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.