磷酸化
p38丝裂原活化蛋白激酶
细胞凋亡
细胞生物学
MAPK/ERK通路
生物
DNA损伤
信号转导
化学
DNA
生物化学
作者
Cheng Lu,Ying Shi,Zhe Wang,Zhihong Song,Mei-Cai Zhu,Qing-Qing Cai,Tao Chen
出处
期刊:FEBS Letters
[Wiley]
日期:2008-07-09
卷期号:582 (18): 2703-2708
被引量:76
标识
DOI:10.1016/j.febslet.2008.06.051
摘要
Phosphorylation of H2AX is believed to be associated with the repair of damaged DNA. Recent findings suggest a novel function of H2AX in cellular apoptosis. Specifically, it was shown that ultraviolet A-activated JNK phosphorylates H2AX to regulate apoptosis. Here we show that serum starvation induces H2AX phosphorylation and apoptosis independent of the JNK pathway. Serum starvation induced p38 phosphorylation, whereas it did not affect the phosphorylation of ERK or JNK. Inhibition of p38 reduced H2AX phosphorylation and apoptosis. Furthermore, p38 was found to phosphorylate H2AX directly in vitro and was colocalized with H2AX in vivo. Finally, we demonstrate that H2AX phosphorylation is required for serum starvation-induced apoptosis. Taken together, these data elucidate a novel signaling pathway (p38/H2AX) to regulate apoptosis.
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