The ubiquitin-interacting motifs of S5a as a unique upstream inhibitor of the 26S proteasome

被引：9

作者：

Elangovan, Muthukumar ^{[1
]}

Shin, Dong Yeon ^{[1
]}

Yoo, Yung Joon ^{[1
]}

机构：

[1] GIST, Dept Life Sci, Kwangju 500712, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 388卷 / 04期

关键词：

Proteasome; S5a; Substrate delivery; Ubiquitin-interacting motif (UIM); SUBUNIT; RECEPTOR; SYSTEM; RPN10;

D O I：

10.1016/j.bbrc.2009.08.078

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：

It has been demonstrated that ubiquitin-conjugated proteins were accumulated by ectopically-expressed S5a as well as the ubiquitin-interacting motifs of S5a (S5a-UIMs). In this study, we further found that free S5a-UIMs stabilized only a subset of proteasomal substrates including p53, c-Fos, c-Jun, and p27 but not beta-catenin, p15, and ornithine decarboxylase. Both S5a-UIMs and epoxomicin inhibited the proliferation of A549 lung cancer cells but arrest at the different stages of cell cycle. Together, our results suggest a potential role of S5a-UIMs as an upstream proteasomal inhibitor by blocking the subset of substrates from delivery to the 26S proteasome. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：723 / 726

页数：4

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