小G蛋白信号调节因子2 (SGSM2)通过与E-cadherin相互作用增强迁移细胞粘附,参与雌激素受体阳性乳腺癌转移。

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC
ACS Applied Electronic Materials Pub Date : 2019-12-01 Epub Date: 2019-02-11 DOI:10.1080/19336918.2019.1568139
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
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引用次数: 9

摘要

小G蛋白信号调节剂(SGSM1/2/3)在癌症中的作用尚不清楚。我们的研究结果表明,SGSM2是一种与E-cadherin/β-catenin强烈相互作用的质膜蛋白。SGSM2下调可增强局灶黏附激酶(FAK)的磷酸化;Y576/577),降低上皮标志物E-cadherin、β-catenin、Paxillin的表达,增加Snail、Twist-1的表达,降低细胞粘附,促进癌细胞迁移。雌激素和纤维连接蛋白治疗可促进SGSM2与磷酸化- fak (Y397)的共定位。BioGRID数据库显示,SGSM2可能与细胞骨架重塑和细胞-细胞连接蛋白相互作用。这些证据表明,SGSM2在肿瘤迁移过程中调节细胞粘附和细胞骨架动力学中起作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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.

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.

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.

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.

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.

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来源期刊
CiteScore
7.20
自引率
4.30%
发文量
567
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