我们证实了p120ctn能与Kaiso结合并携带其出核，解除Kaiso的转录抑制作用。有报道指出Glis2是p120ctn另一核内结合配体，且二者的结合位点同p120ctn与Kaiso的结合位点存在部分重叠，我们转染Glis2可促进p120ctn在核内聚集，我们推测:Glis2能与Kaiso竞争性结合p120ctn，且结合后封闭了p120ctn的出核序列，使其在核内蓄积，从而阻碍了p120ctn-Kaiso途径，发挥肿瘤抑制因子的功能。我们拟通过转染Glis2、NLS突变的Glis2、与p120ctn结合位点突变的Glis2和与Glis2结合位点突变的p120ctn等质粒，利用荧光共聚焦、核/浆抽提、IP、ChIP和成瘤实验等方法，验证和揭示Glis2参与调控p120ctn-Kaiso通路的分子机制，进一步丰富对p120ctn信号分子功能的认识，为肺癌防治提供新的治疗靶点及理论和实验依据。

We confirmed that p120ctn could combine with Kaiso and carry it out of cell nucleus in our previous studies. However, the detailed regulatory mechanisms of the p120ctn-Kaiso signaling pathway remain unclear. Glis2 is another binding ligand of p120ctn, and the binding sites of Glis2 with p120ctn partially overlap with the p120ctn-Kaiso interaction domain. Our results showed Glis2 could promote the aggregation of p120ctn in nucleus. We speculate that Glis2 can compete with Kaiso for binding p120ctn and block the nuclear export-signal which in turn promotes the the nuclear accumulation of p120ctn. Thus Glis2 might function as a tumor suppressor by impeding the p120ctn-Kaiso signaling pathway. We intend to transfect A549 and SPC with Glis2, mNLS-Glis2, p120ctn-mGlis2 and Glis2-mp120ctn, and perform confocal immunofluorescence microscopy, nuclear/cytoplasm protein extraction, IP, ChIP, nude mouse xenograft model to validate and reveal the molecular regulatory mechanisms of p120ctn-Kaiso pathway by Glis2, and enrich our understanding of the function of p120ctn, which could provide new therapeutic targets, and theoretical and experimental evidence for the treatment and prevention of lung cancer.