Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas, N. Plastira 100, Vassilika Vouton, P.O. Box 1385, Heraklion GR 70013, Crete, Greece.
Adv Exp Med Biol. 2010;694:160-71. doi: 10.1007/978-1-4419-7002-2_12.
SUMOylation is a reversible post-translational modification, where a small peptide (SUMO) is covalently attached to a target protein and changes its activity, subcellular localization and/or interaction with other macromolecules. SUMOylation substrates are numerous and diverse and modification by SUMO is involved in many biological functions, including the response to stress. The SUMO pathway has recently been implicated in the process of cellular senescence, the irreversible loss of cell replication potential that occurs during aging in vivo and in vitro. SUMO peptides, a SUMO E3 ligase and a SUMO-specific peptidase can induce or hinder the onset of senescence, thus supporting an association of SUMOylation with cell growth arrest and organismal aging. Preliminary results on comparative analysis ofproteomics and mRNA levels between young and old human and murine tissues show elevated levels of global protein SUMOylation and a decrease in components of the SUMOylation process with age. Further connections between the SUMO pathway and the aging process remain to be elucidated.
SUMOylation 是一种可逆的翻译后修饰,其中一个小肽(SUMO)被共价连接到靶蛋白上,并改变其活性、亚细胞定位和/或与其他大分子的相互作用。SUMOylation 底物数量众多且多样化,SUMO 的修饰参与许多生物学功能,包括对压力的反应。SUMO 途径最近与细胞衰老过程有关,细胞衰老过程是体内和体外衰老过程中细胞复制潜力的不可逆丧失。SUMO 肽、SUMO E3 连接酶和 SUMO 特异性肽酶可以诱导或阻碍衰老的发生,从而支持 SUMOylation 与细胞生长停滞和生物体衰老的关联。对年轻和老年人类和鼠组织的蛋白质组学和 mRNA 水平进行比较分析的初步结果表明,随着年龄的增长,蛋白质 SUMOylation 的总体水平升高,SUMOylation 过程的成分减少。SUMO 途径与衰老过程之间的进一步联系仍有待阐明。