期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 379, 期 2, 页码 583-588出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2008.12.110
关键词
Selenium; Selenium binding protein; pVHL interacting deubiquitinating enzyme; Yeast two hybrid; Prostate cancer
资金
- DOD [W81XWH-07-1-0321]
- [DAMD17-03-1-0173]
- [DAMD17-02-1-0014]
- [DAMD17-03-10233]
Reduced expression of the 56-kDa human selenium binding protein-1 (hSP56) has been reported in many types of human malignancies, including prostate, lung, ovarian, thyroid and colorectal cancers. hSP56 also has been implicated in selenium-dependent cell growth inhibition. However, the molecular basis of hSP56's function has not been elucidated. In the present Study, we identified von Hippel-Lindau protein (pVHL)-interacting deubiquitinating enzyme 1 (VDU1) as a protein partner of hSP56 using a yeast two hybrid screen. The interaction between hSP56 and VDU1 was confirmed by yeast two-hybrid screen and in vitro binding experiments. hSP56 and VDU1 co-localized in the perinuclear region of LNCaP human prostate cancer cells. The full-length VDU1 specifically interacted with a selenium-replete form of hsp56 We also demonstrate stable incorporation of selenium into hSP56, in a mode distinct from conventional selenocysteine-containing selenoproteins. These findings Suggest that hSP56 may play a role in ubiqui nation/deubiquitination-mediated protein degradation pathways in a selenium-dependent manner. (C) 2009 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据