In studies to elucidate key regulatory pathways in signal transduction, several protein serine/threonine (Ser/Thr) kinases have been identified. Included among such kinases are two distinct families of 40S ribosomal protein S6 Ser/Thr kinases present in somatic animal cells, designated p70 S6 kinase and p90 Rsk kinase. p90 Rsk kinase is maximally activated within minutes of addition of growth factors or phorbol ester to cultured cells followed by activation of p70 S6 kinase. Both enzymes are regulated by serine/threonine phosphorylation, suggesting that specific kinases may exist upstream in the signaling pathway that regulate these kinases. In fact, evidence suggests that one such family of activating enzymes includes the members of the ERK MAP kinase family. The ERK MAP kinases are, in turn, regulated by phosphorylation at threonine and tyrosine residues by a protein kinase designated MEK.
