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Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation

Pp42/MAP kinase (refered to here as p42P) becomes enzymatically activated within 5 minutes following addition to quiescent cells of various growth and metabolic agonists (1,2). The activated form of p42P is phosphorylated on threonine and tyrosine and both phosphorylations are required for activity (3), suggesting the enzyme serves to integrate different signaling pathways. We purified p42P to homogeneity, and determined the sequence of the tryptic peptide which contains both of the regulatory phosphorylations (4). This sequence was found to be similar to a previously published partial sequence of a cDNA (ERK1) for another mitogen-activated protein kinase (5). Using oligonucleotides based on this sequence information, we isolated from a mouse 3T3 library a full-length cDNA which encodes p42TMP (Figure 1). The sequence is 85% identical to the rat ERK1 sequence at the amino acid level. However, P42'* is not the murine equivalent of rat ERK1, as we also have isolated a mouse 3T3 cDNA which is 97% identical to the published ERK1 sequence. Thus, there appears to be a family of kinases related to p42P, as suggested by Northern analysis using ERK1 probes (5, 6). This is the first report of a full length sequence for one of these family members. The p42r amino acid sequence is 50% identical to KSS1 (7) and FUS3 (8), two yeast kinases which also function in Go. Interestingly, the region in p42P which contains the regulatory phosphorylations is perfectly conserved in all four kinases, raising the possibility that both the function and the mechanisms of regulation have been evolutionarily conserved in this kinase family.