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

  • Chi Tang Ho (Contributor)
  • Chih-Hsiung Wu (En Chu Kong Hospital) (Contributor)
  • Hang Lung Chang (Creator)
  • Tzu Chun Cheng (Contributor)
  • Hui-Wen Chang (Creator)
  • Chi Cheng Huang (Contributor)
  • Wen Jui Lee (Contributor)
  • Yuan-Soon Ho (Contributor)
  • Juo Han Lin (Contributor)
  • Han Chung Wu (Contributor)
  • Shih-Hsin Tu (Contributor)
  • Li-Ching Chen (Contributor)



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.
Date made available2019
PublisherTaylor & Francis

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