The function of small G protein signalling modulators (SGSM1/2/3) in cancer remains unknown. Our findings demonstrated that SGSM2 is a plasma membrane protein that strongly interacted with E-cadherin/β-catenin. SGSM2 downregulation enhanced the phosphorylation of focal adhesion kinase (FAK; Y576/577), decreased the expression of epithelial markers such as E-cadherin, β-catenin, and Paxillin, and increased the expression of Snail and Twist-1, which reduced cell adhesion and promoted cancer cell migration. Oestrogen and fibronectin treatment was found to promote the colocalization of SGSM2 at the leading edge with phospho-FAK (Y397). The BioGRID database showed that SGSM2 potentially interacts with cytoskeleton remodelling and cell-cell junction proteins. These evidences suggest that SGSM2 plays a role in modulating cell adhesion and cytoskeleton dynamics during cancer migration.

中文翻译：

---

小G蛋白信号调节剂2（SGSM2）通过与E-钙粘蛋白的相互作用增强迁移细胞粘附，从而参与雌激素受体阳性的乳腺癌转移。

小G蛋白信号调节剂（SGSM1 / 2/3）在癌症中的功能仍然未知。我们的发现表明，SGSM2是与E-cadherin /β-catenin强烈相互作用的质膜蛋白。SGSM2下调增强了黏着斑激酶（FAK; Y576 / 577）的磷酸化，降低了E-cadherin，β-catenin和Paxillin等上皮标志物的表达，并增加了Snail和Twist-1的表达，从而减少了细胞粘附并促进癌细胞迁移。发现雌激素和纤连蛋白处理促进了SGSM2在与磷酸FAK（Y397）前沿的共定位。BioGRID数据库显示，SGSM2可能与细胞骨架重塑和细胞间连接蛋白相互作用。