Krek W
Friedrich Miescher Institut, Basel, Switzerland.
Curr Opin Genet Dev. 1998 Feb;8(1):36-42. doi: 10.1016/s0959-437x(98)80059-2.
Temporal control of ubiquitin-proteasome mediated protein degradation is critical for normal G1 and S phase progression. Recent work has shown that central to the temporal control mechanism is a relationship between newly identified E3 ubiquitin protein ligases, designated SCFs (Skp1-cullin-F-box protein ligase complexes), which confer substrate specificity on ubiquitination reactions and the activities of protein kinases that phosphorylate substrates destined for destruction at specific sites, thereby converting them into preferred targets for ubiquitin modification catalyzed by SCFs. The constituents of SCFs are members of evolutionary conserved protein families. SCF-based ubiquitination pathways may play a key role in diverse biological processes, such as cell proliferation, differentiation and development.
泛素 - 蛋白酶体介导的蛋白质降解的时间控制对于正常的G1期和S期进程至关重要。最近的研究表明，时间控制机制的核心是新发现的E3泛素蛋白连接酶（称为SCF，即Skp1 - cullin - F - box蛋白连接酶复合物）之间的关系，它赋予泛素化反应底物特异性，以及蛋白激酶的活性，这些蛋白激酶可磷酸化特定位点上注定要被破坏的底物，从而将它们转化为SCF催化的泛素修饰的优先靶标。SCF的成分是进化保守蛋白家族的成员。基于SCF的泛素化途径可能在多种生物学过程中起关键作用，如细胞增殖、分化和发育。
