Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 16, Issue 10, Pages 4992-5003Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-04-0310
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- NIDDK NIH HHS [R01 DK063443, 1R01 DK-63443-01] Funding Source: Medline
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The junctional adhesion molecules (JAMs) have been recently described as interendothelial junctional molecules and as integrin ligands. Here we show that JAM-B and JAM-C undergo heterophilic interaction in cell-cell contacts and that JAM-C is recruited and stabilized in junctional complexes by JAM-B. In addition, soluble JAM-B dissociates soluble JAM-C homodimers to form JAM-B/JAM-C heterodimers. This suggests that the affinity of JAM-C monomers to form dimers is higher for JAM-B than for JAM-C. Using antibodies against JAM-C, the formation of JAM-B/JAM-C heterodimers can be abolished. This liberates JAM-C from its vascular binding partner JAM-B and makes it available on the apical side of vessels for interaction with its leukocyte counterreceptor alpha(M)beta(2), integrin. We demonstrate that the modulation of JAM-C localization in junctional complexes is a new regulatory mechanism for alpha(M)beta(2)-dependent adhesion of leukocytes.
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