Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Cell Mol Biol Lett. 2021 Jan 5;26(1):1. doi: 10.1186/s11658-020-00245-6.
Protein ubiquitination has become one of the most extensively studied post-translational modifications. Originally discovered as a critical element in highly regulated proteolysis, ubiquitination is now regarded as essential for many other cellular processes. This results from the unique features of ubiquitin (Ub) and its ability to form various homo- and heterotypic linkage types involving one of the seven different lysine residues or the free amino group located at its N-terminus. While K48- and K63-linked chains are broadly covered in the literature, the other types of chains assembled through K6, K11, K27, K29, and K33 residues deserve equal attention in the light of the latest discoveries. Here, we provide a concise summary of recent advances in the field of these poorly understood Ub linkages and their possible roles in vivo.
蛋白质泛素化已成为研究最广泛的翻译后修饰之一。最初作为高度调控的蛋白水解的关键因素被发现，泛素化现在被认为对许多其他细胞过程至关重要。这是由于泛素 (Ub) 的独特特征及其形成各种同种型和异型连接类型的能力，涉及七个不同赖氨酸残基之一或位于其 N 末端的游离氨基。虽然 K48-和 K63 连接链在文献中广泛报道，但通过 K6、K11、K27、K29 和 K33 残基组装的其他类型的链在最新发现的情况下也应得到同等重视。在这里，我们简要总结了该领域这些了解甚少的 Ub 连接及其在体内可能作用的最新进展。
