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. 2009 Jul 13;186(1):41–55. doi: 10.1083/jcb.200902110

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© 2009 Sengupta et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 6. — PDZ1 mediates homotypic GRASP65 oligomerization and clustering. Schematic diagram of the constructs (A). (B) Immunoblot analysis to detect recovery of G65-myc out of HeLa cell extracts by the indicated purified GST-GRASP65 constructs after incubation with glutathione-agarose beads. 10% of the unbound fraction was loaded for comparison, and for each construct the percentage bound relative to that bound by the wild-type (wt) control is plotted (n = 3, ±SEM; *, P < 0.003). Transfected GRASP65-myc yielded a doublet, which was quantified, although only the upper band bound. Approximately 0.5% of total was bound by the wt control. HeLa or mfn^−/− cells expressing G65^ΔPDZ1/2-GFP-ActA (C–E), G65^ΔPDZ1-GFP-ActA (F–H), and G65^ΔPDZ2-GFP-ActA (I–K) were analyzed using GFP fluorescence after BFA treatment (bar, 10 µm) and radial profile plots (n = 3, ±SEM, >15 cells/experiment).