Dual specificity phosphatase 11 (DUSP11)

Dual specificity phosphatase 11 (DUSP11) is an atypical phosphatase enzyme that dephosphorylates both protein (serine/threonine and tyrosine residues) and non-protein substrates (notably, RNAs with 5′-triphosphates)[1][2][3][4]. DUSP11 is unique among dual specificity phosphatases due to its strong and physiologically relevant RNA phosphatase activity, modulating the biogenesis and processing of small regulatory RNAs as well as cellular noncoding RNAs by converting 5′-triphosphorylated RNA ends to 5′-monophosphates[2][3][4]. It is predominantly localized to the nucleus and is inducible in immune cells upon activation[1][3]. Recent work implicates DUSP11 in the regulation of signal transduction (notably NF-κB signaling), innate and adaptive immune responses, and as a modulator of cellular and viral RNA functions[1][2]. Alterations in DUSP11 activity have been associated with cancer progression (including cholangiocarcinoma) and with regulation of responses to infection and inflammation[1][3][4]. DUSP11 therefore functions at the interface of protein signaling and RNA regulation, representing a promising yet underexplored therapeutic and prognostic target in cancer and immune diseases[1][3][4].

Other names

PIR1Phosphatase that interacts with RNA/RNP complex 1RNA/RNP complex 1-interacting phosphataseRNA/RNP complex-interacting phosphataseDual specificity protein phosphatase 11Serine/threonine specific protein phosphatase

Dephosphorylation of RNA 5′-triphosphates to 5′-monophosphates, Dephosphorylation of protein serine/threonine and tyrosine residues, Modulation of immune signaling (e.g., direct dephosphorylation of IKK-β, regulation of NF-κB pathway)