FEBS Letters · 2006 · 56 citations · 13 references
Life SciencesBiochemistryMolecular BiologyCell SignalingProtein-protein InteractionsSignal TransductionCell Signaling NetworksLigand BindingProtein Interaction DomainsProtein Interaction MappingProtein Kinase CascadesProtein-protein Interaction ModulationExtracellular Signal-regulated Kinase PathwayExtracellular Signal-regulated Kinase SignalingKinase Substrate SpecificityMek SignalingMitogen SignalingRaf SignalingRaf-mek-erk SignalingSurface Plasmon Resonance Analysis
The Raf kinase inhibitory protein (RKIP) binds to Raf-1 interfering with binding of the MEK substrate and potentially also Raf-1 activation. In response to mitogen stimulation RKIP dissociates from Raf-1 and later re-associates. Here, using a combination of mutational approaches, biochemical studies, peptide arrays and plasmon surface resonance (BIAcore), we fine map and characterize a minimal 24 amino acid long RKIP binding domain in the Raf-1 N-region, which consists of constitutive elements at both flanks and a center element that is regulated by phosphorylation and enhances the re-binding of RKIP to Raf-1 in the later phase of mitogen stimulation.
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Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP
Kam C. Yeung, Thomas Seitz, Shengfeng Li et al. · Nature · 1999 · 923 citations