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Updated: Nov 6, 2025
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
The emerging roles of dual-specificity phosphatases and their specific characteristics in human cancer
Ping-Ping Gao1, Xiao-Wei Qi1, Na Sun1
1Breast and Thyroid Surgery, Southwest Hospital, Army Medical University, Chongqing 400038, China.
Abstract:
Reversible phosphorylation of proteins, controlled by kinases and phosphatases, is involved in various cellular processes. Dual-specificity phosphatases (DUSPs) can dephosphorylate phosphorylated serine, threonine and tyrosine residues. This family consists of 61 members, 44 of which have been identified in human, and these 44 members are classified into six subgroups, the phosphatase and tensin homolog (PTEN) protein phosphatases (PTENs), mitogen-activated protein kinase phosphatases (MKPs), atypical DUSPs, cell division cycle 14 (CDC14) phosphatases (CDC14s), slingshot protein phosphatases (SSHs), and phosphatases of the regenerating liver (PRLs). Growing evidence has revealed dysregulation of DUSPs as one of the common phenomenons and highlighted their key roles in human cancers. Furthermore, their differential expression may be a potential biomarker for tumor prognosis. Despite this, there are still many unstudied members of DUSPs need to further explore their precise roles and mechanism in cancers. Most importantly, the systematic review is very limited on the functional/mechanistic characteristics and clinical application of DUSPs at present. In this review, the structures, functions and underlying mechanisms of DUSPs are systematically reviewed, and the molecular and functional characteristics of DUSPs in different tumor types according to the current researches are summarized. In addition, the potential roles of the unstudied members and the possible different mechanisms of DUSPs in cancer are discussed and classified based on homology alignment and structural domain analyses. Moreover, the specific characteristics of their expression and prognosis are further determined in more than 30 types of human cancers by using the online databases. Finally, their potential application in precise diagnosis, prognosis and treatment of different types of cancers, and the main possible problems for the clinical application at present are prospected.
Insights
Dual-specificity phosphatases (DUSPs) are crucial in cellular processes and cancer. This review systematically examines DUSP functions, mechanisms, and clinical applications, highlighting their potential as cancer biomarkers and therapeutic targets.
Area of Science:
- Molecular Biology
- Biochemistry
- Oncology
Background:
- Reversible protein phosphorylation by kinases and phosphatases regulates cellular functions.
- Dual-specificity phosphatases (DUSPs) dephosphorylate serine, threonine, and tyrosine residues.
- DUSP dysregulation is common in human cancers, with potential prognostic value.
Purpose of the Study:
- To systematically review DUSP structures, functions, and mechanisms in cancer.
- To summarize DUSP roles and characteristics across various tumor types.
- To explore unstudied DUSP members and their potential in cancer biology and clinical applications.
Main Methods:
- Systematic literature review of DUSP functions and mechanisms.
- Homology alignment and structural domain analysis for DUSP classification.
- Analysis of DUSP expression and prognosis in over 30 human cancers using online databases.
Main Results:
- DUSPs play significant roles in human cancers, with differential expression linked to prognosis.
- Current research is limited on many DUSP members, necessitating further investigation.
- DUSP expression patterns and prognostic significance vary across different cancer types.
Conclusions:
- DUSPs represent promising biomarkers for precise cancer diagnosis and prognosis.
- Understanding DUSP mechanisms offers potential for novel cancer therapeutic strategies.
- Further research is needed to overcome challenges in the clinical application of DUSPs.
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