Identification and classification of shuttle protein in and out of nuclei

核蛋白胸腺肽原α(ProTα)是一种内源性的坏死和凋亡抑制因子，具有多种功能。我们已经发现，Protα是通过非囊泡方式从缺血应激的神经元和星形胶质细胞中释放出来的，并通过抗坏死机制发挥着独特的神经保护作用。此前，我们发现，在一些细胞中，释放的Protα再次向细胞核过渡。在本研究中，我们对Protα胞外释放和重新定位过程中的Protα结合蛋白进行了全面的鉴定，并进行了体外和基于细胞的蛋白质相互作用分析。最终，我们成功地鉴定了非囊泡释放相关蛋白、细胞核中的Protα结合蛋白和新的细胞膜受体。此外，我们还利用Cell Illustrator软件对Protα自我防御作用中涉及的机械变化进行了模拟，得到了与实验工作类似的结果。

The nuclear protein prothymosin-α(ProTα), which possesses multi-function is an intrinsic inhibitor of necrosis and apoptosis. We have already revealed that ProTαis released from neurons and astrocytes on ischemic stress through non-vesicular manner and exerts a unique form of neuroprotection through an anti-necrotic mechanism. Previously, we found out that released ProTαonce again makes the transition to the nucleus in some cells. In this study, we comprehensively identified the ProTα-binding proteins in process of extracellular release and re-nuclear localization of ProTα, and performed protein-protein interaction analysis in in vitro and cell-based assay. Finally, we succeeded the identification of non-vesicular release involved proteins, ProTα-binding proteins in the nucleus and novel cell membrane receptor. In addition, we simulated variation of machineries involved in self-defensive role of ProTαby use of Cell Illustrator software, and obtained the similar result of experimental work.