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      p21-activated kinase 1 (PAK1) can promote ERK activation in a kinase-independent manner.

      The Journal of Biological Chemistry
      Animals, Enzyme Activation, physiology, HEK293 Cells, HeLa Cells, Humans, MAP Kinase Kinase 1, genetics, metabolism, MAP Kinase Kinase 2, MAP Kinase Signaling System, Mice, NIH 3T3 Cells, Neuropeptides, Phosphorylation, Proto-Oncogene Proteins B-raf, Proto-Oncogene Proteins c-raf, p21-Activated Kinases, rac GTP-Binding Proteins, rac1 GTP-Binding Protein

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          Abstract

          PAK1 plays an important role in proliferation and tumorigenesis, at least partially by promoting ERK phosphorylation of C-RAF (Ser-338) or MEK1 (Ser-298). We observed how that overexpression of a kinase-dead mutant form of PAK1 increased phosphorylation of MEK1/2 (Ser-217/Ser-221) and ERK (Thr-202/Tyr-204), although phosphorylation of B-RAF (Ser-445) and C-RAF (Ser-338) remained unchanged. Furthermore, increased activation of the PAK1 activator Rac1 induced the formation of a triple complex of Rac1, PAK1, and MEK1 independent of the kinase activity of PAK1. These data suggest that PAK1 can stimulate MEK activity in a kinase-independent manner, probably by serving as a scaffold to facilitate interaction of C-RAF.

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