期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 44, 期 10, 页码 872-884出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2019.04.007
关键词
-
资金
- Azrieli Foundation
- FEBS Fellowship
- TAU startup grant
- Marguerite Stolz Research Fellowship Fund
- Israel Science Foundation [651/16]
- Instruct-ERIC [577, 5260]
Mutant protein aggregation and misfolding is often correlated with toxicity in neurodegenerative diseases. Aggregate-prone proteins are tagged by ubiquitin that signals them for destruction by the proteasome or autophagy, two key pathways for protein degradation and proteostasis. Here, we review recent studies showing that the regulation of aggregate-prone proteins by ubiquitin signaling is more complex than initially postulated. We discuss how the ubiquitin code of aggregate-prone proteins is written by specific E3 ubiquitin ligases and edited by deubiquitylating enzymes (DUBs) in cells and in brain tissues, as well as how this affects protein degradation. These studies have advanced our understanding of the specificity of the ubiquitin system and provide new information about its relevance to neurodegenerative diseases and therapy.
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。
推荐
暂无数据