A regulatory link between ER-associated protein degradation and the unfolded-protein response.

被引：385

作者：

Friedlander, R ^{[1
]}

Jarosch, E ^{[1
]}

Urban, J ^{[1
]}

Volkwein, C ^{[1
]}

Sommer, T ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany

来源：

NATURE CELL BIOLOGY | 2000年 / 2卷 / 07期

关键词：

D O I：

10.1038/35017001

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Ubiquitin conjugation during endoplasmic-reticulum-associated degradation (ERAD) depends on the activity of Ubc7. Here we show that Ubc1 acts as a further ubiquitin-conjugating enzyme in this pathway. Absence of both enzymes results in marked stabilization of an ERAD substrate and induction of the unfolded-protein response (UPR). Furthermore, basic ERAD activity is sufficient to eliminate unfolded proteins under normal conditions. However, when stress is applied, the UPR is required to increase ERAD activity. We thus demonstrate, for the first time, st regulatory loop between ERAD and the UPR, which is essential for normal growth of yeast cells.

引用

页码：379 / 384

页数：6

共 30 条

[1]

Ausubel FA, 1995, CURRENT PROTOCOLS MO

[2] Role of Cue1p in ubiquitination and degradation at the ER surface [J].