Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

被引：144

作者：

Ko, HS ^{[1
]}

Uehara, T ^{[1
]}

Tsuruma, K ^{[1
]}

Nomura, Y ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Pharmacol, Sapporo, Hokkaido 0600812, Japan

来源：

FEBS LETTERS | 2004年 / 566卷 / 1-3期

关键词：

protein-disulfide isomerase; ubiquilin; endoplasmic reticulum; up-regulation; ubiquitin-proteasome; system; protein degradation;

D O I：

10.1016/j.febslet.2004.04.031

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：110 / 114

页数：5

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