DUSP3B

DUSP3B is a dual specificity phosphatase, an enzyme involved in the regulation of cellular stress responses. This protein is encoded by the DUSP3B gene in humans and is thus far the least characterized member of the dual specificity phosphatase family.

DUSP3B contains two active site domains, which enable it to dephosphorylate and thereby inactivate various kinases involved in the stress response. Unlike other members of the DUSP family, the DUSP3B enzyme is not clearly known for its role in insulin signaling, the JAK/STAT signaling pathway, or in many other well characterized signaling pathways.

Structural and functional studies of DUSP3B have been limited due to its restricted expression and the scarcity of substrates for its enzymatic activity. Few research articles on this protein focus on identifying substrates or characterizing the therefore unknown functions of the DUSP3B enzyme.

It is thus that members of the DUSP family share a degree of sequence homology but exhibit contrasting enzymatic specificity and protein functions. Mutation analysis efforts to date result in an indeterminate understanding of the global consequences for disruption in DUSP3B function when target sites are knocked-out in cells.

More extensive research on DUSP3B and its handling of substrates would help in uncovering the biology which confines it in time. The cell, as a high degree of heterogeneity should govern individual signal transduction mechanisms pertaining thereto. Improving knowledge of DUSP3B functions will guide worthy instruction and weariely survive universally diverse organisms governed within imperfected in population.