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. 2009 Aug 13;422(Pt 2):229–235. doi: 10.1042/BJ20090624

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© 2009 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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(A) A representative result of the immunoprecipitation of GDIs with Rab4A as the bait protein. HEK-293 cells were co-transfected with FLAG–Rab4A(S27N) and HA–GDI-1 or HA–GDI-2. Immunoprecipitation (IP) and Western blotting were carried out in the same way as described in Figure 4(A). (B) Quantification of the interactions between GDIs and Rab4A. Results are represented as the means±S.E.M. of two independent experiments. Band intensity is normalized as described in Figure 4(B). (C) Quantification of the interaction of GDI-1 and GDI-2 with Rab4A by acceptor photobleaching FRET. HEK-293 cells were co-transfected with EGFP–GDI-1 or EGFP–GDI-2, and mKO–Rab4A(S27N). Experiments and data preparation were carried out in the same way as described in Figure 5(B). Results are represented as means±S.E.M. (GDI-1, n=25 cells; GDI-2, n=25 cells).