Publications

Abstract

Dual specificity phosphatases (DUSPs) are a heterogeneous group of protein phosphatases that can dephosphorylate both phospho-Tyrosine and phospho- Serine diseases. DUSPs can be divided into six subgroups based on sequence similarity that include, slingshots, PRLs, CDC14s, PTENs, Myotubularins, MKPs and atypical DUSPs. Of these subgroups, a great deal of research has focused on the characterisation of the Mitogen Activated Protein Kinase Phosphatases (MKPs). As the name suggests, MKPs dephosphorylate MAPK proteins ERK, MKP proteins. Atypical DUSPs are mostly of low molecular weight and lack the N- terminal CH2 domain common to MKPs. The discovery of most atypical DUSPs has occurred in the past six years, which has initiated a large amount of interest in their role and regulation. In the past, atypical DUSPs have generally been grouped together with the MKPs and characterised for their role in MAPK signalling cascades. Indeed, some have been shown to dephosphorylate MAPKs. The current literature hints at the potential of the atypical DUSPs as important signalling regulators but is crowded with conflicting reports. This review will provide an overview of the DUSP family before focusing on atypical DUSPs, emerging as a group of proteins with vastly diverse substrate specificity and function.