Rania Al-Mahdi ́s thesis 25.10.15
نویسنده
چکیده
The atypical MAP kinases ERK3 and ERK4 are activated by phosphorylation of a single serine residue lying within the signature sequence S-E-G in the activation loop. Thus far theregulation of ERK3 and ERK4 phosphorylation and thus activity is poorly understood. Herewe have screened mammalian dual-specificity MAP kinase phosphatases for their ability tointeract with ERK3 and ERK4 and report that the inducible nuclear phosphatase DUSP2, previously identified as a regulator of signaling through both the ERK1/2 and p38 MAPKpathways, binds specifically to both ERK3 and ERK4. This interaction is mediated via theconserved common docking (CD) domains within the carboxyl-terminal domains ofERK3/ERK4 and requires the kinase interaction motif (KIM) located within the non-catalytic amino terminus of DUSP2. The interaction between ERK3/ERK4 and DUSP2 results in thestabilization of DUSP2 and the dephosphorylation of ERK3/ERK4 both in vitro and in vivo.Moreover, the ability of ERK4 to stabilize DUSP2 is dependent on the catalytic activity ofERK4. Furthermore, DUSP2 is efficiently phosphorylated by ERK4 in vitro. Finally, we demonstrate that DUSP2 expression inhibits ERK3 and ERK4 mediated activation of itsdownstream substrate MK5. We conclude that the activity of DUSP2 is not restricted to theclassical MAPK pathways and that DUSP2 is a physiological regulator of the atypicalERK3/ERK4-MK5 signaling pathway in mammalian cells.
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