Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes.
Histidine kinases and the missing phosphoproteome from prokaryotes to eukaryotes.
复制标题
DOI：
10.1038/labinvest.2017.118
复制
发表时间：
2018-03
期刊：
影响因子：
--
通讯作者：
Hunter T
中科院分区：
文献类型：
--
作者：
Adam K;Hunter T
蛋白质磷酸化是真核生物中最常见的翻译后修饰类型。磷酸化蛋白质组被定义为在各种条件下存在于细胞蛋白质组中的实验可检测的磷酸化位点的完整集合。然而，我们仍然远未鉴定细胞中的所有磷酸化位点，这主要是由于缺乏关于涉及除Ser、Thr和Tyr之外的残基的磷酸化事件的信息。存在四种类型的磷酸-蛋白质键，它们产生九种不同的磷酸残基- pSer、pThr、pTyr、pHis、pLys、pArg、pAsp、pGlu和pCys。蛋白质磷酸化的研究主要集中在Ser、Thr和Tyr的磷酸化上。最近开发的1-和3-pHis单克隆抗体有望增加我们对His磷酸化和所涉及的激酶和磷酸酶的理解。几种His激酶在原核生物中被很好地定义，特别是参与双组分系统（TCS）信号传导的那些。然而，在高等真核生物中，最初被表征为核苷二磷酸激酶的蛋白质NM 23是唯一被表征的蛋白质-组氨酸激酶。这种普遍存在且保守的His激酶使其活性位点His自磷酸化，并将这种磷酸转移到核苷二磷酸或蛋白质His残基上。使用新开发的抗pHis抗体对NM 23蛋白靶点的研究必将有助于阐明难以捉摸的基于His磷酸化的信号通路。本文综述了NM 23/NME/NDPK磷酸转移酶所起的作用，以及pHis磷酸化蛋白质组的加入如何扩大磷酸化蛋白质组，使His磷酸化成为全球磷酸化世界的一部分。它还总结了为什么我们对磷酸化的理解在很大程度上仍然局限于酸稳定磷酸化蛋白质组，并强调了作为组氨酸磷酸化世界入口的NM 23组氨酸激酶的研究。
Protein phosphorylation is the most common type of post-translational modification in eukaryotes. The phosphoproteome is defined as the complete set of experimentally detectable phosphorylation sites present in a cell’s proteome under various conditions. However, we are still far from identifying all the phosphorylation sites in a cell mainly due to the lack of information about phosphorylation events involving residues other than Ser, Thr and Tyr. Four types of phosphate-protein linkage exist and these generate nine different phosphoresidues – pSer, pThr, pTyr, pHis, pLys, pArg, pAsp, pGlu, and pCys. Most of the effort in studying protein phosphorylation has been focused on Ser, Thr and Tyr phosphorylation. The recent development of 1- and 3-pHis monoclonal antibodies promises to increase our understanding of His phosphorylation and the kinases and phosphatases involved. Several His kinases are well defined in prokaryotes, especially those involved in Two-Component System (TCS) signaling. However in higher eukaryotes, NM23, a protein originally characterized as a nucleoside diphosphate kinase, is the only characterized protein-histidine kinase. This ubiquitous and conserved His kinase autophosphorylates its active site His, and transfers this phosphate either onto a nucleoside diphosphate or onto a protein His residue. Studies of NM23 protein targets using newly developed anti-pHis antibodies will surely help illuminate the elusive His phosphorylation-based signaling pathways. This review discusses the role that the NM23/NME/NDPK phosphotransferase plays, how the addition of the pHis phosphoproteome will expand the phosphoproteome, and make His phosphorylation part of the global phosphorylation world. It also summarizes why our understanding of phosphorylation is still largely restricted to the acid stable phosphoproteome, and highlights the study of NM23 histidine kinase as an entrée into the world of histidine phosphorylation.
登录
查看更多内容
DOI：
10.1073/pnas.0401031101
发表时间：
2004-04-27
影响因子：
11.1
作者：
Bennett, SE;Chen, CY;Mosbaugh, DW
通讯作者：
Mosbaugh, DW
DOI：
10.1111/j.1432-1033.1995.200_c.x
发表时间：
1995-11-15
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
ENGEL, M;VERON, M;WELTER, C
通讯作者：
WELTER, C
影响因子：
4.8
作者：
Cuello, F;Schulze, RA;Wieland, T
通讯作者：
Wieland, T
影响因子：
4.8
作者：
Cho, Ha Yeon;Cho, Hyo Je;Kang, Beom Sik
通讯作者：
Kang, Beom Sik
影响因子：
64.5
作者：
BIGGS, J;HERSPERGER, E;SHEARN, A
通讯作者：
SHEARN, A