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The family of serine/threonine kinases known as ERKs (extracellular signal regulated kinases) or MAPKs (mitogen-activated protein kinases) is activated after cell stimulation by a variety of hormones and growth factors. Cell stimulation induces a signaling cascade that leads to phosphorylation of MEK (MAPK/ERK kinase) which, in turn, activates ERK via tyrosine and threonine phosphorylation. A myriad of proteins represent the downstream effectors for the active ERK and implicate it in the control of cell proliferation and differentiation, as well as regulation of the cytoskeleton. Activation of ERK is normally transient and cells possess dual specificity phosphatases that are responsible for its down-regulation. Furthermore, multiple studies have shown that elevated ERK activity is associated with some cancers. ERK1 is a 44 kDa member of the ERK family and shares 85% homology with ERK2 (42 kDa).
