Supporting this idea, immunofluorescence studies revealed not only the BRAFV600E-mediated inhibition of MST1-induced FoxO3 nuclear translocation, but also a direct interaction between MST1 and BRAFV600E, which was confirmed through IP assays that shown that BRAFV600E binds to the C-terminal dimerization domain of MST1
Supporting this idea, immunofluorescence studies revealed not only the BRAFV600E-mediated inhibition of MST1-induced FoxO3 nuclear translocation, but also a direct interaction between MST1 and BRAFV600E, which was confirmed through IP assays that shown that BRAFV600E binds to the C-terminal dimerization domain of MST1. In fact, the dimerization domain of MST1/2 mediates MST1 kinase activity by…
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