New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation

被引：184

作者：

Qi, Ling ^{[1
,2
]}

Tsai, Billy ^{[3
]}

Arvan, Peter ^{[1
,2
]}

机构：

[1] Univ Michigan, Med Sch, Dept Mol & Integrat Physiol, Ann Arbor, MI 48105 USA

[2] Univ Michigan, Med Sch, Div Metab Endocrinol & Diabet, Ann Arbor, MI 48105 USA

[3] Univ Michigan, Med Sch, Dept Cell & Dev Biol, Ann Arbor, MI 48105 USA

来源：

TRENDS IN CELL BIOLOGY | 2017年 / 27卷 / 06期

关键词：

ER-ASSOCIATED DEGRADATION; UNFOLDED PROTEIN RESPONSE; UBIQUITIN LIGASE COMPLEX; INNER NUCLEAR-MEMBRANE; QUALITY-CONTROL; MISFOLDED GLYCOPROTEINS; TRANSMEMBRANE PROTEIN; EMBRYONIC LETHALITY; SEL1L PROTEIN; E3; LIGASE;

D O I：

10.1016/j.tcb.2016.12.002

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Many human diseases are associated with mutations causing protein misfolding and aggregation in the endoplasmic reticulum (ER). ER-associated degradation (ERAD) is a principal quality-control mechanism responsible for targeting misfolded ER proteins for cytosolic degradation. However, despite years of effort, the physiological role of ERAD in vivo remains largely unknown. Several recent studies have reported intriguing phenotypes of mice deficient for ERAD function in specific cell types. These studies highlight that mammalian ERAD has been designed to perform a wide-range of cell-type-specific functions in vivo in a substrate-dependent manner.

引用

页码：430 / 440

页数：11

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