Kerscher Oliver
Biology Department, Millington Hall, Room 328, Landrum Drive, College of William and Mary, Williamsburg, Virginia 23185, USA.
EMBO Rep. 2007 Jun;8(6):550-5. doi: 10.1038/sj.embor.7400980.
The small ubiquitin-like modifier, SUMO, can be covalently linked to specific proteins and many substrates carrying this modification have been identified. However, for some proteins, the role that SUMO modification imparts remains obscure. Our understanding of SUMO biology and function has been significantly advanced by the recent discovery of proteins and protein domains that contain SUMO-interacting motifs (SIMs), which interact non-covalently with SUMO. Unlike the motifs and domains that mediate ubiquitin binding, the diversity of SIMs seems limited. Nevertheless, SIMs have already increased our understanding of how SUMO affects DNA repair, transcriptional activation, nuclear body formation and protein turnover. This review takes a detailed look at how SIMs were identified, how they specifically bind to SUMO, their crucial roles in multi-step enzymatic processes, and how they direct the assembly and disassembly of dimeric and multimeric protein complexes.
小泛素样修饰物(SUMO)能够与特定蛋白质共价连接,并且许多带有这种修饰的底物已被鉴定出来。然而,对于一些蛋白质而言,SUMO修饰所赋予的作用仍不清楚。最近发现了含有SUMO相互作用基序(SIM)的蛋白质和蛋白质结构域,它们与SUMO非共价相互作用,这极大地推动了我们对SUMO生物学和功能的理解。与介导泛素结合的基序和结构域不同,SIM的多样性似乎有限。尽管如此,SIM已经增进了我们对SUMO如何影响DNA修复、转录激活、核体形成和蛋白质周转的理解。本综述详细探讨了SIM是如何被鉴定出来的、它们如何特异性结合SUMO、它们在多步酶促过程中的关键作用,以及它们如何指导二聚体和多聚体蛋白质复合物的组装和解聚。