Ku70 is stabilized by increased cellular SUMO.
Ku70 is stabilized by increased cellular SUMO.
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DOI：
10.1016/j.bbrc.2007.11.136
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发表时间：
2008-02
影响因子：
3.1
通讯作者：
V. Yurchenko;Zhuping Xue;V. Gama;S. Matsuyama;M. Sadofsky
中科院分区：
文献类型：
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作者：
V. Yurchenko;Zhuping Xue;V. Gama;S. Matsuyama;M. Sadofsky
Ku70是一种蛋白质，在几个重要的细胞过程中处于核心位置。作为DNA-末端结合复合体的一部分，它是非同源末端连接途径中必不可少的，是端粒正常维持所必需的，并有助于DNA损伤识别和细胞凋亡的调节。因此，调节Ku70的力量可能对细胞的生理状态有很大的影响。我们在这里报道，小蛋白SUMO的短暂表达导致Ku70丰度的惊人增加。令人惊讶的是，Ku70的直接SUMOylation似乎并不需要这种效果。相反，Ku70似乎是通过对降解速率的间接影响而稳定下来的。通过提高促进SUMOylation的酶的表达，也获得了相同的结果。很可能许多其他蛋白质也会受到类似的调节，从而提供对细胞状态的一般控制。
Ku70 is a protein that finds itself at the heart of several important cellular processes. It is essential to the non-homologous end joining pathway as a part of the DNA-end binding complex, required for proper maintenance of telomeres and contributes to the DNA damage recognition and regulation of apoptosis. Forces that regulate Ku70 are therefore likely to have large consequences on the physiologic state of the cell. We report here that transient expression of the small protein SUMO resulted in a surprising increase in the abundance of Ku70. Surprisingly, the direct SUMOylation of Ku70 does not appear to be required for this effect. Rather, Ku70 appears to be stabilized through indirect effects on the rate of degradation. The same outcome was obtained by raising the expression of enzymes that promote SUMOylation. It is likely that many other proteins will be similarly regulated, providing a general control of cellular state.