Figure 5.

Activation of DUSP6 phosphatase by interaction with substrate ERK. This is a simplified schematic representation of ERK binding to DUSP6, resulting in catalytic activation. The carboxy-terminal catalytic domain is represented by a circle and the amino terminus containing the ERK binding (EB) domain by a rectangle. DUSP6 appears to exist in a low-activity state until binding to ERK through the EB domain results in a conformational change, triggering activation of the phosphatase. This results in ERK dephosphorylation and subsequent dissociation of the complex.