期刊
MOLECULAR CELL
卷 82, 期 12, 页码 2190-2200出版社
CELL PRESS
DOI: 10.1016/j.molcel.2022.05.007
关键词
-
资金
- NCI Outstanding Investigator Award [CA242443]
- Renato Dulbecco Chair in Cancer Research
Protein phosphorylation is a reversible post-translational modification involving various natural amino acids. While serine, threonine, and tyrosine phosphorylation have been extensively studied, less is known about non-canonical phosphorylations such as histidine phosphorylation. Recent advances in research tools have accelerated our understanding of the multifaceted functions of histidine phosphorylation in cellular processes.
Protein phosphorylation is a reversible post-translational modification. Nine of the 20 natural amino acids in proteins can be phosphorylated, but most of what we know about the roles of protein phosphorylation has come from studies of serine, threonine, and tyrosine phosphorylation. Much less is understood about the phosphorylation of histidine, lysine, arginine, cysteine, aspartate, and glutamate, so-called non-canonical phosphorylations. Phosphohistidine (pHis) was discovered 60 years ago as a mitochondrial enzyme intermediate; since then, evidence for the existence of histidine kinases and phosphohistidine phosphatases has emerged, together with examples where protein function is regulated by reversible histidine phosphorylation. pHis is chemically unstable and has thus been challenging to study. However, the recent development of tools for studying pHis has accelerated our understanding of the multifaceted functions of histidine phosphorylation, revealing a large number of proteins that are phosphorylated on histidine and implicating pHis in a wide range of cellular processes.
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