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JCS ePress online publication date 18 Jan 2005
doi: 10.1242/jcs.01661

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Research Article

Expression of junctional adhesion molecule-A prevents spontaneous and random motility


Gianfranco Bazzoni*, Paolo Tonetti, Luca Manzi, Maria R. Cera, Giovanna Balconi, and Elisabetta Dejana
* Author for correspondence (e-mail: bazzoni{at}marionegri.it)

Junctional adhesion molecule-A (JAM-A) is a cell-surface glycoprotein that localizes to intercellular junctions and associates with intracellular proteins via PSD95-Dlg-ZO1-binding residues. To define the functional consequences of JAM-A expression, we have produced endothelial cells from JAM-A-deficient mice. We report here that the absence of JAM-A enhanced spontaneous and random motility. In turn, the enhanced motility of JAM-A-negative cells was abrogated either on transfection of exogenous JAM-A or on treatment with inhibitors of glycogen synthase kinase-3{beta} (GSK-3{beta}). In addition, in JAM-A-positive cells, motility was enhanced on inactivation of protein kinase C{zeta} (PKC{zeta}), which is an inhibitor of GSK-3{beta}. Although these findings suggested that JAM-A might inhibit GSK-3{beta}, we found that expression per se of JAM-A did not change the levels of inactive GSK-3{beta}. Thus, JAM-A expression may regulate effectors of motility that are also downstream of the PKC{zeta}/GSK-3{beta} axis. In support of this view, we found that JAM-A absence increased the number of actin-containing protrusions, reduced the stability of microtubules and impaired the formation of focal adhesions. Notably, all the functional consequences of JAM-A absence were reversed either on treatment with GSK-3{beta} inhibitors or on transfection of full-length JAM-A, but not on transfection of a JAM-A deletion mutant devoid of the PSD95-Dlg-ZO1-binding residues. Thus, by regulating cytoskeletal and adhesive structures, JAM-A expression prevents cell motility, probably in a PSD95-Dlg-ZO1-dependent manner.
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