4.6 Review

ERAD substrates: Which way out?

期刊

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
卷 21, 期 5, 页码 526-532

出版社

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2009.12.007

关键词

Endoplasmic reticulum; Protein folding; Protein quality control; ER-associated degradation; Molecular chaperones; Folding enzymes; De-mannosylation; E3 ubiquitin ligases; Dislocons

资金

  1. Foundation for Research on Neurodegenerative Diseases, ONELIFE
  2. Fondazione San Salvatore
  3. Swiss National Center of Competence in Research on Neural Plasticity and Repair
  4. Swiss National Science Foundation
  5. Synapsis Foundation
  6. Bangerter-Rhyner Foundation
  7. US Public Health [GM086874, AI078142]

向作者/读者索取更多资源

Global folding of polypeptides entering the endoplasmic reticulum ( ER) starts as soon as they emerge from the narrow Sec61 translocon. Attainment of the native structure can take from several minutes to hours, depending on the gene product. Until then, non-native folding intermediates must be protected from molecular chaperones that recognize misfolded determinants and could prematurely interrupt folding programs by re-directing them to disposal pathways. On the other hand, futile folding attempts must actively be stopped to prevent intraluminal accumulation of defective cargo. This review describes recent advances in understanding how terminally misfolded polypeptides are extracted from the folding environment and directed to specific dislocons within the ER membrane for transfer to the cytoplasm for proteasome-mediated degradation. (c) 2009 Elsevier Ltd. 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。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据