Fig. 5. Mutations of the RHOG–ELMO2^RBD interface disrupts interactions.

ITC binding assay for (a) Wild-type RHOG in the inactive GDP-bound state (left) or active GTP-bound state (right) with wild-type ELMO2^RBD; (b) K9A mutant of ELMO2^RBD with wild-type RHOG; and (c) D38A and R66A mutants of activated RHOG with wild-type ELMO2^RBD. For ITC assays showing no binding, the K_d was not determined (ND). The positions of these residues are shown in Fig. 4c. The experiments were performed independently three times with similar results.