Protein kinase CK2: a challenge to canons
Protein kinase CK2: a challenge to canons
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DOI：
10.1242/jcs.00074
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发表时间：
2002-10-15
影响因子：
4
通讯作者：
Pinna, LA
中科院分区：
文献类型：
--
作者：
Pinna, LA
CK2是一种非常保守的多效蛋白激酶，有300多种底物，其中大多数是参与信号转导、基因表达和其他核功能的蛋白质。CK2磷受体位点由多个酸性残基指定，相对于目标残基+3位置的位点具有至关重要的相关性。CK2全酶由两个催化亚基（α α, α ' α ‘或α α ’）和两个非催化亚基的二聚体组成，它们对细胞活力至关重要，其确切功能尚不清楚。尽管β亚基深刻影响CK2的许多特性，但分离的催化亚基和全酶都具有组成性活性，这可能是CK2致癌潜力的原因。鉴于全酶的结构，P亚基可以在生理条件下进行可逆解离，并发挥锚定元件和/或作为蛋白质底物和效应物的对接平台的作用。这些不寻常的特征可能有助于CK2参与许多关键的生物学功能，特别是RNA合成，Wnt信号传导，泛素化和细胞存活。
CK2 is an extremely conserved pleiotropic protein kinase with a growing list of more than 300 substrates, the majority of which are proteins implicated in signal transduction, gene expression and other nuclear functions. The CK2 phosphoacceptor sites are specified by multiple acidic residues, with the one at position +3 relative to the target residue being of crucial relevance. The CK2 holoenzyme is composed of two catalytic subunits (alphaalpha, alpha'alpha' or alphaalpha'), which are essential for cell viability, and a dimer of two non-catalytic beta subunits, whose precise function is still poorly understood. Although the beta subunits deeply affect many properties of CK2, both the isolated catalytic subunits and the holoenzyme are constitutively active, which is probably responsible for the oncogenic potential of CK2. Given the structure of the holoenzyme, the P subunits could undergo reversible dissociation under physiological conditions and play a role as anchoring elements and/or as a docking platform for protein substrates and effectors. These unusual features are likely to be instrumental in the involvement of CK2 in a number of key biological functions, notably RNA synthesis, Wnt signaling, ubiquitination and cell survival.