Dual specificity protein phosphatase 10 (MKP5) (MKP5)

Dual specificity protein phosphatase 10 (DUSP10), commonly known as Mitogen-activated protein kinase phosphatase 5 (MKP5), is an enzyme that acts as a negative regulator of the Mitogen-Activated Protein Kinase (MAPK) signaling pathways [UniProt: Q9Y6W6]. It specifically targets and dephosphorylates the stress-activated kinases c-Jun N-terminal kinase (JNK) and p38 MAPK, thereby controlling cellular responses to environmental stress and inflammatory stimuli [PubMed: 11278933]. MKP5 is highly expressed in the immune system and skeletal muscle, where it plays a pivotal role in modulating innate and adaptive immunity as well as tissue repair [PubMed: 21844325]. In Duchenne Muscular Dystrophy (DMD), MKP5 has emerged as a promising therapeutic target because its genetic or pharmacological inhibition enhances muscle stem cell function and promotes muscle regeneration [PubMed: 28592548]. Beyond muscular dystrophy, MKP5 is implicated in metabolic disorders like obesity and various inflammatory diseases due to its role in regulating cytokine production [PubMed: 21844325]. While there are currently no FDA-approved drugs targeting MKP5, experimental small-molecule inhibitors are being developed to treat muscle wasting and inflammatory conditions [PubMed: 28592548].

Other names

DUSP10Mitogen-activated protein kinase phosphatase 5MKP-5Dual specificity protein phosphatase 10

Inhibition of the phosphatase activity of MKP5, leading to sustained activation of JNK and p38 MAP kinases.