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. 2020 May 13;7(14):2000098. doi: 10.1002/advs.202000098

Figure 2.

Figure 2

DC‐Rhoin is a specific inhibitor among Rho family proteins, which disrupts the interactions of RhoA with GEF and GDI in vitro through covalent binding to residue Cys107 of RhoA. a) Compound DC‐Rhoin mainly inhibited the binding of RhoA with GEF‐LARG and GDI; rather than the interaction between RhoA and RhoGAP domain of ARAP3 (Arf‐GAP with Rho‐GAP domain, ANK repeat, and PH domain‐containing protein 3). PD represents the pull‐down assay. b) DC‐Rhoin did not block the interaction between RhoAC107A and LARG at the concentration of 25 µm in vitro. c) DC‐Rhoin inhibited the binding between Rho GTPases and their respective GEFs, PD represents the pull‐down assay. d) DC‐Rhoin had slight effect on other small GTPases. PD represents the pull‐down assay. e) In NIH3T3 cells, DC‐Rhoin inhibited the activation of RhoA or Cdc42 at the dose of 25 µm, the activity of Rac1 was inhibited at a much higher concentration of DC‐Rhoin at 100 µm. f) In NIH3T3 cells, DC‐Rhoin had minimal effect on the activation of Ral or Ras.