Dual specificity phosphatase 9 (DUSP9)

Dual specificity phosphatase 9 (DUSP9), also known as MKP-4, is a member of the dual specificity phosphatase family that catalyzes the removal of phosphate groups from both phosphotyrosine and phosphoserine/threonine residues on protein substrates. DUSP9 plays a crucial role in the inactivation of mitogen-activated protein kinases (MAPKs), particularly the ERK, JNK, and p38 families, thus acting as a key negative regulator of MAPK signal transduction. It is expressed in various tissues, localizes predominantly in the cytoplasm, and helps fine-tune cell responses to stress, growth factors, and cytokines, being implicated in the regulation of insulin signaling, cancer cell resistance, and inflammation.

Other names

MKP-4Mitogen-activated protein kinase phosphatase 4

Drugs or molecules that increase DUSP9 (MKP-4) activity can dephosphorylate and inactivate MAP kinases (ERK, JNK, p38), thereby negatively regulating pro-inflammatory and stress signaling cascades and potentially reversing insulin resistance