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

Juo Han Lin, Wen Jui Lee, Han Chung Wu, Chih Hsiung Wu, Li Ching Chen, Chi Cheng Huang, Hang Lung Chang, Tzu Chun Cheng, Hui Wen Chang, Chi Tang Ho, Shih Hsin Tu, Yuan Soon Ho

研究成果: 雜誌貢獻文章

摘要

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.
原文英語
期刊Cell Adhesion and Migration
DOIs
出版狀態已發佈 - 一月 1 2019

指紋

Monomeric GTP-Binding Proteins
Cadherins
Cell Adhesion
Estrogen Receptors
Breast Neoplasms
Neoplasm Metastasis
Catenins
Cytoskeleton
Paxillin
Focal Adhesion Protein-Tyrosine Kinases
Neoplasms
Intercellular Junctions
Fibronectins
Cell Movement
Blood Proteins
Estrogens
Membrane Proteins
Down-Regulation
Phosphorylation
Cell Membrane

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology

引用此文

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title = "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",
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.",
keywords = "breast cancer, cell adhesion, E-cadherin, EMT, oestrogen receptor, SGSM",
author = "Lin, {Juo Han} and Lee, {Wen Jui} and Wu, {Han Chung} and Wu, {Chih Hsiung} and Chen, {Li Ching} and Huang, {Chi Cheng} and Chang, {Hang Lung} and Cheng, {Tzu Chun} and Chang, {Hui Wen} and Ho, {Chi Tang} and Tu, {Shih Hsin} and Ho, {Yuan Soon}",
year = "2019",
month = "1",
day = "1",
doi = "10.1080/19336918.2019.1568139",
language = "English",
journal = "Cell Adhesion and Migration",
issn = "1933-6918",
publisher = "Landes Bioscience",

}

TY - JOUR

T1 - 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

AU - Lin, Juo Han

AU - Lee, Wen Jui

AU - Wu, Han Chung

AU - Wu, Chih Hsiung

AU - Chen, Li Ching

AU - Huang, Chi Cheng

AU - Chang, Hang Lung

AU - Cheng, Tzu Chun

AU - Chang, Hui Wen

AU - Ho, Chi Tang

AU - Tu, Shih Hsin

AU - Ho, Yuan Soon

PY - 2019/1/1

Y1 - 2019/1/1

N2 - 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.

AB - 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.

KW - breast cancer

KW - cell adhesion

KW - E-cadherin

KW - EMT

KW - oestrogen receptor

KW - SGSM

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