Max F. Perutz Laboratories, Department of Biochemistry and Cell Biology, Center for Molecular Biology, University of Vienna Vienna, Austria.
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences Vienna, Austria.
Front Plant Sci. 2014 Jan 31;5:15. doi: 10.3389/fpls.2014.00015. eCollection 2014.
Covalent attachment of the small modifier ubiquitin to Lys ε-amino groups of proteins is surprisingly diverse. Once attached to a substrate, ubiquitin is itself frequently modified by ubiquitin, to form chains. All seven Lys residues of ubiquitin, as well as its N-terminal Met, can be ubiquitylated, implying cellular occurrence of different ubiquitin chain types. The available data suggest that the synthesis, recognition, and hydrolysis of different chain types are precisely regulated. This remarkable extent of control underlies a versatile cellular response to substrate ubiquitylation. In this review, we focus on roles of Lys63-linked ubiquitin chains in plants. Despite limited available knowledge, several recent findings illustrate the importance of these chains as signaling components in plants.
蛋白质赖氨酸 ε-氨基共价连接小修饰物泛素的方式出乎意料地多样。一旦连接到底物上，泛素本身就经常被泛素修饰，形成链。泛素的七个赖氨酸残基以及其 N 端甲硫氨酸都可以被泛素化，这意味着细胞中存在不同的泛素链类型。现有数据表明，不同链类型的合成、识别和水解受到精确调控。这种显著的控制程度为细胞对底物泛素化的灵活反应提供了基础。在这篇综述中，我们重点关注赖氨酸 63 连接的泛素链在植物中的作用。尽管可用知识有限，但最近的一些发现表明这些链作为植物中的信号成分的重要性。
