Dual-specificity phosphatases: an update on their activity regulation and roles in metabolic diseases

IF 2.5 Q2 PHYSIOLOGY
Caroline De Roo, Erin McLean, Ruijie Liu
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引用次数: 0

Abstract

Reversible protein phosphorylation is catalyzed by both protein kinases and phosphatases, affecting cellular signal transduction in physiological and pathological processes. In contrast to protein kinases, the substrates and in vivo function of approximately 200 phosphatases are less characterized. The big family of protein phosphatases consists of serine/threonine phosphatases, tyrosine phosphatases, and dual-specificity phosphatases (DUSPs), which dephosphorylate both serine/threonine, and tyrosine residues within the target proteins. Over the last two decades, progress in the study of DUSPs allows for not only a better understanding of their activation and signaling termination but also the effect of their abnormal expression in the development of various diseases, such as diabetes, cancer, neurodegenerative disorders, and nonalcoholic fatty liver disease. The focus of this minireview is to discuss current understanding of transcriptional and post-translational regulation of DUSPs, as well as their emerging roles in energy metabolism.
双特异性磷酸酶:其活性调控及其在代谢性疾病中的作用的最新进展
可逆蛋白磷酸化是由蛋白激酶和磷酸酶共同催化的,在生理和病理过程中影响细胞信号转导。与蛋白激酶相比,大约200种磷酸酶的底物和体内功能的特征较少。蛋白磷酸酶大家庭由丝氨酸/苏氨酸磷酸酶、酪氨酸磷酸酶和双特异性磷酸酶(DUSPs)组成,DUSPs可以使目标蛋白内的丝氨酸/苏氨酸和酪氨酸残基去磷酸化。在过去的二十年中,dusp研究的进展不仅使我们能够更好地了解它们的激活和信号终止,而且还使我们能够更好地了解它们的异常表达在各种疾病的发展中的作用,如糖尿病、癌症、神经退行性疾病和非酒精性脂肪性肝病。这篇综述的重点是讨论目前对dusp转录和翻译后调控的理解,以及它们在能量代谢中的新作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Current Opinion in Physiology
Current Opinion in Physiology Medicine-Physiology (medical)
CiteScore
5.80
自引率
0.00%
发文量
52
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