Signaling through monoubiquitination.
Signaling through monoubiquitination.
复制标题
DOI：
10.1007/978-3-540-69494-6_6
复制
发表时间：
2004
影响因子：
--
通讯作者：
S. Sigismund;Simona Polo;P. P. D. Fiore-P.;P. P. D. Fiore-P.
中科院分区：
文献类型：
--
作者：
S. Sigismund;Simona Polo;P. P. D. Fiore-P.;P. P. D. Fiore-P.
泛素化是一种翻译后修饰，其中一个小的保守肽（泛素）通过一系列复杂的酶促反应被附加到细胞中的靶蛋白上。最近，一种特殊形式的泛素化，即单泛素化，作为一种控制蛋白质功能的非蛋白水解可逆修饰而出现。在这篇综述中，我们重点介绍了单泛素化作为一种信号诱导修饰的最新发现，该修饰受源自活性受体酪氨酸激酶的途径等控制。此外，我们回顾了泛素修饰控制的主要细胞过程，包括膜运输、组蛋白功能、转录调控、DNA 修复和 DNA 复制。
Ubiquitination is a post-translational modification in which a small conserved peptide, ubiquitin, is appended to target proteins in the cell, through a series of complex enzymatic reactions. Recently, a particular form of ubiquitination, monoubiquitination, has emerged as a nonproteolytic reversible modification that controls protein function. In this review, we highlight recent findings on monoubiquitination as a signaling-induced modification, controlled, among others, by pathways originating from active receptor tyrosine kinases. Furthermore, we review the major cellular processes controlled by ubiquitin modification, including membrane trafficking, histone function, transcription regulation, DNA repair, and DNA replication.