Regulation of Endothelial Adherens Junctions by Tyrosine Phosphorylation

Figure 4

The net effect on cadherin tail phosphorylation depends on the action of multiple kinases and phosphatases. The VE-cadherin cytoplasmic region contains multiple phosphorylatable residues (in red) located in or near the JMD and CBD domains responsible for catenin binding (marked in green). Larger font highlights tyrosines 658, 685, and 731, together with serine 665, which have been more intensely studied. The overall phosphorylation status is the effect of a network of kinase (red arrows) and phosphatase (blue arrows) activities. These kinases and phosphatases can modify the cadherin tail and/or associated catenins directly or indirectly via the regulation of other associated kinases and phosphatases. Dotted arrowheads: CK-I and CK-II activity was shown to phosphorylate homologous residues in E-cadherin tail.