Figure 8. Effects of mutations in the SARAH_RASSF5 domain on dimerization with full length MST1.

(A) The SARAH domain sequence of RASSF5. Main interacting non-polar (yellow), acidic (red) and basic (blue) residues are shown. The three positions in which mutations were introduced are marked by asterisks (*). (B) (i) Co-immunoprecipitation assay to show heterodimerisation between myc-MST1 K59R and wild-type (WT) EGFP-RASSF5 and its three mutants. The loading controls are shown below. (ii) Quantification of the bands in terms of relative intensity to the WT control (Mean ± SD. n = 3; *p < 0.05, **p < 0.01, ***p < 0.001). (C) Co-immunoprecipitation assay of the negative controls. A simultaneous negative control was performed using cell lysates containing only EGFP-RASSF5 or its mutants. The loading controls are shown below.