Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains
Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains
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DOI：
10.1016/j.febslet.2004.04.031
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发表时间：
2004-05-21
期刊：
影响因子：
3.5
通讯作者：
Nomura, Y
中科院分区：
文献类型：
--
作者：
Ko, HS;Uehara, T;Nomura, Y
哺乳动物细胞通过高水平表达应激相关基因获得对多种应激源的耐受性。我们之前已经证明，蛋白二硫异构酶（PDI）和泛素在缺氧/脑缺血反应中上调，并在抵抗这些损伤中发挥关键作用。我们在这里表明泛素优先与多泛素链和19S蛋白酶体亚基相互作用。综上所述，这些结果表明泛素可以作为一种衔接蛋白，既可以与PDI相互作用，又可以介导多泛素化蛋白向内质网膜附近细胞质溶胶中的蛋白酶体的传递。(C) 2004年欧洲生化学会联合会。Elsevier B.V.版权所有。
Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.