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. 2013 Mar 15;24(6):715–733. doi: 10.1091/mbc.E12-07-0537

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© 2013 Johnson 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 2: — (A) In the yeast two-hybrid assay, Cx43 interacts with the μ2 subunit of the AP2 complex in a sorting motif–dependent manner. Yeast were cotransformed with the indicated GAL4-binding domain and GAL4 transcription activation domain fusion constructs. Measured by growth on selective media (−His), only the wild-type (WT) tail of Cx43 interacted with the μ2 subunit of the AP2 complex. PVA3 (p53) and PTD1 (large T-antigen) served as positive control, while rabinosyn-5 served as the negative control. (B) Cx43 (green) colocalizes with clathrin and EEA-1 in single cells. (C and D) Cx43 (green) colocalizes with the AP2 complex (red) in both single and contacting cells. (B–D) Outlined boxes are shown at higher power.