Caspase-8 sumoylation is associated with nuclear localization
Caspase-8 sumoylation is associated with nuclear localization
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DOI：
10.1038/sj.onc.1208448
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发表时间：
2005-05-05
期刊：
影响因子：
8
通讯作者：
Vazquez, A
中科院分区：
文献类型：
--
作者：
Besnault-Mascard, L;Leprince, C;Vazquez, A
半胱氨酸蛋白酶caspase-8在不同凋亡途径的启动中起关键作用，并控制各种细胞类型（包括神经元、成纤维细胞和淋巴细胞）的成熟和分化。caspase-8的特异性底物存在于细胞质和细胞核中，这可能决定caspase-8的最终生物学效应。然而，caspase-8的细胞定位的调节机制仍然是未知的。我们在这里表明，与其他半胱天冬酶如半胱天冬酶-9和-3相反，半胱天冬酶-8可以在赖氨酸156处被sumoylated。这种类小泛素化（i）与caspase-8的核定位有关，（ii）不损害caspase-8的活化。
The cysteine protease caspase-8 plays a pivotal role in the initiation of different apoptotic pathways and controls the maturation and differentiation of various cell types including neurons, fibroblasts and lymphocytes. Specific substrates of caspase-8 are present in both the cytoplasm and the nucleus, which may determine the ultimate biological effect of caspase-8. However, the mechanisms regulating the cellular localization of caspase-8 are still unknown. We show here that, in contrast to other caspases such as caspase-9 and -3, caspase-8 can be sumoylated at lysine 156. This sumoylation (i) is associated with the nuclear localization of caspase-8 and (ii) did not impair caspase-8 activation.