Faculty of Basic Medicine, MV Lomonosov Moscow State University, 119991 Moscow, Russia.
Faculty of Basic Medicine, MV Lomonosov Moscow State University, 119991 Moscow, Russia; Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Box 210, 17177 Stockholm, Sweden.
Trends Cell Biol. 2017 May;27(5):322-339. doi: 10.1016/j.tcb.2017.01.003. Epub 2017 Feb 7.
Apoptosis is a crucial program of cell death that controls development and homeostasis of multicellular organisms. The main initiators and executors of this process are the Cysteine-dependent ASPartate proteASES - caspases. A number of regulatory circuits tightly control caspase processing and activity. One of the most important, yet, at the same time still poorly understood control mechanisms of activation of caspases involves their post-translational modifications. The addition and/or removal of chemical groups drastically alters the catalytic activity of caspases or stimulates their nonapoptotic functions. In this review, we will describe and discuss the roles of key caspase modifications such as phosphorylation, ubiquitination, nitrosylation, glutathionylation, SUMOylation, and acetylation in the regulation of apoptotic cell death and cell survival.
细胞凋亡是一种控制多细胞生物发育和内稳态的细胞死亡的关键程序。这个过程的主要启动子和执行者是半胱氨酸依赖性天冬氨酸特异性蛋白酶 - 胱天蛋白酶。许多调节回路严格控制半胱天冬酶的加工和活性。其中一个最重要的,但同时仍然理解甚少的激活胱天蛋白酶的控制机制涉及它们的翻译后修饰。化学基团的添加和/或去除会极大地改变胱天蛋白酶的催化活性或刺激其非凋亡功能。在这篇综述中,我们将描述和讨论关键的胱天蛋白酶修饰,如磷酸化、泛素化、硝化、谷胱甘肽化、SUMO 化和乙酰化,在调节细胞凋亡和细胞存活中的作用。