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Signaling threshold regulation by the Ras effector IMP Matheny SA; White MAJ Biol Chem 2009[Apr]; 284 (17): 11007-11The Ras effector and E3 ligase family member IMP (impedes mitogenic signal propagation) acts as a steady-state resistor within the Raf-MEK-ERK kinase module. IMP concentrations are directly regulated by Ras, through induction of autoubiquitination, to permit productive Raf-MEK complex assembly. Inhibition of Raf-MEK pathway activation by IMP occurs through the inactivation of KSR, a scaffold/adapter protein that couples activated Raf to its substrate MEK1. The capacity of IMP to inhibit signal propagation through Raf to MEK is, in part, a consequence of disrupting KSR1 homo-oligomerization and c-Raf-B-Raf hetero-oligomerization. These observations suggest that IMP functions as a threshold modulator, controlling sensitivity of the cascade to stimulus by directly limiting the assembly of functional KSR1-dependent Raf-MEK complexes.|*Signal Transduction[MESH]|Animals[MESH]|Dimerization[MESH]|Humans[MESH]|MAP Kinase Kinase 1/metabolism[MESH]|Models, Biological[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH]|Proto-Oncogene Proteins B-raf/metabolism[MESH]|Proto-Oncogene Proteins c-raf/metabolism[MESH]|Substrate Specificity[MESH]|Ubiquitin-Protein Ligases/*metabolism[MESH]|ras Proteins/*metabolism[MESH] |
