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Vol. 13, Issue 4, 1175-1189, April 2002
and§
*Mario Negri Institute for Pharmacological Research, 20157 Milan,
Italy; Previously published reports support the concept that, besides
promoting homotypic intercellular adhesion, cadherins may transfer intracellular signals. However, the signaling pathways triggered by cadherin clustering and their biological significance are still poorly understood. We report herein that transfection of VE-cadherin (VEC) cDNA in VEC null endothelial cells induces actin
rearrangement and increases the number of vinculin positive adhesion
plaques. VEC expression augments the level of active Rac but decreases active Rho. Microinjection of a dominant negative Rac mutant altered stress fiber organization, whereas inhibition of Rho was ineffective. VEC expression increased protein and mRNA levels of the Rac-specific guanosine exchange factor Tiam-1 and induced its localization at
intercellular junctions. In addition, in the presence of VEC, the
amounts of Tiam, Rac, and the Rac effector PAK as well as the level of
PAK phosphorylation were found increased in the membrane/cytoskeletal fraction. These observations are consistent with a role of VEC in
localizing Rac and its signaling partners in the same membrane compartment, facilitating their reciprocal interaction. Through this
mechanism VEC may influence the constitutive organization of the actin cytoskeleton.
Fondatione Italiana Ricerco sul Cancro (FIRC)
Institute of Molecular Oncology, 20139 Milan, Italy;
Imperial College, 5W7 2AZ London, United Kingdom; and
§Dipartimento di Scienze Cliniche e Biologiche, Facolta'
di Medicina e Chirurgia, Universita' dell'Insubria, 21100 Varese,
Italy
Corresponding author. E-mail address:
lampugnani{at}ifom-firc.it.
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