Abstract
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.
Original language | English |
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Pages (from-to) | 120-137 |
Number of pages | 18 |
Journal | Cell Adhesion and Migration |
Volume | 13 |
Issue number | 1 |
DOIs | |
Publication status | Published - Feb 2019 |
Keywords
- breast cancer
- cell adhesion
- E-cadherin
- EMT
- oestrogen receptor
- SGSM
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
- Cell Biology