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Review
. 2025 Apr 29;23(1):485.
doi: 10.1186/s12967-025-06499-y.

Dual-specific phosphatases-8: a new target for clinical disease intervention

Tingping Cao  1   2 , Quanling Zhou  1   2 , Fujun Li  1   2 , Mingyue Wang  1   2 , Ming Zhang  2 , Xiaohui Li  2 , Hailong Zhao  1 , Ya Zhou  3   4   5
Affiliations
Review

Dual-specific phosphatases-8: a new target for clinical disease intervention

Tingping Cao et al. J Transl Med. .

Abstract

Dual-specific phosphatase-8 (DUSP8), identified as the first gene in a genome-wide association study (GWAS), is implicated in cellular oxidative stress, proliferation, apoptosis, and drug resistance through its negative regulation of the dephosphorylation activities of JNK, ERK, and p38 within the MAPK pathway. Recent studies have shown that DUSP8 plays a pivotal role in the progression of several human diseases, notably colorectal cancer, diabetic kidney disease, and breast cancer. This suggests that DUSP8 may represent a novel target for clinical intervention in these diseases. This review first introduces the biological structure and function of DUSP8, with a focus on its relationship with a series of diseases and the regulatory mechanisms involved. Furthermore, we concentrate on unresolved scientific questions in the current research, aiming to establish a new theoretical foundation for the diagnosis and treatment of related diseases.

Keywords: Colorectal cancer; DUSP8; Diabetic kidney disease; MAPK; Regulatory mechanism.

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Conflict of interest statement

Declarations. Ethics approval and consent to participate: Not applicable. Consent for publication: Not applicable. Conflict of interest: The authors declare that we have no relevant financial or non-financial interests that could be perceived as potential conflicts of interest in relation to the research and writing of this article.

Figures

Fig. 1 A
Fig. 1 A
The structure of DUSP8. (By Figdraw.)
Fig. 1B
Fig. 1B
Schematic diagram of DUSP8 protein structural domains. (By Figdraw.) Note: T and Y represent phosphorylated threonine and tyrosine residues, respectively, while X is any amino acid
Fig. 2
Fig. 2
Timeline of the research progression of DUSP8. (By Figdraw.)
Fig. 3
Fig. 3
Mechanistic overview of DUSP8’s Role in regulating multiple human diseases. (By Figdraw.)
Fig. 4
Fig. 4
Prospects for future research works on DUSP8. (By Figdraw.)
See this image and copyright information in PMC

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