Tanaka T, Yamaguchi R, Sabe H, Sekiguchi K, Healy J M
Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
FEBS Lett. 1996 Dec 9;399(1-2):53-8. doi: 10.1016/s0014-5793(96)01280-x.
Short cytoplasmic domains of integrin heterodimers are crucial for transduction of signals generated by adhesion of cells to the extracellular matrix. Here, we describe the use of peptides mimicking the intracellular tails of integrin alpha5beta1 to assay in vitro associations with cytoskeletal proteins. Our results suggest that the focal adhesion protein, paxillin, may interact directly with the intracellular region of the integrin beta1 subunit. Paxillin is known to form stable complexes with several signaling molecules, including focal adhesion kinase. Physical interaction between paxillin and the beta1 cytoplasmic domain suggests a model in which paxillin may function as a key intermediary in integrin-mediated signal transduction.
整合素异二聚体的短细胞质结构域对于细胞与细胞外基质黏附所产生信号的转导至关重要。在此，我们描述了使用模拟整合素α5β1细胞内尾巴的肽来检测与细胞骨架蛋白的体外结合。我们的结果表明，黏着斑蛋白桩蛋白可能直接与整合素β1亚基的细胞内区域相互作用。已知桩蛋白可与包括黏着斑激酶在内的几种信号分子形成稳定复合物。桩蛋白与β1细胞质结构域之间的物理相互作用提示了一种模型，即桩蛋白可能在整合素介导的信号转导中作为关键中间体发挥作用。
