相扑蛋白
磷酸化
翻译后修饰
乙酰化
细胞生物学
蛋白质磷酸化
泛素
生物
化学
生物化学
基因
蛋白激酶A
酶
作者
Qian Nie,Xiang Gong,M. Liu,Di Li
出处
期刊:Current Molecular Medicine
[Bentham Science]
日期:2017-02-01
卷期号:16 (10): 906-913
被引量:16
标识
DOI:10.2174/1566524016666161223105555
摘要
Post-translational modifications (PTMs) such as phosphorylation, acetylation, methylation, ubiquitylation, sumoylation are important mechanisms to regulate functions of different proteins. Among various PTMs, phosphorylation, discovered about 60 years ago, is probably the most common modification. In contrast, sumoylation, identified about two decades ago is emerging as a key regulatory mechanism modulating protein functions. Although studies on protein phosphorylation and sumoylation have been extensively reviewed, much less attention has been paid to their cross-talk and their co-regulation of the same protein target. Here we summarize various examples of the cross-talks between protein phosphorylation and sumoylation, and discuss their functions in regulating normal physiology and pathogenesis. Keywords: PTM, phosphorylation, sumoylation, protein functions.
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