A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation

被引：371

作者：

Nobuko Hosokawa ^{[1
]}

Ikuo Wada ^{[2
]}

Kiyotaka Hasegawa ^{[3
]}

Tetuya Yorihuzi ^{[1
]}

Linda O Tremblay ^{[1
]}

Annette Herscovics ^{[2
]}

Kazuhiro Nagata ^{[4
]}

机构：

[1] Department of Molecular and Cellular Biology,

[2] Institute for Frontier Medical Sciences,undefined

[3] Kyoto University,undefined

[4] Core Research for Evolutional Science and Technology,undefined

[5] JST,undefined

[6] Department of Biochemistry,undefined

[7] Sapporo Medical University School of Medicine,undefined

[8] McGill Cancer Centre,undefined

[9] McGill University,undefined

来源：

The EMBO Reports | 2001年 / 2卷 / 5期

关键词：

D O I：

10.1093/embo-reports/kve084

中图分类号：

学科分类号：

摘要：

The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded proteins are retrotranslocated from the ER and degraded by cytoplasmic proteasomes, a mechanism known as ER‐associated degradation (ERAD). We report the cDNA cloning of Edem, a mouse gene encoding a putative type II ER transmembrane protein. Expression of Edem mRNA was induced by various types of ER stress. Although the luminal region of ER degradation enhancing α‐mannosidase‐like protein (EDEM) is similar to class I α1,2‐mannosidases involved in N‐glycan processing, EDEM did not have enzymatic activity. Overexpression of EDEM in human embryonic kidney 293 cells accelerated the degradation of misfolded α1‐antitrypsin, and EDEM bound to this misfolded glycoprotein. The results suggest that EDEM is directly involved in ERAD, and targets misfolded glycoproteins for degradation in an N‐glycan dependent manner.

引用

页码：415 / 422

页数：7

共 93 条

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