4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway

Article Abstract:

Activity of the serine/threonine kinase Akt/PKB is necessary in cascade of signals that goes toward phosphorylation and inactivating 4E-BP1, a repressor of mRNA translation. PI 3-kinase brings on phosphorylation of 4E-BP1 in a wortmannin- and rapamycin-sensitive way; activated Akt-mediated phosphorylation of 4E-BP1 is wortmannin-resistant and rapamycin-sensitive. It appears that Akt is required for in vivo phosphorylation of 4E-BP1. The PI3-kinase-Akt signaling pathway, together with FRAP/mTOR, brings on phosphorylation of 4E-BP1. 4E-BP1 is phosphorylated by the Akt(PKB) signaling pathway and inactivated by it.

Methods, Proteins, Genetic regulation, Genetic transcription, Transcription (Genetics), Molecular biology, Protein kinases, Phosphorylation

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The deficiency of Akt1 is sufficient to suppress tumor development in [Pten.sup.?-] mice

Article Abstract:

An attempt is made to show the deficiency of Akt1 activity, which is sufficient to dramatically inhibit tumor development in [Pten.sup.?-] mice. It is suggested that even haplodeficiency of Akt1 is sufficient to markedly attenuate the development of high-grade prostrate intraepithelial neoplasia (PIN) and endo metrial carcinoma and also, the findings have vital implications for cancer therapy.

Cancer, Tumor suppressor genes, Intestinal polyps, Structure, Tumour suppressor genes

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Upstream and downstream of mTOR

Article Abstract:

The upstream regulators that activate mammalian Target Of Rapamycin (mTOR) and the downstream targets affecting protein synthesis are described. The contribution of mTOR in the control of cell growth and proliferation, and its relevance to cancer and synaptic plasticity is summarized.

Protein biosynthesis, Mammals, Rapamycin

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