Enhanced SUMOylation in polyglutamine diseases
Enhanced SUMOylation in polyglutamine diseases
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DOI：
10.1016/s0006-291x(02)00211-5
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发表时间：
2002-04-26
影响因子：
3.1
通讯作者：
Okazawa, H
中科院分区：
文献类型：
--
作者：
Ueda, H;Goto, J;Okazawa, H
小泛素样修饰物（SUMO）是与泛素同源的蛋白质，可能调节核内蛋白质定位、核转运和泛素化。我们检查了DRPLA患者。SCA 1、MJD和亨廷顿氏病，并发现大脑受影响区域的神经元对SUMO-1（SUMO家族成员）反应强烈。用表达突变型ataxin-1的转基因小鼠进行Western印迹，显示小脑皮质SUMO化蛋白增加。这些结果表明SUMO-1系统在多聚谷氨酰胺疾病中激活，并预测其参与病理过程。(C)2002 Elsevier Science（美国）。All rights reserved.
Small ubiquitin-like modifiers (SUMOs) are proteins homologous to ubiquitin that possibly regulate intranuclear protein localization, nuclear transport, and ubiquitination. We examined patients of DRPLA. SCA1, MJD, and Huntington's disease and found that neurons in affected regions of the brain react strongly to SUMO-1, a family member of SUMOs. Western blot with a transgenic mouse expressing mutant ataxin-1 showed the increase of SUMOylated proteins in the cerebellar cortex. which we named ESCA1 and ESCA2, These results indicated activation of SUMO-1 system in polyglutamine diseases and predicted its involvement in the pathology. (C) 2002 Elsevier Science (USA). All rights reserved.