Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y
Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan.
J Cell Biol. 1999 May 3;145(3):539-49. doi: 10.1083/jcb.145.3.539.
We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin-based cell-cell AJs in various tissues and cell lines. In E-cadherin-expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin-based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word "necto" meaning "to connect").
我们分离出一种新的肌动蛋白丝结合蛋白，命名为afadin，它定位于各种组织和细胞系中基于钙黏着蛋白的细胞间黏附连接（AJs）。Afadin有一个PDZ结构域、三个富含脯氨酸的区域和一个肌动蛋白丝结合结构域。我们在此发现，afadin直接与免疫球蛋白超家族的一个成员相互作用，该成员最初作为由PRR1和PRR2组成的脊髓灰质炎病毒受体相关蛋白（PRR）家族被分离出来，最近被鉴定为α疱疹病毒受体。PRR有一个COOH末端共有基序，afadin的PDZ结构域与之结合。PRR和afadin在各种组织和细胞系中基于钙黏着蛋白的细胞间AJs处共定位。在表达E-钙黏着蛋白的EL细胞中，PRR通过与afadin相互作用被募集到基于钙黏着蛋白的细胞间AJs处。PRR表现出不依赖Ca2+的细胞间黏附活性。这些结果表明，PRR是免疫球蛋白超家族的一种细胞间黏附分子，它通过与afadin相互作用被募集到基于钙黏着蛋白的细胞间AJs处。我们将PRR重新命名为nectin（源自拉丁语“necto”，意为“连接”）。
