Fig. 5: Paxillin binding to adhesions is driven by the LIM domains but stabilized by the N-terminus. | Communications Biology

Fig. 5: Paxillin binding to adhesions is driven by the LIM domains but stabilized by the N-terminus.

From: Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions

Fig. 5

a, f Schematic representation of paxillin a truncation mutants and f N-terminal mutants. All proteins were N-terminally tagged with PA-GFP or mCherry. b, g Experimental dissociation kinetics of PA-GFP_paxillin wt and b truncation mutants or g N-terminal mutants, from β3_mCherry-positive FAs. c, h Box plot of the half-life of PA-GFP_paxillin wt and c truncation mutants or h N-terminal mutants, in β3_mCherry-positive FAs. Statistical analysis is provided in Supplementary Dataset 4. d Quantification of mCherry_paxillin wt and truncation mutants retained in FAs, isolated from NIH-3T3 cells co-expressing β3WT_GFP. Statistical analysis is provided in Supplementary Dataset 1. e Representative TIRF images of FAs in NIH-3T3 cells co-expressing β3WT_GFP and mCherry_paxillin proteins. Left panel: FAs in intact cells; right panel: isolated FAs. i Quantification of the β3VE/YA integrin flow in adhesions, expressed as mean displacement over time (µm/min) per replicate. Statistical analysis is provided in Supplementary Dataset 2. Neg ctr: PA-GFP in photoactivation experiments and mCherry in isolated FAs. ns (not significant) p > 0.05; *p ≤ 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001. Sample size, complete statistical analysis, and p values are provided in tables in supplementary datasets.

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