Association of the human SUMO-1 protease SENP2 with the nuclear pore
Association of the human SUMO-1 protease SENP2 with the nuclear pore
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DOI：
10.1074/jbc.m201799200
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发表时间：
2002-05-31
影响因子：
4.8
通讯作者：
Dasso, M
中科院分区：
文献类型：
--
作者：
Hang, J;Dasso, M
SUMO-1是一种小的泛素样蛋白，可以与其他蛋白质共价结合。一个蛋白酶家族催化含SUMO-1的物种的解缀合。该家族的成员也将新合成的SUMO-1加工成其可缀合的形式。为了更好地理解这些酶，我们研究了人SUMO-1蛋白酶SENP 2的定位和行为。在这里，我们已经表明，SENP 2协会与核孔的核面，这种协会需要蛋白质序列附近的N末端SENP 2。我们还表明，SENP 2结合到NUP 153，核孔蛋白，是本地化的核质面的孔。Nup 153结合需要介导其体内靶向的SENP 2的相同结构域。去除SENP 2的Nup 153相互作用区域导致细胞内SUMO-1缀合物谱的显著变化。我们的研究结果表明，与孔的关联在SENP 2的调节中起着重要的负面作用，可能是通过将其活性限制在细胞核内的缀合蛋白的子集上。
SUMO-1 is a small ubiquitin-like protein that can be covalently conjugated to other proteins. A family of proteases catalyzes deconjugation of SUMO-1-containing species. Members of this family also process newly synthesized SUMO-1 into its conjugatable form. To understand these enzymes better, we have examined the localization and behavior of the human SUMO-1 protease SENP2. Here we have shown that SENP2 associates with the nuclear face of nuclear pores and that this association requires protein sequences near the N terminus of SENP2. We have also shown that SENP2 binds to Nup153, a nucleoporin that is localized to the nucleoplasmic face of the pore. Nup153 binding requires the same domain of SENP2 that mediates its targeting in vivo. Removal of the Nup153-interacting region of SENP2 results in a significant change in the spectrum of SUMO-1 conjugates within the cell. Our results suggest that association with the pore plays an important negative role in the regulation of SENP2, perhaps by restricting its activity to a subset of the conjugated proteins within the nucleus.