A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1

被引：99

作者：

Nadav, E ^{[1
]}

Shmueli, A

Barr, H

Gonen, H

Ciechanover, A

Reiss, Y

机构：

[1] Tel Aviv Univ, George S Wise Fac Life Sci, Dept Biochem, IL-69978 Tel Aviv, Israel

[2] Technion Israel Inst Technol, Dept Biochem, IL-31096 Haifa, Israel

[3] Technion Israel Inst Technol, Bruce Rappaport Fac Med, Rappaport Family Inst Res Med Sci, IL-31096 Haifa, Israel

[4] Proteol Ltd, IL-76124 Rehovot, Israel

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 303卷 / 01期

关键词：

ubiquitin-protein ligase; endoplasmic reticulum-associated degradation; HMG-CoA reductase; cystic fibrosis transmembrane conductance regulator; hHrd1;

D O I：

10.1016/S0006-291X(03)00279-1

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：

The yeast hHrd1 is a ubiquitin-protein ligase (E3) involved in ER-associated degradation. It was originally identified by genetic methods as an E3 of the yeast cholesterol biosynthetic enzyme HMG-CoA reductase (HMGR). We report the identification and cloning of a human homologue of Hrd1 (hHrd1). Immunofluorescence imaging confirms that the endogenous hHrd1 resides in the ER and in vitro assay demonstrates that it has a ubiquitin-ligase activity. However, the homology between the human and yeast Hrd1 is limited to the N-terminal domain of the proteins, and hHrd1 does not appear to be involved in the degradation of mammalian HMGR. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：91 / 97

页数：7

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