泛素
泛素类
酶
细胞生物学
生物化学
生物
亚细胞定位
信号转导
泛素连接酶
基因
细胞质
作者
Brenda A. Schulman,J. Wade Harper
摘要
The attachment of ubiquitin-like proteins (UBLs) to proteins is a central mechanism of modulation of protein function. Enzymatic, structural and genetic studies have elucidated how mechanistically and structurally related E1 enzymes activate UBLs and selectively direct them to downstream pathways. Attachment of ubiquitin or ubiquitin-like proteins (known as UBLs) to their targets through multienzyme cascades is a central mechanism to modulate protein functions. This process is initiated by a family of mechanistically and structurally related E1 (or activating) enzymes. These activate UBLs through carboxy-terminal adenylation and thiol transfer, and coordinate the use of UBLs in specific downstream pathways by charging cognate E2 (or conjugating) enzymes, which then interact with the downstream ubiquitylation machinery to coordinate the modification of the target. A broad understanding of how E1 enzymes activate UBLs and how they selectively coordinate UBLs with downstream function has come from enzymatic, structural and genetic studies.
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