中文摘要：

Periaxin 在哺乳动物的 Schwann 房间和透镜纤维房间被表示，并且为联系细胞骨架的蛋白质在一幅屏幕被识别了。Charcot-Marie-Tooth 4F 被 periaxin 基因的损失或变化引起。也就是， periaxin 基因编码二蛋白质 isoforms L-periaxin 和 S-periaxin。S-periaxin 包含 147 氨基酸残余并且有一个 N 终端 PDZ 领域。在这份报纸， S-periaxin 被报导是通过有它在温和氧化条件下面的 Cys88 和 Cys139 残余的分子间的二硫化物契约的形成的 homodimerized。S-periaxin 更暗淡的共有原子价被西方的污点分析和双分子的荧光互补分析也观察。S-periaxin dimerization 形成能被细胞的氧化还原作用变化调整。这些结果把可能的机制提供给 periaxin 建筑群，复杂稳定性的改进，和在细胞外的矩阵和细胞骨架之间的一个连接的建立的形成。

英文摘要：

Periaxin is expressed in mammalian Schwann cells and lens fiber cells, and has been identified in a screen for cytoskeleton-associated proteins. Charcot-Marie-Tooth 4F is caused by losses or muta- tions of the periaxin gene. The periaxin gene encodes two protein isoforms, namely, L-periaxin and S-periaxin. S-periaxin contains 147 amino acid residues and has an N-terminal PDZ domain. In this paper, S-periaxin was reported to be homodimerized through the formation of intermolecular disulfide bonds with its Cys88 and Cys139 residues under mild oxidation conditions. The covalent dimer of S-periaxin was also observed by western blot analysis and bimolecular fluorescence com- plementation analyses. S-periaxin dimerization formation could be regulated by cellular redox fluc- tuations. These results offer a possible mechanism to the formation of periaxin complexes, improvement of complex stability, and establishment of a link between the extracellular matrix and the cytoskeleton.