Ubiquitination of full-length cyclin.
Ubiquitination of full-length cyclin.
复制标题
全长细胞周期蛋白的泛素化。
DOI：
10.1016/0014-5793(95)00799-f
复制
发表时间：
1995
期刊：
影响因子：
3.5
通讯作者：
Rechsteiner,M
中科院分区：
文献类型：
--
作者：
Mahaffey,DT;Yoo,Y;Rechsteiner,M
有丝分裂细胞周期蛋白是关键的细胞周期调节剂，在细胞周期的大部分时间里相对稳定，然后在有丝分裂时迅速降解。我们检测到全长非洲爪蟾细胞周期蛋白 B2 的泛素缀合物，强烈表明泛素化而不是蛋白水解切割是细胞周期蛋白破坏的起始事件。泛素结合物的最高水平与快速蛋白水解阶段相关。这一结果支持了先前的发现，即泛素系统参与细胞周期蛋白水解。然而，我们还在细胞生长抑制因子停滞和间期提取物中观察到细胞周期蛋白-泛素缀合物，其中细胞周期蛋白更稳定。在这些条件下，泛素化细胞周期蛋白的生理作用是核的。
Mitotic cyclins are key cell-cycle regulators that are relatively stable through most of the cell-cycle then rapidly degraded at mitosis. We have detected ubiquitin conjugates of full-length Xenopus cyclin B2 strongly suggesting that ubiquitination rather than a proteolytic cleavage is the initiating event in cyclin destruction. The highest levels of ubiquitin conjugates correlate with the phase of rapid proteolysis. This result supports previous findings that implicate the ubiquitin system in cyclin proteolysis. However, we also observe cyclin-ubiquitin conjugates in both cytostatic factor arrested and interphase extracts where cyclin is more stable. The physiologic role of ubiquitinated cyclin under these conditions is nuclear.