Reuver S M, Garner C C
Department of Neurobiology, University of Alabama at Birmingham, Birmingham, AL 35294-0021, USA.
J Cell Sci. 1998 Apr;111 ( Pt 8):1071-80. doi: 10.1242/jcs.111.8.1071.
Members of the SAP family of synapse-associated proteins have recently emerged as central players in the molecular organization of synapses. In this study, we have examined the mechanism that localizes one member, SAP97, to sites of cell-cell contact. Utilizing epithelial CACO-2 cells and fibroblast L-cells as model systems, we demonstrate that SAP97 is associated with the submembranous cortical cytoskeleton at cell-cell adhesion sites. Furthermore, we show that its localization into this structure is triggered by E-cadherin. Although SAP97 can be found in an E-cadherin/catenin adhesion complex, this interaction seems to be mediated by the attachment of SAP97 to the cortical cytoskeleton. Our results are consistent with a model in which SAP97 is recruited to sites of cell-cell contact via an E-cadherin induced assembly of the cortical cytoskeleton.
突触相关蛋白SAP家族的成员最近已成为突触分子组织中的核心参与者。在本研究中，我们研究了将其中一个成员SAP97定位到细胞间接触位点的机制。利用上皮CACO-2细胞和成纤维细胞L细胞作为模型系统，我们证明SAP97与细胞间粘附位点的膜下皮质细胞骨架相关。此外，我们表明其定位于该结构是由E-钙粘蛋白触发的。虽然可以在E-钙粘蛋白/连环蛋白粘附复合物中发现SAP97，但这种相互作用似乎是由SAP97附着于皮质细胞骨架介导的。我们的结果与一个模型一致，即SAP97通过E-钙粘蛋白诱导的皮质细胞骨架组装被募集到细胞间接触位点。
