Tournier Cathy
University of Manchester, Manchester, UK.
Genes Cancer. 2013 Sep;4(9-10):397-400. doi: 10.1177/1947601913486349.
c-Jun NH2-terminal kinase (JNK) was discovered almost 20 years ago as the protein kinase responsible for phosphorylating c-Jun at Ser-63 and Ser-73. These sites had previously been demonstrated to be essential for the stimulation of c-Jun activity and for cooperation with Ha-ras in oncogenic transformation. This led to the idea that JNK was a positive regulator of cellular transformation. However, the analysis of jnk gene deletion in various mouse models of cancer has produced conflicting findings, with some studies supporting the pro-oncogenic function of JNK and others providing evidence that JNK acts as a tumor suppressor. This review will discuss how these unexpected findings have increased our understanding of the role of JNK signaling in cancer and have provided a source of new working hypotheses.
c-Jun氨基末端激酶(JNK)大约在20年前被发现,是负责在Ser-63和Ser-73位点磷酸化c-Jun的蛋白激酶。这些位点此前已被证明对于刺激c-Jun活性以及与Ha-ras在致癌转化中的协同作用至关重要。这导致了JNK是细胞转化的正调控因子这一观点。然而,在各种癌症小鼠模型中对jnk基因缺失的分析产生了相互矛盾的结果,一些研究支持JNK的促癌功能,而另一些研究则提供证据表明JNK起到肿瘤抑制作用。本综述将讨论这些意外发现如何增进了我们对JNK信号通路在癌症中作用的理解,并提供了新的工作假设来源。