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. 2014 Jan 9;3:e27687. doi: 10.4161/cl.27687

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Copyright © 2014 Landes Bioscience

This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

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graphic file with name cl-3-e27687-g4.jpg — Figure 4. The p115 cc2 domain promotes dissociation of the Rab1b-GDI2 complex but fails to enhance nucleotide exchange. (A-B) Rates of MANT-GTP incorporation into His-Rab1b in the presence of GST or GST-p115-cc2. (C) Equivalent amounts (approximately 3 µg) of bead-bound His-ScRab1b, a fraction of which was associated with FLAG-GDI2, was incubated with approximately 2μg of cc2. FLAG-GDI2 proteins in the unbound fraction or bound to beads were detected by immunoblotting using a polyclonal anti-FLAG antibody and the percentage of released FLAG-GDI2 was quantified (mean ± SD; n = 3).