A journey from phosphotyrosine to phosphohistidine and beyond

被引:36
|
作者
Hunter, Tony [1 ]
机构
[1] Salk Inst Biol Studies, Mol Cell Biol, La Jolla, CA 92037 USA
关键词
NUCLEOSIDE DIPHOSPHATE KINASE; PROTEIN HISTIDINE PHOSPHATASE; NDPK-B; PHOSPHORYLATION; ACTIVATION; ANTIBODIES; TYROSINE; NM23-H1; CELLS; PHOSPHOPROTEOME;
D O I
10.1016/j.molcel.2022.05.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2190 / 2200
页数:11
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