Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial Caco-2 cells
Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial Caco-2 cells
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DOI：
10.1074/jbc.m006991200
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发表时间：
2001-03-23
影响因子：
4.8
通讯作者：
Bazzoni, G
中科院分区：
文献类型：
--
作者：
Martínez-Estrada, OM;Villa, A;Bazzoni, G
我们在这里报道了连接黏附分子(JAM)与钙/钙调蛋白依赖的丝氨酸蛋白激酶(CASK)的相互作用，CASK是一种与膜相关的鸟苷晚期激酶相关的蛋白质。在Caco-2细胞中，JAM和CASK共沉淀，并沿质膜侧面的细胞间接触处共定位。JAM与CASK的结合需要CASK的PSD95/DLG/ZO-1(PDZ)结构域和JAM细胞质尾部可能的PDZ结合基序Phe-Leu-Val(COOH)。这两个蛋白质在连接定位上的时间解离表明，与CAASK的关联不是将JAM重新招募到细胞间连接所必需的。与成熟的细胞间接触相比，连接组装的特点是提高了木桶在Triton X-100中的溶解度，减少了Triton不溶性果酱-木桶复合体的数量。我们认为，当CASK部分从细胞骨架结合中释放出来时，在连接组装过程中，JAM与CAASK的结合是被调制的。
We report here that junctional adhesion molecule (JAM) interacts with calcium/calmodulin-dependent serine protein kinase (CASK), a protein related to membrane-associated guanylate kinases. In Caco-2 cells, JAM and CASK were coprecipitated and found to colocalize at intercellular contacts along the lateral surface of the plasma membrane. Association of JAM with CASK requires the PSD95/dlg/ZO-1 (PDZ) domain of CASK and the putative PDZ-binding motif Phe-Leu-Val(COOH) in the cytoplasmic tail of JAM. Temporal dissociation in the junctional localization of the two proteins suggests that the association with CASK is not required for recruiting JAM to intercellular junctions. Compared with mature intercellular contacts, junction assembly was characterized by both enhanced solubility of CASK in Triton X-100 and reduced amounts of Triton-insoluble JAM-CASK complexes. We propose that JAM association with CASK is modulated during junction assembly, when CASK is partially released from its cytoskeletal associations.