Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro. Activation of a Ca 2+-inhibitable protein kinase that phosphorylates microtubule-associated protein 2 in vitro by growth factors, phorbol esters, and serum in quiescent cultured human fibroblasts. These processes are cell proliferation, cell survival, cell growth, cell metabolism, cell migration and cell differentiation. We then systematically discuss how ERK signalling regulates six fundamental cellular processes in response to extracellular cues. We begin with a brief overview of the structure, regulation, substrate recognition and subcellular localization of ERK1 and ERK2. In this Review, we discuss the current understanding of this important class of kinases. The mechanisms underlying the regulation of ERK1 and ERK2, their mode of action and their impact on the development and homeostasis of various organisms have been the focus of much attention for nearly three decades. By phosphorylating widely diverse substrates, ERK proteins govern a variety of evolutionarily conserved cellular processes in metazoans, the dysregulation of which contributes to the cause of distinct human diseases. The proteins extracellular signal-regulated kinase 1 (ERK1) and ERK2 are the downstream components of a phosphorelay pathway that conveys growth and mitogenic signals largely channelled by the small RAS GTPases.
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