期刊
EXPERT REVIEW OF PROTEOMICS
卷 12, 期 3, 页码 295-308出版社
TAYLOR & FRANCIS LTD
DOI: 10.1586/14789450.2015.1039993
关键词
molecular chaperone; protein aggregation; protein folding; protein homeostasis; protein-protein interaction; small heat shock protein; alpha-crystallin
资金
- Deutsche Forschungsgemeinschaft [SFB 1035]
- CIPSM
- Peter und Traudl Engelhorn Stiftung
Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that are implicated in a variety of diseases. Upon stress, they stabilize unfolding proteins and prevent them from aggregating. However, under physiological conditions without severe stress, some sHsps interact with other proteins. In a perspective view, their ability to bind specific client proteins might allow them to fine-tune the availability of the client for other, client-dependent cellular processes. Additionally, some sHsps seem to interact with specific co-chaperones. These co-chaperones are usually part of large protein machineries that are functionally modulated upon sHsps interaction. Finally, secreted human sHsps seem to interact with receptor proteins, potentially as signal molecules transmitting the stress status from one cell to another. This review focuses on the mechanistic description of these different binding modes for human sHsps and how this might help to understand and modulate the function of sHsps in the context of disease.
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