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Mitogen-activated protein kinases (MAP kinases) are active only when phosphorylated. Here we examine whether the activation of Xenopus p42MAP kinase might involve changes in its association with other proteins as well as changes in its phosphorylation state. We find that when p42MAP kinase is phosphorylated and active, it is monomeric, and that when p42MAP kinase is nonphosphorylated and inactive, about half of it is monomeric and half is a component of a 110-kDa complex. We identify Rsk, an 82-kDa protein kinase that can be phosphorylated and partially activated by p42MAP kinase, as being specifically associated with inactive p42MAP kinase. It is possible that the complex of inactive p42MAP kinase and inactive Rsk acts as a single signal reception particle and that the activation of the two kinases may be better described as a fork in a bifurcating signal transduction pathway than as successive levels in a kinase cascade.
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