"KSR-1 and BRAF or CRAF interaction is enhanced by pharmacological RAF inhibition, regulating drug-induced RAF dimer formation ( xref – xref )."
"Using co-IP, we tested the interactions between the N-terminal regulatory regions (NTRs) of BRAF, CRAF, and KSR1."
"Using yeast two-hybrid (Y2H) screening, we identified the F311S mutation in MEK1 that abrogated KSR1, BRAF and CRAF binding ( xref )."
"We took advantage of the fact that kinase-dead forms of BRAF, CRAF and KSR1 could function as trans-activators to functionally separate the RAF dimer into an “activator” component (dead) and a “receiver” component (live), as proposed for other dimeric kinases ( xref )."
"In addition, association of B-Raf and/or Raf-1 with the scaffold protein KSR1 also modulates activation of MEK [ xref – xref ]."
"To confirm that dimerization is required, dimerization-impairing forms of kinase-dead BRAF (R509H), CRAF (DDEE/R401H) and KSR1 (DDEE/R615H) ( xref ) were tested."
"These mutations also increased binding to endogenous KSR1, BRAF, and CRAF ( xref )."