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J Cell Biol. 2015 Jan 5;208(1):23-32. doi: 10.1083/jcb.201409108.

Rac1 functions as a reversible tension modulator to stabilize VE-cadherin trans-interaction.

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Department of Pharmacology, University of Illinois College of Medicine, Chicago, IL 60612.
Department of Physiology, Institute for Cardiovascular Research, Vrije University of Amsterdam, 1081 HV Amsterdam, Netherlands.
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Department of Biomedical Engineering, Virginia Commonwealth University, Richmond, VA 23284.


The role of the RhoGTPase Rac1 in stabilizing mature endothelial adherens junctions (AJs) is not well understood. In this paper, using a photoactivatable probe to control Rac1 activity at AJs, we addressed the relationship between Rac1 and the dynamics of vascular endothelial cadherin (VE-cadherin). We demonstrated that Rac1 activation reduced the rate of VE-cadherin dissociation, leading to increased density of VE-cadherin at AJs. This response was coupled to a reduction in actomyosin-dependent tension across VE-cadherin adhesion sites. We observed that inhibiting myosin II directly or through photo-release of the caged Rho kinase inhibitor also reduced the rate of VE-cadherin dissociation. Thus, Rac1 functions by stabilizing VE-cadherin trans-dimers in mature AJs by counteracting the actomyosin tension. The results suggest a new model of VE-cadherin adhesive interaction mediated by Rac1-induced reduction of mechanical tension at AJs, resulting in the stabilization of VE-cadherin adhesions.

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