Dual specificity protein phosphatase 14 (DUSP14)

Dual specificity protein phosphatase 14 (DUSP14) is a cysteine-based enzyme capable of dephosphorylating both tyrosine and serine/threonine residues on protein substrates, mainly inactivating MAP kinases such as ERK, JNK, and p38[2][3][1]. Unlike canonical MKPs, DUSP14 lacks the N-terminal CH2 (Cdc25 homology 2) domain and is classified as an “atypical DUSP” within the phosphatase superfamily, displaying substantial substrate specificity diversity[2][1][6]. It plays a role in negative regulation of immune cell signaling, particularly T cell receptor signaling, by inactivating MAP3K7 adapter TAB1[2]. Dysregulation of DUSP14 and related DUSPs is implicated in altered immune responses and may contribute to various diseases including cancer and inflammatory disorders[1][6]. While the potential for DUSP14 as a therapeutic target is recognized, no drugs currently target it specifically, and broad inhibition may carry risks due to compensatory mechanisms and overlapping functions within the DUSP family[6][1][2].

Other names

MKP6MKP-LMitogen-activated protein kinase phosphatase 6MAP kinase phosphatase 6MKP-6MKP-1-like protein tyrosine phosphatase

Drugs targeting DUSP14 (hypothetical) would likely inhibit or modify its phosphatase activity, resulting in altered MAP kinase signaling, possibly affecting immune responses or cancer cell proliferation