Fig. 5: The conformational change in the ABD correlates with an increased α-catenin turnover.

a, b Representative intensity images of differentiated MEKs expressing F7-NF-697 in PA (a) and MA (b) directly after photobleaching and after 560 s of fluorescence recovery. Dashed squares in magenta, cyan, and green indicate photobleached regions of interest. Kymograms show fluorescence recovery from regions 1 (PA) and 2 (MA) in the green dashed squares. c The calculated mobile fractions indicate a faster protein turnover of α-catenin molecules in MA. Low mobile fractions are associated with PA and can be further dampened by CytoD treatment (pooled, PA and MA: N = 5 replicates, n = 107, 42, 65 junctions; CytoD: N = 3 replicates, n = 45 junctions). d Recovery of the normalized mean fluorescence intensities shown with s.e.m. from FRET-FLIM/FRAP experiments in cells expressing F7-NF-697; data are categorized into PA (green) and MA (blue). Data from cells treated with CytoD are shown in cyan. e Quantification of live-cell FRET-FLIM/FRAP experiments in MEKs expressing F7-NF-697. Plotting mobile fractions over FRET efficiencies obtained from individual AJs reveals a correlation between α-catenin conformation and AJ turnover. The regression line, with a 95% confidence interval, was calculated by a Spearman correlation test (n = 107 values). f Regression curves obtained from bi-exponential fitting of data from standard FRAP experiments; data are categorized into PA (green) and MA (blue). Fitting parameters are shown in tables; values are given with standard error (N = 6 replicates, n = 40, 40). Boxplots show the median, the 25th and 75th percentiles and whiskers reaching to the last data point within 1.5× interquartile range. Scale bar: 10 μm. Two-sample KS test: ***p < 0.001, n.s. (not significant) p ≥ 0.05.