※ MKP family introduction

    MAPK phosphatase (MKP) is a large family of dual-specificity phosphatases. The family members are characterized by the C-terminal catalytic domains which share the sequence similarity with prototypic dual-specificity protein phosphatase VH-1 and the N-terminal domain contains two regions of sequence similarity to the catalytic domain of the Cdc25 phosphatase. MKP are involved in varieties of cellular processes. DUSP10/MKP-5 can negatively regulate the JNK signaling pathway and play an important role in negatively regulating innate immune responses and proper T cell function. In addition, DUSP10/MKP-5 can regulate p38 MAPK activity. DUSP1/MKP-1 is involved in regulating metabolic by dephosphorylating its MAPK substrates. DUSP9/MKP-4 plays a critical role in placental development and function. DUSP6/MKP-3 acts as a negative feedback regulator of fibroblast growth factor signaling (1).

Reference
1. Dickinson, R.J. and Keyse, S.M. (2006) Diverse physiological functions for dual-specificity MAP kinase phosphatases. J Cell Sci, 119, 4607-4615. PMID: 17093265