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          Institute: MPI für molekulare Biomedizin     Collection: Publikationen molekulare Biomedizin     Display Documents



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ID: 123157.0, MPI für molekulare Biomedizin / Publikationen molekulare Biomedizin
The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity
Authors:Ebnet, K.; Aurrand-Lions, M.; Kuhn, A.; Kiefer, F.; Butz, S.; Zander, K.; Meyer zu Brickwedde, M. K.; Suzuki, A.; Imhof, B. A.; Vestweber, D.
Language:English
Date of Publication (YYYY-MM-DD):2003-10-01
Title of Journal:Journal of Cell Science
Journal Abbrev.:J Cell Sci
Volume:116
Issue / Number:Pt 19
Start Page:3879
End Page:3891
Review Status:not specified
Audience:Not Specified
Abstract / Description:Tight junctions play a central role in the establishment of cell polarity in vertebrate endothelial and epithelial cells. A ternary protein complex consisting of the cell polarity proteins PAR-3 and PAR-6 and the atypical protein kinase C localizes at tight junctions and is crucial for tight junction formation. We have recently shown that PAR-3 directly associates with the junctional adhesion molecule (JAM), which suggests that the ternary complex is targeted to tight junctions of epithelial cells through PAR-3 binding to JAM. The expression of JAM-related proteins by endothelial cells prompted us to test whether recruitment of the ternary complex in endothelial cells can occur through binding to JAM-2, JAM-3, endothelial cell-selective adhesion molecule (ESAM) or coxsackie- and adenovirus receptor (CAR). Here we show that the two JAM-related proteins JAM-2 and JAM-3 directly associate with PAR-3. The association between PAR-3 and JAM-2/-3 is mediated through the first PDZ domain of PAR-3. In agreement with the predominant expression of JAM-2 and JAM-3 in endothelial cells, we found that PAR-3 is expressed by endothelial cells in vivo and is localized at cell contacts of cultured endothelial cells. PAR-3 associates with JAM-2/-3 but not with the JAM-related Ig-superfamily members ESAM or CAR. In addition, we show that the tight junction-associated protein ZO-1 associates with JAM-2/-3 in a PDZ domain-dependent manner. Using ectopic expression of JAM-2 in CHO cells, we show that the junctional localization of JAM-2 is regulated by serine phosphorylation and that its clustering at cell-cell contacts recruits endogenous PAR-3 and ZO-1. Our findings suggest that JAM-2 affects endothelial cell junctions by its regulated clustering at intercellular contacts, and they support a role for JAM-2, and possibly JAM-3, in tight junction formation of endothelial cells.
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für molekulare Biomedizin
Identifiers:URL:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [ID No:1]
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