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首页> 外文OA文献 >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
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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

机译：连接粘附分子（JAM）家族成员JAM-2和JAM-3与细胞极性蛋白PAR-3相关：JAM在内皮细胞极性中的可能作用

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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.
机译：紧密连接在脊椎动物内皮细胞和上皮细胞的细胞极性建立中起关键作用。由细胞极性蛋白PAR-3和PAR-6和非典型蛋白激酶C组成的三元蛋白复合物位于紧密连接处，对于形成紧密连接至关重要。我们最近发现PAR-3直接与连接黏附分子（JAM）缔合，这表明三元复合物通过PAR-3与JAM的结合而靶向上皮细胞的紧密连接。内皮细胞表达JAM相关蛋白促使我们测试内皮细胞中三元复合物的募集是否可以通过与JAM-2，JAM-3，内皮细胞选择性粘附分子（ESAM）或柯萨奇和腺病毒结合而发生受体（CAR）。在这里，我们显示了两个JAM相关蛋白JAM-2和JAM-3与PAR-3直接相关。 PAR-3和JAM-2 / -3之间的关联是通过PAR-3的第一个PDZ域介导的。与JAM-2和JAM-3在内皮细胞中的主要表达相一致，我们发现PAR-3在体内由内皮细胞表达，并位于培养的内皮细胞的细胞接触处。 PAR-3与JAM-2 / -3相关，但与JAM相关的Ig超家族成员ESAM或CAR不相关。此外，我们显示紧密连接相关的蛋白ZO-1以PDZ域依赖的方式与JAM-2 / -3相关。使用JAM-2在CHO细胞中的异位表达，我们显示JAM-2的结合定位受丝氨酸磷酸化的调节，并且其在细胞接触处的聚集招募了内源性PAR-3和ZO-1。我们的发现表明，JAM-2通过其在细胞间接触处的调控簇影响内皮细胞连接，并且它们支持JAM-2，甚至可能是JAM-3在内皮细胞紧密连接的形成中的作用。

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