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

• Published in: Cell adhesion & migration Vol. 13; no. 1; pp. 121 - 138
• Main Authors: Lin, Juo-Han, Lee, Wen-Jui, Wu, Han-Chung, Wu, Chih-Hsiung, Chen, Li-Ching, Huang, Chi-Cheng, Chang, Hang-Lung, Cheng, Tzu-Chun, Chang, Hui-Wen, Ho, Chi-Tang, Tu, Shih-Hsin, Ho, Yuan-Soon
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01.01.2019; Taylor & Francis Group
• Subjects: breast cancer; cell adhesion; E-cadherin; EMT; oestrogen receptor; SGSM; SGSM; breast cancer; oestrogen receptor; E-cadherin; EMT; cell adhesion
• ISSN: 1933-6918; 1933-6926; 1933-6926
• DOI: 10.1080/19336918.2019.1568139

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.