Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Nucleus. 2012 Sep-Oct;3(5):429-32. doi: 10.4161/nucl.21980. Epub 2012 Aug 27.
Posttranslational modification of proteins with SUMO and the RanGTP/GDP cycle are two essential cellular mechanisms contributing directly or indirectly to almost every cellular event. The SUMO E3 ligase RanBP2 (Nup358) and the Ran GTPase activating protein (RanGAP1) are known to form a stable complex throughout the cell cycle suggesting a link between sumoylation of proteins and RanGTP hydrolysis. In a recent study we demonstrated that the stable complex of RanBP2, sumoylated RanGAP1 and Ubc9 (and not RanBP2 by itself) represents the physiologically relevant form of the SUMO ligase. Characterization of the interactions reveals an intricate proximity of two catalytic activities, sumoylation and RanGTP hydrolysis. In this ExtraView we summarize our results and discuss some ideas about a potential coupling of both processes.
蛋白质的 SUMO 化和 RanGTP/GDP 循环的翻译后修饰是两种直接或间接参与几乎所有细胞事件的重要细胞机制。SUMO E3 连接酶 RanBP2(Nup358)和 Ran GTPase 激活蛋白(RanGAP1)已知在整个细胞周期中形成稳定的复合物,这表明蛋白质的 SUMO 化和 RanGTP 水解之间存在联系。在最近的一项研究中,我们证明了 RanBP2、SUMO 化的 RanGAP1 和 Ubc9 的稳定复合物(而不是单独的 RanBP2)代表了 SUMO 连接酶的生理相关形式。相互作用的特征揭示了两种催化活性(SUMO 化和 RanGTP 水解)的复杂接近。在这个 ExtraView 中,我们总结了我们的结果,并讨论了两个过程潜在耦合的一些想法。