α-Parvin promotes breast cancer progression and metastasis through interaction with G3BP2 and regulation of TWIST1 signaling

Oncogene
Ying SunChuanyue Wu

Abstract

Identification of molecular alterations driving breast cancer progression is critical for the development of effective therapy. In this study, we show that the level of α-parvin is elevated in triple-negative breast cancer cells. The depletion of α-parvin from triple-negative breast cancer cells effectively inhibits breast cancer cell growth, migration, and invasion in vitro, and tumor progression and metastasis in vivo. At the molecular level, we identify Ras-GTPase-activing protein SH3-domain-binding protein 2 (G3BP2) as an α-parvin-binding protein. Knockdown of α-parvin promotes G3BP2 interaction with TWIST1, increases ubiquitination and proteasome-dependent degradation of TWIST1, and consequently reduces the cellular level of TWIST1 and its downstream signaling. Importantly, the depletion of G3BP2 reverses the reduction in the level and signaling of TWIST1 and the suppression of breast cancer progression induced by the loss of α-parvin. Furthermore, the re-expression of an α-parvin mutant in which the G3BP2-binding site is ablated, unlike that of wild-type α-parvin, in α-parvin-deficient breast cancer cells, is unable to restore the level and signaling of TWIST1 and promote breast cancer progression. Finally, we show that p...Continue Reading

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Methods Mentioned

BETA
bioluminescence imaging
co-immunoprecipitation
immunoprecipitation
pull down
pulldown
co-IP
transfection
ubiquitination
proximity ligation
proximity ligation assay

Software Mentioned

GraphPad
Elements F
Pro Plus
NIS
OriginPro
Prism
Living Image Acquisition and Analysis
Image
Leica X

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