单位：[a]Department of Biochemistry and Molecular Biology, School of Basic Medicine, Capital Medical University, Beijing 100069, P. R. China[b]Cancer Institute of Capital Medical University, Beijing 100069, P. R. China[c]Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Beijing 100069, P. R. China[d]Department of General Surgery, Beijing Friendship Hospital Capital University of Medical Science, Beijing 100050, P. R. China临床科室国家中心普外分中心普外五科（综合普外科）首都医科大学附属北京友谊医院[e]Cardiff-China Medical Research Collaborative, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XN, UK.
Ehm2, which belongs to the FERM superfamily, is a metastasis-associated protein. However, its function in cancer metastasis and the associated molecular mechanism is not definitely clear. Alternative splicing is an important biological step during mRNA processing and has been reported to be related with many diseases including cancers. Ehm2 has two transcript variants. Transcript variant 1(Ehm2/1) encodes isoform 1 of 518 amino acids, while transcript variant 2(Ehm2/2) encodes isoform 2 of 913 amino acids. In this study, we found that Ehm2/1 was the main transcript variant in the MCF-7 breast cancer cell line. Forced expression of Ehm2/1 upregulated the total protein amount but had no effect on the mRNA levels of beta-catenin. The increased beta-catenin was found to be dominantly located at the cell membrane. Meanwhile, knockdown of Ehm2/1 in MCF-7 cells decreased the total protein amount but not the mRNA levels of beta-catenin. Further results showed that Ehm2/1 interacted with beta-catenin and colocalized with it at the cell membrane. E-cadherin, a partner of beta-catenin in cadherin-catenin complexes, was also upregulated by the overexpression of Ehm2/1 and also colocalized with it at the cell membrane. Meanwhile, overexpression of Ehm2/1 inhibited the migration ability of MCF-7 cells. These results suggested that Ehm2/1 may render beta-catenin at the cell membrane by interacting with beta-catenin and E-cadherin.
基金：
Beijing Municipal Science & Technology CommissionBeijing Municipal Science & Technology Commission [Z151100001615039]; Joint Research Fund on Basic and Clinical Medicine from Capital Medical University [12JL14]; Cancer Research Wales; Life Science Research Network Wales (NRN); Ser Cymru
第一作者单位：[a]Department of Biochemistry and Molecular Biology, School of Basic Medicine, Capital Medical University, Beijing 100069, P. R. China[b]Cancer Institute of Capital Medical University, Beijing 100069, P. R. China[c]Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Beijing 100069, P. R. China
通讯作者：
通讯机构：[a]Department of Biochemistry and Molecular Biology, School of Basic Medicine, Capital Medical University, Beijing 100069, P. R. China[b]Cancer Institute of Capital Medical University, Beijing 100069, P. R. China[c]Beijing Key Laboratory for Cancer Invasion and Metastasis Research, Beijing 100069, P. R. China[e]Cardiff-China Medical Research Collaborative, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XN, UK.
推荐引用方式(GB/T 7714)：
Hefen Yu,Zhicheng Ge,Yang Si,et al.The splice variant Ehm2/1 in breast cancer MCF-7 cells interacted with beta-catenin and increased its localization to plasma membrane[J].RSC ADVANCES.2016,6(82):78436-78444.doi:10.1039/c6ra07975j.
APA：
Hefen Yu,Zhicheng Ge,Yang Si,Gang Chen,Yuxiang Zhang&Wen G. Jiang.(2016).The splice variant Ehm2/1 in breast cancer MCF-7 cells interacted with beta-catenin and increased its localization to plasma membrane.RSC ADVANCES,6,(82)
MLA：
Hefen Yu,et al."The splice variant Ehm2/1 in breast cancer MCF-7 cells interacted with beta-catenin and increased its localization to plasma membrane".RSC ADVANCES 6..82(2016):78436-78444
