Fig. 2: Dimerization of active talin is required to promote potent ligand binding to integrin.
From: Mechanism of integrin activation by talin and its cooperation with kindlin
a A model of multivalent ligand binding to integrin mediated by talin dimerization. b Integrin activation triggered by active full-length talin (tlnM3) is partially reduced by deletion of dimerization domain (tlnM3 DDdel) as measured by the PAC-1-binding assays. All values are given as mean ± S.E.M. ****p < 0.0001 with 95% confidence interval −2.814 to −1.826 (t-test), N = 6 biologically independent samples. c Histogram of PAC-1 binding shows that DDdel (magenta) causes significantly reduced PAC-1 staining. d Cell adhesion to fibronectin, vitronectin, and laminin are all affected when we introduce endogenous level of talin DD deletion or R2526G mutation to talin1/2dko fibroblasts to disrupt talin dimerization. WT values were set to 1. Relative cell adhesion was plotted as mean ±95% CI, N = 6 independent experiments. Fibronectin: ***p < 0.0001, Vitronectin: *p = 0.0233, **p = 0.0018, Laminin: **p = 0.0097. Statistical significance was tested by one-way ANOVA followed by Tukey’s multiple-comparison test. b, d Raw data are provided in Source Data file.
