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. 2011 Nov 15;22(22):4362–4372. doi: 10.1091/mbc.E11-04-0283

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© 2011 O'Leary 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 8: — Internal deletion within a 26–amino acid VCD segment disrupts trafficking. (A) Location of the 26–amino acid segment in Pcdh-γA3 bounded by the Δct163 and Δct190 truncations. Underlined is the location of 12–amino acid excision in (B) full-length and (E) constant-domain-deleted Pcdh-γA3-GFP (Δ741-752-GFP and Δ741-752Δconst-GFP, respectively). Δ741-752-GFP colocalized with LAMP-2 (C) in a perinuclear manner but only weakly coclustered RFP-LC3 (C). In contrast, Δ741-752Δconst-GFP lacked both LAMP-2 colocalization (F) and RFP-LC3 clustering activity (F). By CLEM, Δ741-752-GFP (D) corresponded to enlarged vacuoles that resembled disrupted lysosomes (V), with very few tubules (arrowhead). CLEM of Δ741-752Δconst-GFP (G) revealed that this construct was associated with membrane whorls. Bar,10 μm in C and F; 5 μm in light images in D and G; and 500 nm in EM images.