Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAP kinase superfamily, which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAP kinases, different tissue distribution and subcellular localization, and different modes of expression induction by extracellular stimuli. This gene product binds to and inactivates p38 and SAPK/JNK. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2014]
Forensic Context
A study in mice demonstrated that the DUSP10 was down-regulated at 6 hours post-injury specifically in skeletal muscle following a local hind limb burn, but its expression was not altered in response to a distant dorsum burn [Padfield et al. DOI:10.01.ta.0000230567.56797.6c].