Regulation of ubiquitination-mediated protein degradation by survival kinases in cancer.
Regulation of ubiquitination-mediated protein degradation by survival kinases in cancer.
复制标题
调节泛素化介导的蛋白质通过癌症中的存活激酶降解。
DOI：
10.3389/fonc.2012.00015
复制
发表时间：
2012
影响因子：
4.7
通讯作者：
Hung MC
中科院分区：
文献类型：
--
作者：
Yamaguchi H;Hsu JL;Hung MC
泛素-蛋白酶体系统通过选择性降解靶蛋白对多种生理过程至关重要，并且已被证明在人类癌症中起关键作用。致癌因子的激活和肿瘤抑制因子的抑制已被证明是癌症发展所必需的，并且蛋白质泛素化已与致癌因子和肿瘤抑制因子的调节相关联。三种激酶，AKT，细胞外信号调节激酶和IκB激酶，我们称为癌激酶，在多种人类癌症中被激活。我们和其他人已经确定了几个关键的下游靶标，这些靶标通常由这些致癌激酶调节，其中一些通过泛素介导的蛋白酶体降解直接或间接调节，包括FOXO 3，β-连环蛋白，髓样细胞白血病-1和Snail。在这篇综述中，我们总结了我们和其他小组的这些发现，并讨论了未来潜在的研究和临床应用。
The ubiquitin–proteasome system is essential for multiple physiological processes via selective degradation of target proteins and has been shown to plays a critical role in human cancer. Activation of oncogenic factors and inhibition of tumor suppressors have been shown to be essential for cancer development, and protein ubiquitination has been linked to the regulation of oncogenic factors and tumor suppressors. Three kinases, AKT, extracellular signal-regulated kinase, and IκB kinase, we refer to as oncokinases, are activated in multiple human cancers. We and others have identified several key downstream targets that are commonly regulated by these oncokinases, some of which are regulated directly or indirectly via ubiquitin-mediated proteasome degradation, including FOXO3, β-catenin, myeloid cell leukemia-1, and Snail. In this review, we summarize these findings from our and other groups and discuss potential future studies and applications in the clinic.