c-jun公司
泛素
生物
磷酸化
泛素连接酶
激酶
细胞生物学
转录因子
癌变
C端
生物化学
分子生物学
基因
氨基酸
作者
J Zhang,Feng Zhu,Li X,Dong Z,Yang Xu,Cong Peng,Li S,Yong-Yeon Cho,Kangde Yao,Zykova Ta,AM Bode
出处
期刊:Oncogene
[Springer Nature]
日期:2011-08-22
卷期号:31 (14): 1835-1844
被引量:23
摘要
The c-Jun transcription factor is a highly unstable oncoprotein. Several ubiquitin ligases mediate c-Jun degradation. However, c-Jun can be stabilized once it is phosphorylated at the N-terminus by c-Jun N-terminal kinases (JNKs) or other protein kinases. This phosphorylation decreases c-Jun ubiquitination and degradation. The underlying mechanism for this phenomenon is still unknown. Here, we show that receptor for activated C-kinase 1 (Rack1) can bind with c-Jun and ubiquitin ligase Fbw7 to form a complex. When c-Jun is phosphorylated at the N-terminus, c-Jun is released from the complex and cannot be ubiquitinated by Fbw7, which leads to increased stabilization and accumulation of c-Jun. These results reveal that Rack1 has a very important role in tumorigenesis by maintaining the stability of c-Jun that has been phosphorylated at its N-terminus by JNKs or other kinases.
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