Regulation and Function of Protein Histidine Phosphorylation
10.16476/j.pibb.2024.0264
- VernacularTitle:蛋白质组氨酸磷酸化修饰的调节及功能作用
- Author:
Xiao-Ran LIU
1
;
Mei-Ning XING
1
;
Wan-Tao YING
1
Author Information
1. Beijing Institute of Lifeomics, State Key Laboratory of Medical Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing 102206, China
- Publication Type:Journal Article
- Keywords:
protein phosphorylation;
histidine kinase;
histidine phosphatase;
histidine phosphorylation
- From:
Progress in Biochemistry and Biophysics
2024;51(10):2694-2704
- CountryChina
- Language:Chinese
-
Abstract:
Protein phosphorylation modification is one of the key regulatory mechanisms in cellular signaling transduction and metabolic processes. The phosphorylation state of target proteins is regulated by specific protein kinases and phosphatases, which add or remove phosphate groups. Histidine phosphorylation (pHis) plays a crucial role in both prokaryotes and eukaryotes life activities and is linked to various pathological processes. Unlike the stable phosphorylation of proteins via phosphate ester bonds, histidine phosphorylation is linked through phosphoramide bonds, making it highly sensitive to high temperatures and low pH. This sensitivity has historically impeded progress in identifying and studying histidine phosphorylation. In recent years, the development of new techniques in phosphoproteomics and the emergence of pHis-specific antibodies have promoted the identification and functional research of pHis-modified substrates. For the first time, more than 700 pHis-modified proteins have been identified in mammalian cells, and pHis-modified substrates such as focal adhesion kinase (FAK) and phosphoglycerate mutase 1 (PGAM1) have been found to promote tumor development. This article mainly reviewed the key mechanisms and functions of histidine kinases and histidine phosphatases in regulating the histidine phosphorylation of specific substrates, and highlights their significant roles in human physiological and pathological processes, aiming to provide guidance for further research into the biological functions of histidine phosphorylation.
