Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
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DOI：
10.1016/j.febslet.2004.06.077
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发表时间：
2004-07-30
期刊：
影响因子：
3.5
通讯作者：
Nukina, N
中科院分区：
文献类型：
--
作者：
Doi, H;Mitsui, K;Nukina, N
通过连续提取核可溶性蛋白，从ecdysine诱导的突变株neuro2A细胞中纯化出含有150重复谷氨酰胺残基的增强型绿色荧光蛋白和核定位信号融合的截断n端亨廷顿蛋白的核聚集体。为了分析聚集体相互作用的蛋白质，我们对核聚集体进行了高效液相色谱-质谱分析。结果数据显示存在三种新的推定聚集相互作用蛋白：泛素1，泛素2和Tollip。在亨廷顿病（HD）小鼠模型中，这些蛋白也与神经元核内包涵体相关。这些与聚集体相互作用的蛋白质含有泛素相互作用的基序，这表明它们被聚集到聚集体中，在那里它们可能失去正常的功能。(C) 2004年欧洲生化学会联合会。Elsevier B.V.版权所有。
Nuclear aggregates of enhanced green fluorescent protein and nuclear localization signal-fused truncated N-terminal huntingtin containing 150 repeats of glutamine residue were purified from ecdysine-inducible mutant neuro2A cell line by sequential extraction of nuclear soluble proteins. To analyze the aggregate-interacting proteins, we subjected the nuclear aggregates to high performance liquid chromatography-mass spectrometry analysis. The resulting data revealed the presence of three new putative aggregate-interacting proteins: ubiquilin 1, ubiquilin 2 and Tollip. These proteins also associated with neuronal intranuclear inclusions in a mouse model of Huntington disease (HD). These aggregate-interacting proteins contain ubiquitin-interacting motifs, suggesting that they are recruited to the aggregates where they may lose their normal function. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.