Lu Albert, Pfeffer Suzanne R
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
Trends Cell Biol. 2014 Jul;24(7):389-99. doi: 10.1016/j.tcb.2014.02.001. Epub 2014 Mar 11.
Mulitmeric cullin-RING ubiquitin ligases (CRLs) represent the largest class of ubiquitin ligases in eukaryotes. However, most CRL ubiquitylation pathways remain uncharacterized. CRLs control a myriad of functions by catalyzing mono- or poly-ubiquitylation of target proteins. Recently, novel CRLs have been identified along the secretory pathway where they modify substrates involved in diverse cellular processes such as vesicle coat assembly and cell cycle progression. This review discusses our current understanding of CRL ubiquitylation within the secretory pathway, with special emphasis on the emerging role of the Golgi as a ubiquitylation platform. CRLs are also implicated in endosome function, where their specific roles are less well understood.
多聚体cullin-RING泛素连接酶(CRLs)是真核生物中最大的一类泛素连接酶。然而,大多数CRL泛素化途径仍未得到充分研究。CRLs通过催化靶蛋白的单泛素化或多泛素化来控制众多功能。最近,在分泌途径中发现了新的CRLs,它们在该途径中修饰参与多种细胞过程(如囊泡包被组装和细胞周期进程)的底物。本文综述了我们目前对分泌途径中CRL泛素化的理解,特别强调了高尔基体作为泛素化平台的新作用。CRLs也与内体功能有关,但其具体作用尚不太清楚。