A distinct PAR complex associates physically with VE-cadherin in vertebrate endothelial cells (2006)

A10 IDENIden, S., Rehder, D., August, B., Suzuki, A., Noda, K., Nagafuchi, A., Wolburg-Buchholz, K., Wolburg, H., Ohno, S., Behrens, J., Vestweber, D., Ebnet, K., EMBO Rep. 2006 Dec;7(12):1239-46. Epub 2006 Oct 20.

Abstract


A cell polarity complex consisting of partitioning defective 3 (PAR-3), atypical protein kinase C (aPKC) and PAR-6 has a central role in the development of cell polarity in epithelial cells. In vertebrate epithelial cells, this complex localizes to tight junctions. Here, we provide evidence for the existence of a distinct PAR protein complex in endothelial cells. Both PAR-3 and PAR-6 associate directly with the adherens junction protein vascular endothelial cadherin (VE-cadherin). This association is direct and mediated through non-overlapping domains in VE-cadherin. PAR-3 and PAR-6 are recruited independently to cell-cell contacts. Surprisingly, the VE-cadherin-associated PAR protein complex lacks aPKC. Ectopic expression of VE-cadherin in epithelial cells affects tight junction formation. Our findings suggest that in endothelial cells, another PAR protein complex exists that localizes to adherens junctions and does not promote cellular polarization through aPKC activity. They also point to a direct role of a cadherin in the regulation of cell polarity in vertebrates.

 

Pubmed

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