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. 2008 Dec 5;283(49):34457–34468. doi: 10.1074/jbc.M801465200

FIGURE 4.

FIGURE 4.

The FH1 domain of hDia-1 is critical for binding to the RAGE cytoplasmic domain. A, schematic diagram of Myc-tagged hDia-1 and truncation mutants used in this study. Numbers indicate amino acid positions in human Dia-1. Rho-BD, Rho GTPase binding domain; DID, diaphanous inhibitory domain; DD, dimerization domain; CC, coiled-coil region; FH1 and -2, formin-homology region 1 and 2; DAD, diaphanous autoinhibitory domain. B, to analyze the domain(s) of Dia-1, which interacts with the RAGE cytoplasmic domain, coimmunoprecipitation (IP) experiments were performed. SK-BR-3 cells were transiently cotransfected with the indicated Myc-tagged hDia-1 constructs and the His-tagged RAGE cytoplasmic domain. Immunoprecipitation was performed with anti-His antibodies followed by Western blotting (WB) with anti-Myc antibodies (left panel). Western blot analysis was performed on input lysate as indicated with anti-Myc and anti-His antibodies for hDia-1 and RAGE cytoplasmic domain constructs, respectively (right panel). Note that the hDia-RhoBD does not bind to the RAGE cytoplasmic domain. All panels (A-B) are representative images of multiple independent experiments.