Lee Justine C, Peter Marcus E
The Ben May Institute for Cancer Research, University of Chicago, Chicago, IL 60637, USA.
Immunol Rev. 2003 Jun;193:39-47. doi: 10.1034/j.1600-065x.2003.00043.x.
Cell elimination through apoptosis, or programmed cell death, is an evolutionarily conserved central tenet of biology from embryological development to immune homeostasis. While many of the apoptotic signaling pathways have been elucidated, the relationship between ubiquitin and apoptosis is only beginning to be defined. In the past decade, many reports of polyubiquitin conjugation of key pro- and anti-apoptotic molecules have characterized ubiquitin as an essential regulatory modification targeting proteins for proteasomal degradation. However, recent work relating monoubiquitination and nonclassical polyubiquitin conjugation to apoptotic molecules has added an additional level of diversity to the role of ubiquitin in apoptotic regulation beyond degradation. This review focuses on the direct effects of ubiquitination on apoptosis-signaling molecules.
通过凋亡或程序性细胞死亡进行的细胞清除,是生物学中从胚胎发育到免疫稳态的一个进化上保守的核心原则。虽然许多凋亡信号通路已被阐明,但泛素与凋亡之间的关系才刚刚开始被界定。在过去十年中,许多关于关键促凋亡和抗凋亡分子的多聚泛素化缀合的报告,已将泛素表征为一种针对蛋白酶体降解的蛋白质的重要调节修饰。然而,最近将单泛素化和非经典多聚泛素化缀合与凋亡分子联系起来的研究,为泛素在凋亡调节中的作用增添了超出降解之外的另一层多样性。本综述重点关注泛素化对凋亡信号分子的直接影响。