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. Author manuscript; available in PMC: 2014 Oct 8.
Published in final edited form as: Structure. 2013 Aug 22;21(10):1757–1768. doi: 10.1016/j.str.2013.07.008

Figure 6. RASSF5 Blocks Mst2 Autoactivation through Heterodimerization.

Figure 6

(A) The kinetic profiles of T180 autophosphorylation of full-length Mst2, the full-length Mst2 and RASSF5-SARAH complex, the full-length point mutant Mst2K473A, and the full-length point mutant Mst2K473A and RASSF5-SARAH complex were shown. The relative α-Mst2 P-T180 intensities were normalized against Mst2 reaction at 60 minute (100%). Data are representative of at least two independent experiments.

(B) In vitro dimerization assay of Mst2 mutants. HA- and Myc-tagged Mst2 proteins were co-translated in vitro in the presence of 35S-methionine. The input and anti-HA IP were separated by SDS-PAGE and analyzed with a phosphor imager. Mutants that retain the dimerization ability were colored in blue.

(C) Quantification of the homodimerization of Mst2 mutants in (B).

(D) Binding between GST-RASSF5-SARAH and in vitro translated Mst2 proteins. Mst2K473A has a weakened interaction with GST-RASSF5 and is labeled in red.

(E) Quantification of GST-RASSF5 binding of Mst2 mutants in (D).