Sandbox Reserved 707: Difference between revisions

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	These studies indicate that the binding of an inhibitor to C-RAF leads to the formation of a C-RAF homodimer and C-RAF activation resulting in downstream MEK-ERK activation. Another possible, but not mutually exclusive, mechanism is that binding of an inhibitor to B-RAF leads to the formation of a B-RAF–C-RAF heterodimer and C-RAF activation. That RAF-kinase-induced paradoxical activation occurs in B-RAF -/- mouse embryonic fibroblasts does not rule out the possibility that B-RAF–C-RAF heterodimers play a role in paradoxical activation.		These studies indicate that the binding of an inhibitor to C-RAF leads to the formation of a C-RAF homodimer and C-RAF activation resulting in downstream MEK-ERK activation. Another possible, but not mutually exclusive, mechanism is that binding of an inhibitor to B-RAF leads to the formation of a B-RAF–C-RAF heterodimer and C-RAF activation. That RAF-kinase-induced paradoxical activation occurs in B-RAF -/- mouse embryonic fibroblasts does not rule out the possibility that B-RAF–C-RAF heterodimers play a role in paradoxical activation. A recent study showed that A-RAF acts as a Scaffold to stabilize the heterodimers of B-RAF and C-RAF<ref>PMID:22927515</ref>.

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