Abstract
The possible formation of a stable complex between extracellular signal-regulated kinases (ERKs) and Raf protein kinases was investigated in an attempt to understand the molecular mechanism by which Raf protein kinases were differentially regulated in response to the various stimuli, leading to the activation of ERKs in rat hippocampus. ERK3 was found to coelute with B-Raf, but not c-Raf1, after fractionation of rat hippocampal lysates by QMA anionic exchange chromatography. ERK3 was released into soluble supernatant fraction from the B-Raf, but not c-Raf1, immunoprecipitate, after incubation with ATP. These results, taken together, suggest the specific association of ERK3 with B-Raf in rat hippocampus.
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