Research progress in PRAS40.
10.11817/j.issn.1672-7347.2018.06.017
- Author:
Gang CHEN
1
;
Gangcai ZHU
1
;
Xin ZHANG
1
Author Information
1. Department of Otorhinolaryngology Head and Neck Surgery, Second Xiangya Hospital, Central South University, Changsha 410011, China.
- Publication Type:Journal Article
- MeSH:
Adaptor Proteins, Signal Transducing;
metabolism;
Humans;
Mechanistic Target of Rapamycin Complex 1;
metabolism;
Phosphorylation;
Proto-Oncogene Proteins c-akt;
metabolism;
TOR Serine-Threonine Kinases;
metabolism
- From:
Journal of Central South University(Medical Sciences)
2018;43(6):685-690
- CountryChina
- Language:Chinese
-
Abstract:
Prolin-rich Akt substrate of 40 kD (PRAS40) is firstly identified as a partner of 14-3-3 protein and a substrate of Akt kinase by Roth et al in 2003. Accumulated evidence shows that PRAS40 is mainly activated by phosphorylate modification at different sites. PRAS40 may be involved in various of signaling pathways, such as mammalian target of rapamycin complex 1 (mTORC1), protein kinase B (Akt), NF-κB and ribosomal protein L11 (RPL11) etc, which can regulate cell proliferation, senescence, autophagy, apoptosis and exosome secretion.
