Proteolysis and the G1-S transition:: the SCF connection
Proteolysis and the G1-S transition:: the SCF connection
复制标题
DOI：
10.1016/s0959-437x(98)80059-2
复制
发表时间：
1998-02-01
影响因子：
4
通讯作者：
Krek, W
中科院分区：
文献类型：
--
作者：
Krek, W
泛素-蛋白酶体介导的蛋白质降解的时间控制对于正常的G（1）和S期进展至关重要。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，指定SCF（Skp 1-cullin-F-box蛋白连接酶复合物），赋予底物特异性的泛素化反应和蛋白激酶的活性，磷酸化底物注定在特定位点的破坏，从而将它们转化为优选的目标，由SCF催化的泛素修饰之间的关系。SCF的组成成分是进化上保守的蛋白质家族的成员。基于SCF的泛素化途径可能在多种生物过程中发挥关键作用，例如细胞增殖、分化和发育。
Temporal control of ubiquitin-proteasome mediated protein degradation is critical for normal G(1) 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.