Zeng Li-Rong, Vega-Sánchez Miguel E, Zhu Tong, Wang Guo-Liang
Department of Plant Pathology and Plant Molecular Biology and Biotechnology Program, The Ohio State University, Columbus, OH 43210, USA.
Cell Res. 2006 May;16(5):413-26. doi: 10.1038/sj.cr.7310053.
Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.
翻译后修饰对于蛋白质稳定性和蛋白质活性的调节至关重要。已经报道了各种类型的蛋白质修饰，如磷酸化、甲基化、乙酰化、肉豆蔻酰化、糖基化和泛素化。其中，泛素化与其他修饰不同，因为大多数泛素化蛋白质会被靶向26S蛋白酶体进行降解。泛素/26S蛋白酶体系统构成了细胞中的主要蛋白质降解途径。近年来，泛素化机制在控制众多真核细胞功能中的重要性越来越受到重视。越来越多的E3泛素连接酶及其底物，包括各种重要的细胞调节因子已被鉴定出来。过去几年的研究表明，泛素化系统对于广泛的植物发育过程以及对非生物和生物胁迫的反应都很重要。本综述讨论了在植物-微生物相互作用中起重要作用的植物和病原体中泛素化相关蛋白功能分析的最新进展。
