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蛋白激酶CK2是一种真核细胞中普遍存在的信使非依赖性丝/苏氨酸蛋白激酶,可催化细胞内多种蛋白质的磷酸化,由2个催化亚基CK2α或α’以及2个调节亚基CK2β组成的异源四聚体结构。为深入了解CK2的结构与功能,通过运用同源重组敲除、条件性敲除及RNAi引起的基因敲减技术分别对其3个亚基进行敲除与抑制,发现在CK2亚基敲除与抑制后,可对个体生殖、胚胎发育、肿瘤、代谢以及衰老造成重要的影响,说明CK2各亚基具有重要的生物学功能。本文就敲除与敲减蛋白激酶CK2任一亚基后其功能变化的进展作一综述。
Protein kinase CK2, a ubiquitous messenger-independent silk / threonine protein kinase in eukaryotic cells, catalyzes the phosphorylation of multiple proteins in cells and consists of two catalytic subunits, CK2α or α ’, and two regulatory Subunit CK2β heterotetrameric structure. In order to further understand the structure and function of CK2, three subunits were knocked out and inhibited by using homologous recombination knockout, conditional knockout and RNAi-induced gene knockdown respectively. It was found that in CK2 subunit knockout and Inhibition, can have an important impact on individual reproduction, embryonic development, tumor, metabolism and aging, indicating CK2 subunits have important biological functions. This review summarizes the changes in function after knocking out and knocking down any subunit of protein kinase CK2.