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.
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
- Cell Biology
Lin, J. H., Lee, W. J., Wu, H. C., Wu, C. H., Chen, L. C., Huang, C. C., Chang, H. L., Cheng, T. C., Chang, H. W., Ho, C. T., Tu, S. H., & Ho, Y. S. (2019). Small G protein signalling modulator 2 (SGSM2) is involved in oestrogen receptor-positive breast cancer metastasis through enhancement of migratory cell adhesion via interaction with E-cadherin. Cell Adhesion and Migration. https://doi.org/10.1080/19336918.2019.1568139