Turner C E
Department of Anatomy and Cell Biology, SUNY Health Science Center, Syracuse 13210, USA.
Int J Biochem Cell Biol. 1998 Sep;30(9):955-9. doi: 10.1016/s1357-2725(98)00062-4.
Paxillin is a 68 kDa cytoplasmic protein that localizes to discrete sites of cell attachment to the extracellular matrix called focal adhesions. It is a multi-domain adapter protein capable of interacting with several structural and signaling proteins including vinculin, FAK, PYK2, Src and Crk. Phosphorylation of paxillin in response to integrin-mediated cell adhesion and growth factor stimulation regulates some of these interactions. Thus, paxillin functions as a scaffold for the recruitment of molecules into a signal transduction complex that is closely apposed to the plasma membrane. This is likely to facilitate the efficient processing of external stimuli that modulate important cellular events including cell adhesion, cell motility and growth control. Since paxillin interacts with several proteins known to cause cell transformation, the binding sites for these proteins on paxillin represent potential targets for therapeutic agents.
桩蛋白是一种68 kDa的细胞质蛋白，定位于细胞与细胞外基质附着的离散部位，即粘着斑。它是一种多结构域衔接蛋白，能够与包括纽蛋白、粘着斑激酶（FAK）、脯氨酸酪氨酸激酶2（PYK2）、Src和Crk在内的多种结构蛋白和信号蛋白相互作用。响应整合素介导的细胞粘附和生长因子刺激，桩蛋白的磷酸化调节其中一些相互作用。因此，桩蛋白作为一种支架，用于将分子招募到紧密靠近质膜的信号转导复合物中。这可能有助于高效处理调节重要细胞事件（包括细胞粘附、细胞运动和生长控制）的外部刺激。由于桩蛋白与几种已知会导致细胞转化的蛋白质相互作用，这些蛋白质在桩蛋白上的结合位点代表了治疗药物的潜在靶点。
