首页> 外文期刊>Gene: An International Journal Focusing on Gene Cloning and Gene Structure and Function >Zhao, J.-L.a , Liang, S.-Q.a , Fu, W.a b , Zhu, B.-K.a b , Li, S.-Z.a , Han, H.a , Qin, H.-Y.a The LIM domain protein FHL1C interacts with tight junction protein ZO-1 contributing to the epithelial-mesenchymal transition (EMT) of a breast adenocarcinoma cell line
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Zhao, J.-L.a , Liang, S.-Q.a , Fu, W.a b , Zhu, B.-K.a b , Li, S.-Z.a , Han, H.a , Qin, H.-Y.a The LIM domain protein FHL1C interacts with tight junction protein ZO-1 contributing to the epithelial-mesenchymal transition (EMT) of a breast adenocarcinoma cell line

机译:赵J.-La,梁,S.-Qa,傅,Wab,朱,B.-Kab,李,S.-Za,韩,哈,秦,H.-Ya LIM域蛋白FHL1C相互作用紧密连接蛋白ZO-1有助于乳腺癌细胞系上皮-间质转化(EMT)

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摘要

FHL1C is a LIM domain protein that has been implied in transcription regulation through interacting with other proteins, such as RBP-J, the critical transcription factor of the Notch signaling pathway. The LIM domain is a protein-protein interaction interface, suggesting that FHL1C could bind other proteins to enable its functions. In order to explore the interacting proteins with FHL1C, in this study we screened FHL1C-interacting proteins by using immunoprecipitation and mass spectrometric analysis. ZO-1, a member of the Zonula occludens proteins that constitute tight junctions, was sorted out as one candidate by using these techniques. Furthermore, we confirmed the interaction between FHL1C and ZO-1 in cells by using the mammalian two-hybrid assay and the co-immunoprecipitation assay, and verified that ZO-1 could interact with FHL1C through the PDZ domains of ZO-1. Moreover, with immunofluorescence staining, we found that FHL1C could induce ZO-1 translocating into nucleus. With a breast adenocarcinoma cell line MCF7, we showed that the interaction between FHL1C and ZO-1 could contribute to the epithelial-mesenchymal transition (EMT). Taken together, our study might provide new insight into the function of FHL1C on the regulation of EMT in cancer cells.
机译:FHL1C是一种LIM域蛋白,通过与其他蛋白(例如Notch信号通路的关键转录因子RBP-J)相互作用,在转录调控中得到了暗示。 LIM结构域是蛋白质-蛋白质相互作用的界面,表明FHL1C可以结合其他蛋白质以实现其功能。为了探索与FHL1C相互作用的蛋白,在本研究中,我们通过免疫沉淀和质谱分析筛选了与FHL1C相互作用的蛋白。通过使用这些技术,ZO-1是构成紧密连接的Zonula咬合蛋白的成员,被选为一种候选蛋白。此外,我们通过使用哺乳动物双杂交测定和免疫共沉淀测定证实了细胞中FHL1C和ZO-1之间的相互作用,并证实ZO-1可以通过ZO-1的PDZ域与FHL1C相互作用。此外,通过免疫荧光染色,我们发现FHL1C可以诱导ZO-1转运到细胞核中。对于乳腺癌细胞系MCF7,我们显示FHL1C和ZO-1之间的相互作用可能有助于上皮-间质转化(EMT)。综上所述,我们的研究可能为FHL1C在调节癌细胞EMT中的功能提供新的见解。

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