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- W2007193712 abstract "Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, ILLCRMP-1, a novel isoform of CRMP-1, can promote cancer cell migration, invasion and associates with poor clinical outcome in patients with non-small cell lung cancer (NSCLC). However, the underlying mechanisms for regulation of LCRMP-1 in cancer cell invasiveness remain still obscure. Here, we report that GSK-3β can phosphorylate LCRMP-1 at Thr-628 in consensus sequences and this phosphrylation is crucial for function of LCRMP-1 on filopodia formation and cancer cell invasion. Impediment of Thr-628 phosphorylation attenuates the effects of LCRMP-1 to form filopodia and promote cancer invasion; simultaneously, kinase-dead GSK-3β diminishes regulation of LCRMP-1 on cancer cell invasion. Furthermore, we also found that patients with low-level inactive GSK-3β expression and high-level LCRMP-1 expression have worse overall survival than those with high-level inactive GSK-3β expressions and low-level LCRMP-1 expressions (P< 0.0001). Collectively, these results demonstrate that GSK-3β-dependent phosphorylation of LCRMP-1 provides an important mechanism for regulation of LCRMP-1 on cancer cell invasiveness and clinical outcome.Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 5316. doi:1538-7445.AM2012-5316" @default.
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- W2007193712 date "2012-04-15" @default.
- W2007193712 modified "2023-10-17" @default.
- W2007193712 title "Abstract 5316: GSK3β-dependent phosphorylation of LCRMP-1 is required for filopoda formation and tumor invasion" @default.
- W2007193712 doi "https://doi.org/10.1158/1538-7445.am2012-5316" @default.
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