Biochemical characterization of cell cycle deubiquitinating enzymes

细胞周期去泛素化酶的生化表征

• 批准号: RGPIN-2015-04372
• 负责人: Meloche, Sylvain
• 金额: $ 2.48万
• 依托单位: Université de Montréal
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2015
• 资助国家: 加拿大
• 起止时间: 2015-01-01 至 2016-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=589754
• 关键词: Biochemical; characterization; cell; cycle; deubiquitinating

Cell proliferation is regulated by a complex network of biochemical reactions that ensure that each cell division step is performed correctly and in proper sequence. Among these reactions is the timed degradation of cellular regulatory proteins by an enzymatic system known as the ubiquitin-proteasome system (UPS). In this system, enzyme complexes named E3 ubiquitin ligases add multiple copies of ubiquitin to a substrate protein, tagging it for rapid degradation by the proteasome. Another family of enzymes identified as deubiquitinating enzymes (DUBs) remove ubiquitin from substrate proteins, opposing the action of E3 ligases. The balance in the activities of E3 ligases and DUBs determine the stability of substrate proteins and plays a key role in the regulation of the cell division cycle. Deregulation of this balance leads to uncontrolled cell proliferation and genetic instability.

细胞增殖由一个复杂的生化反应网络来调节，以确保每个细胞分裂步骤都以正确和正确的顺序进行。在这些反应中，有一种被称为泛素-蛋白酶体系统(UPS)的酶系统对细胞调节蛋白的定时降解。在这个系统中，名为E3泛素连接酶的酶复合体将多个拷贝的泛素添加到底物蛋白上，标记它以供蛋白酶体快速降解。另一类酶被鉴定为去泛素酶(DUBS)，它从底物蛋白中去除泛素，与E3连接酶的作用相反。E3连接酶和DUBS活性的平衡决定了底物蛋白的稳定性，在细胞分裂周期的调控中起着关键作用。这种平衡的放松会导致不受控制的细胞增殖和遗传不稳定。