ERK proteins are regulated by dual phosphorylation at specific tyrosine and threonine sites mapping within a characteristic Thr-Glu-Tyr motif. Phosphorylation at both the Thr and Tyr residues is required for full enzymatic activation. In response to activation, MAP kinases phosphorylate downstream components on serine and threonine. Upstream MAP kinase regulators include MAP kinase kinase (MEK), MEK kinase and Raf-1. The ERK family has three additional members: ERK 3, ERK 5 and ERK 6.
