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. 2011 Jan 15;22(2):189–201. doi: 10.1091/mbc.E10-03-0256

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© 2011 Gorelik et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — Small GTPase Rif binds mDia2 through domains G-DID. (A) Coomassie staining of MBP or MBP-tagged mDia2 proteins (Nt and NtΔBD) that were used in a GTPase-binding assay with GST-Rif Q75L or GST as control. The presence of BD does not increase binding to active Rif in vitro. (B) An immunoblot of MBP-mDia2 proteins Nt, NtΔBD, BD-G-DID, and BD-G that were used in a GTPase binding assay with GST-Rif Q75L or GST control. Constructs Nt, NtΔBD, and BD-G-DID bound Rif, whereas construct BD-G could not be detected unless high exposure times were used. Quantification of band intensities relative to respective controls shows a 2.4-fold (A) and 3.8-fold (B) increase for MBP-Nt and a 6.0-fold (A) and 9.2-fold (B) increase for MBP-NtΔBD. There is no difference in the MBP band intensity between GST and GST-Rif (A). Panels A and B represent separate experiments.