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. 2010 Dec 14;286(8):6697–6706. doi: 10.1074/jbc.M110.183558

FIGURE 1.

FIGURE 1.

KN-62 affects AKAP79-PKC interactions in isoform-dependent manner. AKAP79(31–52) was incubated with PKC isoforms (200 ng; Input lane, 25 ng) and KN-62 as indicated. A, left, representative blots showing the effect of KN-62 on PKC isoform binding AKAP79(31–52). Right, graphical summary of data normalized to their respective controls. Statistical significance for each group is as follows: PKCα: n = 6; 100 nm and 1 μm, p < 0.05; PKCβ: n = 4–5; not significant; PKCγ: n = 5–6; 100 nm and 1 μm, p < 0.01; 10 μm, p < 0.05; PKCδ: n = 4–5; 10 nm–10 μm, p < 0.01; PKCϵ: n = 7–8; 1–10 μm, p < 0.01; and PKCζ: n = 4–5; not significant. B, percentage of control binding to AKAP79(31–52) in response to KN-62 (1 μm) is plotted versus the fraction of input bound for each PKC isoform. Percentages are calculated as the amount of PKC recovered in control lanes normalized to the input lane. Black, red, and green symbols reflect typical, novel, and atypical PKC isoforms, respectively. The dashed line represents the best fit through the data determined by linear regression analysis (r = 0.85). All graphs depict mean ± S.E.