泛素码的组装与拆卸。

Ubiquitin code assembly and disassembly.

机构信息

Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.

出版信息

Curr Biol. 2014 Mar 17;24(6):R215-20. doi: 10.1016/j.cub.2014.02.002.

DOI:10.1016/j.cub.2014.02.002

Abstract

Ubiquitin, a 76 amino-acid polypeptide, presents a compact three-dimensional structure, utilising a fold that recurs within larger polypeptides and in other protein modifiers, such as NEDD8 and SUMO. Ubiquitylation was initially recognised as a signal for proteasome-mediated degradation. We shall consider here how this view has evolved to appreciate that the dynamic appendage of different types of ubiquitin chains represents a versatile, three-dimensional code, fundamental to the control of many cellular processes.

摘要

泛素，一种由 76 个氨基酸组成的多肽，呈现出紧凑的三维结构，利用一种在较大多肽和其他蛋白质修饰物（如 NEDD8 和 SUMO）中重复出现的折叠。泛素化最初被认为是蛋白酶体介导降解的信号。在这里，我们将考虑这一观点是如何演变的，以认识到不同类型的泛素链的动态附加代表了一种通用的、三维的密码，对许多细胞过程的控制至关重要。