HETEROTYPIC AND HOMOTYPIC ASSOCIATIONS BETWEEN EZRIN AND MOESIN, 2 PUTATIVE MEMBRANE CYTOSKELETAL LINKING PROTEINS
HETEROTYPIC AND HOMOTYPIC ASSOCIATIONS BETWEEN EZRIN AND MOESIN, 2 PUTATIVE MEMBRANE CYTOSKELETAL LINKING PROTEINS
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DOI：
10.1073/pnas.90.22.10846
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发表时间：
1993-11-15
影响因子：
11.1
通讯作者：
BRETSCHER, A
中科院分区：
文献类型：
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作者：
GARY, R;BRETSCHER, A
埃兹蛋白和膜突蛋白是富含肌动蛋白的细胞表面结构的组成部分，被认为是膜-细胞骨架连接蛋白。在这里，我们表明，一个稳定的复合物埃兹蛋白和膜突蛋白可以从培养的细胞中分离的免疫沉淀与特异性抗体。这两种蛋白质直接相互作用的能力用印迹覆盖程序证实，其中溶液中的生物素标记的蛋白质与固定的结合伴侣一起孵育。除了异型协会埃兹蛋白和膜突蛋白，同型结合埃兹蛋白埃兹蛋白和膜突蛋白膜突蛋白也证明了在体外。这些结果表明，埃兹蛋白和膜突蛋白可能参与皮质细胞骨架结构的动态方面的机制。
Ezrin and moesin are components of actin-rich cell surface structures that are thought to function as membrane-cytoskeletal linking proteins. Here we show that a stable complex of ezrin and moesin can be isolated from cultured cells by immunoprecipitation with specific antibodies. The capacity of these two proteins to interact directly was confirmed with a blot-overlay procedure in which biotin-tagged proteins in solution were incubated with immobilized binding partners. In addition to the heterotypic association of ezrin and moesin, homotypic binding of ezrin to ezrin and of moesin to moesin was also demonstrated in vitro. These results suggest mechanisms by which ezrin and moesin might participate in dynamic aspects of cortical cytoskeletal structure.