Dual specificity protein phosphatase 22

DUSP22 is a dual specificity protein phosphatase that dephosphorylates both phosphotyrosine and phosphoserine/phosphothreonine residues. It functions as a negative regulator of T-cell receptor signaling by activating JNK pathways and promoting degradation of the E3 ubiquitin ligase UBR2, thereby inhibiting T-cell mediated immune responses. The protein also dephosphorylates and inactivates the tyrosine kinase LCK (UniProt: Q9NRW4).

DUSP22 is involved in immune cell signaling and may contribute to B-cell receptor function. No other disease associations are documented in UniProt.

DUSP22 is downregulated in Alzheimer's disease brain tissue. Chaparral AD proteomics data from human post-mortem AD brain versus age-matched controls (TMT-labeled DDA proteomics across four subcellular fractions) shows a mean log2 fold-change of −0.55, indicating reduced protein abundance in AD (Chaparral AD proteomics). The functional significance of this reduction in AD pathogenesis remains to be determined.