Development and application of chemical proteomics identify p120-catenin glutathionylation regulating E-cadherin stability. Kukulage et al.
One important function of p120 is to bind and stabilize E-cadherin at the plasma membrane. Therefore, we examined the localization of p120 and E-cadherin in high and low glucose conditions. In MCF7 cells expressing p120 WT, E-cadherin was mainly localized at the membrane. p120 (FLAG, red) showed high co-localization with E-cadherin (green) under high glucose (25 mM) (Pearson coefficient 0.69 ± 0.09, n = 35). On the other hand, under low glucose (5 mM), p120 was distributed to the cytoplasm, whereas E-cadherin was mainly localized to the membrane, significantly decreasing their co-localization (Pearson coefficient 0.34 ± 0.06, n = 35). Importantly, MCF7 cells expressing p120 C692S showed high co-localization of p120 and E-cadherin in high glucose (25 mM) (Pearson coefficient 0.71 ± 0.09, n = 35), and the co-localization remained relatively unchanged even in low glucose (5 mM) (Pearson coefficient 0.68 ± 0.09, n = 35), supporting that p120 C692 glutathionylation (or oxidation) is responsible for the cytoplasmic redistribution of p120 under the stressed condition.