The nucleoporin RanBP2 has SUMO1 E3 ligase activity
The nucleoporin RanBP2 has SUMO1 E3 ligase activity
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DOI：
10.1016/s0092-8674(01)00633-x
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发表时间：
2002-01-11
期刊：
影响因子：
64.5
通讯作者：
Melchior, F
中科院分区：
文献类型：
--
作者：
Pichler, A;Gast, A;Melchior, F
SUMO 1的翻译后修饰调节蛋白质/蛋白质相互作用、定位和稳定性。SUMO化需要E1酶Aos 1/Uba 2和E2酶Ubc 9。皮亚斯蛋白是近年来发现的一类E3样因子。在这里，我们表明核孔蛋白RanBP 2/Nup 358也具有SUMO 1 E3样活性。RanBP 2直接与E2酶Ubc 9相互作用，并强烈增强SUMO 1从Ubc 9转移到SUMO 1靶标Sp100。E3样活性包含在RanBP 2的33 kDa结构域内，该结构域缺乏RING指基序并且不类似于皮亚斯家族蛋白。我们的研究结果将SUMO化定位在NPC的细胞质细丝上，并表明至少对于某些底物，修饰和核输入是相关的事件。
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events.