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Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability.

Abstract：

:Mitogen-activated protein kinases (MAPKs) are key regulators of signal transduction and cell responses. Abnormalities in MAPKs are associated with multiple diseases. Dual-specificity phosphatases (DUSPs) dephosphorylate many key signaling molecules, including MAPKs, leading to the regulation of duration, magnitude, or spatiotemporal profiles of MAPK activities. Hence, DUSPs need to be properly controlled. Protein post-translational modifications, such as ubiquitination, phosphorylation, methylation, and acetylation, play important roles in the regulation of protein stability and activity. Ubiquitination is critical for controlling protein degradation, activation, and interaction. For DUSPs, ubiquitination induces degradation of eight DUSPs, namely, DUSP1, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, and DUSP16. In addition, protein stability of DUSP2 and DUSP10 is enhanced by phosphorylation. Methylation-induced ubiquitination of DUSP14 stimulates its phosphatase activity. In this review, we summarize the knowledge of the regulation of DUSP stability and ubiquitination through post-translational modifications.

journal_name

Int J Mol Sci

journal_title

International journal of molecular sciences

authors

Chen HF,Chuang HC,Tan TH

doi

10.3390/ijms20112668

subject

Has Abstract

pub_date

2019-05-30 00:00:00

issue

11

issn

1422-0067

pii

ijms20112668

journal_volume

20

pub_type

杂志文章,评审

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