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Abstract
Mitogen-activated protein (MAP) kinases are activated by combined tyrosine and threonine
phosphorylation catalysed by MAP kinase kinase, a novel class of protein kinases with
dual specificity for both tyrosine and serine/threonine. MAP kinase kinase is turned
on by serine/threonine phosphorylation catalysed by an immediate upstream kinase.
The MAP kinase cascade appears to be conserved during evolution and thus might play
an essential role in diverse intracellular signaling processes from yeasts to vertebrates.