E. Gallick,Wei Zhang,Sue-Hwa Lin,Jian Kuang
出处
期刊:Oncogene
[Springer Nature]
日期:2013-05-27
卷期号:33 (18): 2385-2394
被引量:26
摘要
Activation of the mitogen-activated protein kinase (MAPK) cascade in mammalian cell lines positively regulates the G2/M transition. The molecular mechanism underlying this biological phenomenon remains poorly understood. Ribosomal S6 kinase (RSK) is a key downstream element of the MAPK cascade. Our previous studies established roles of RSK2 in Cdc25C activation during progesterone-induced meiotic maturation of Xenopus oocytes. In this study we demonstrate that both recombinant RSK and endogenous RSK in Xenopus egg extracts phosphorylate all three isoforms of human Cdc25 at a conserved motif near the catalytic domain. In human HEK293 and PC-3mm2 cell lines, RSK preferentially phosphorylates Cdc25A and Cdc25B in mitotic cells. Phosphorylation of the RSK sites in these Cdc25 isoforms increases their M-phase-inducing activities. Inhibition of RSK-mediated phosphorylation of Cdc25 inhibits G2/M transition. Moreover, RSK is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of T359/S363 in RSK. Together, these findings indicate that RSK promotes G2/M transition in mammalian cells through activating phosphorylation of Cdc25A and Cdc25B.
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