Figure 5

ERK1/2 is activated through MEK1/2 phosphorylation and association with RIP1 complex. (a) Phosphorylation of ERK1/2 was triggered by ESA, but was impaired by Nec1. (b) ERK1/2 was constitutively associated with RIP1 regardless of ESA stimulation. MEK1/2 formed the complex containing RIP1 and ERK1/2 to phosphorylate ERK1/2. (c) ESA induced MEK1/2 phosphorylation, which was suppressed by Nec1 and Nec5, but not Nec1i.