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- W2334335968 abstract "Integrin-linked kinase (ILK), PINCH1 and α-parvin form a ternary complex that plays crucial roles in integrins signaling. We report here that mda-9/syntenin is essential for the assembly of integrin β1-ILK-PINCH1-α-parvin signaling complexes during adhesion to collagen-I (COL-1). Modulation of mda-9/syntenin expression affects COL-1-induced activation of protein kinase B (PKB/Akt). mda-9/Syntenin associates with ILK and this association is increased at the plasma membrane in response to COL-1. mda-9/Syntenin regulates COL-1-induced association between ILK and PKB/Akt, and plasma membrane targeting of ILK-PKB/Akt, suggesting that mda-9/syntenin modulates the plasma membrane targeting of PKB/Akt via ILK. Strikingly, inhibition of mda-9/syntenin impairs COL-1-induced plasma membrane translocation of ILK-PINCH1-α-parvin complex and the assembly of integrin β1-ILK-PINCH1-α-parvin signaling complexes. Consistently, inhibition of mda-9/syntenin blocks the COL-1-induced reorganization of actin cytoskeleton and cell migration, as well as activation of Rac1 and ERK1/21/2. Thus, our study defines the role of mda-9/syntenin in COL-1-induced integrin signaling and describes new mechanism of mda-9/syntenin for the regulation of cell migration. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 1486. doi:10.1158/1538-7445.AM2011-1486" @default.
- W2334335968 created "2016-06-24" @default.
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- W2334335968 date "2011-04-15" @default.
- W2334335968 modified "2023-09-27" @default.
- W2334335968 title "Abstract 1486: Mda-9/Syntenin regulates integrin signaling by facilitating membrane translocation of ILK/PINCH1/α-parvin complex" @default.
- W2334335968 doi "https://doi.org/10.1158/1538-7445.am2011-1486" @default.
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