Unfolded protein response signaling in mitochondria.
- Author:
Chun-Wei MA
1
;
Bing-Hong GAO
2
Author Information
1. School of Kinesiology, Shanghai University of Sport, Shanghai 200438, China.
2. School of Physical Education and Sport Training, Shanghai University of Sport, Shanghai 200438, China. gaobinghong@126.com.
- Publication Type:Journal Article
- MeSH:
Mitochondria;
Mitochondrial Proteins/metabolism*;
Oxidative Stress;
Signal Transduction;
Unfolded Protein Response
- From:
Acta Physiologica Sinica
2021;73(5):835-844
- CountryChina
- Language:Chinese
-
Abstract:
The mitochondrial unfolded protein response is an important component of the mitochondrial protein quality control program. It can effectively remove unfolded or misfolded proteins under stress, and maintain a stable and healthy mitochondrial pool. The mitochondrial unfolded protein response is coordinated by multiple signaling pathways. The classical ATF4/ATF5-CHOP pathway is induced by accumulation of unfolded or misfolded proteins in the mitochondrial matrix, which reduces stress toxicity by regulating molecular chaperones and proteases. Sirt3-FOXO3a-SOD2 pathway, located in the mitochondrial matrix, plays an important role in anti-oxidative damage. The ERα-NRF1-HTRA2 pathway mainly removes unfolded proteins in the mitochondrial membrane space and improves the quality control of mitochondrial proteins. These three signaling pathways work both independently and cooperatively to enhance mitochondrial capacity and maintain health under stress.
