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- W2078161202 abstract "Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, ILGlycine N-methyltransferase (GNMT) is a tumor suppressor for hepatocellular carcinoma (HCC). Previously, we reported that GNMT regulates mTOR signaling pathway through interacting with an mTOR binding protein-DEPTOR. Sequence blasting and phylogenetic analysis demonstrated that the first DEP domain of DEPTOR clustered with P-Rex2, a regulator of the small guanosine triphosphatase Rac. Since P-Rex2 has been showed to be able to antagonize PTEN in PI3K pathway, the aims of this study was to analyze the interaction between GNMT and P-Rex2 and their association in PI3K-Akt signaling pathway. Gel filtration assay demonstrated that GNMT and P-Rex2 were eluted in the same fractions. Reciprocal co-immunoprecipitation experiments demonstrated that GNMT interacts with different domains of P-Rex2 including DH, PH, PDZ and InsPx4-Phosphatase. Overexpression of P-Rex2 enhanced Akt activation in HCC cell line as well as in breast cancer cell lines and such effect was blocked by over-expression of GNMT. Pulse-chase experiments showed that overexpression of GNMT caused significant reduction of the half-life of P-Rex2 from 15 hr to 9.5 hr. Finally, overexpression of GNMT in HuH-7 cells resulted in a proteasome-dependent degradation of P-Rex2. Therefore, GNMT affects PI3K-Akt pathway via direct binding with P-Rex2 and enhance its degradation.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 2234. doi:1538-7445.AM2012-2234" @default.
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- W2078161202 date "2012-04-15" @default.
- W2078161202 modified "2023-09-22" @default.
- W2078161202 title "Abstract 2234: Activation of PI3K pathway by P-Rex2 is inhibited by GNMT" @default.
- W2078161202 doi "https://doi.org/10.1158/1538-7445.am2012-2234" @default.
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