Patton E E, Willems A R, Tyers M
Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Canada.
Trends Genet. 1998 Jun;14(6):236-43. doi: 10.1016/s0168-9525(98)01473-5.
The ubiquitin-dependent proteolytic pathway targets many key regulatory proteins for rapid intracellular degradation. Specificity in protein ubiquitination derives from E3 ubiquitin protein ligases, which recognize substrate proteins. Recently, analysis of the E3s that regulate cell division has revealed common themes in structure and function. One particularly versatile class of E3s, referred to as Skp1p-Cdc53p-F-box protein (SCF) complexes, utilizes substrate-specific adaptor subunits called F-box proteins to recruit various substrates to a core ubiquitination complex. A vast array of F-box proteins have been revealed by genome sequencing projects, and the early returns from genetic analysis in several organisms promise that F-box proteins will participate in the regulation of many processes, including cell division, transcription, signal transduction and development.
泛素依赖性蛋白水解途径靶向许多关键调节蛋白，使其在细胞内快速降解。蛋白质泛素化的特异性源于E3泛素蛋白连接酶，其可识别底物蛋白。最近，对调节细胞分裂的E3连接酶的分析揭示了其结构和功能的共同特点。一类特别通用的E3连接酶，称为Skp1p-Cdc53p-F盒蛋白（SCF）复合物，利用称为F盒蛋白的底物特异性衔接子亚基，将各种底物招募到核心泛素化复合物中。基因组测序项目已揭示了大量的F盒蛋白，并且来自几种生物体的遗传分析的早期结果表明，F盒蛋白将参与包括细胞分裂、转录、信号转导和发育在内的许多过程的调节。
