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         headline:A transforming mutation in the pleckstrin homology domain of AKT1 in cancer
         description:Although AKT1 (v-akt murine thymoma viral oncogene homologue 1) kinase is a central member of possibly the most frequently activated proliferation and survival pathway in cancer, mutation of AKT1 has not been widely reported. Here we report the identification of a somatic mutation in human breast, colorectal and ovarian cancers that results in a glutamic acid to lysine substitution at amino acid 17 (E17K) in the lipid-binding pocket of AKT1. Lys 17 alters the electrostatic interactions of the pocket and forms new hydrogen bonds with a phosphoinositide ligand. This mutation activates AKT1 by means of pathological localization to the plasma membrane, stimulates downstream signalling, transforms cells and induces leukaemia in mice. This mechanism indicates a direct role of AKT1 in human cancer, and adds to the known genetic alterations that promote oncogenesis through the phosphatidylinositol-3-OH kinase/AKT pathway. Furthermore, the E17K substitution decreases the sensitivity to an allosteric kinase inhibitor, so this mutation may have important clinical utility for AKT drug development. The AKT/protein kinase B signalling pathway regulates cell proliferation and growth and is involved in cellular processes, including apoptosis and glucose metabolism. While activating mutations in other pathway components have been found, no cancer-activating AKT point mutations were known. But now a mutation in AKT1 has been found in human breast, colorectal and ovarian cancers which activates this kinase by enhancing its membrane association, implicating AKT1 directly in cancer causation. A recurrent mutation found in the akt1 gene has been identified in breast, ovarian and colorectal tumours. The crystal structure of the mutant protein is determined and it is found that the protein displays in increased plasma membrane localization and functions as an oncogene in vitro and in a mouse model for leukaemia.
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      headline:A transforming mutation in the pleckstrin homology domain of AKT1 in cancer
      description:Although AKT1 (v-akt murine thymoma viral oncogene homologue 1) kinase is a central member of possibly the most frequently activated proliferation and survival pathway in cancer, mutation of AKT1 has not been widely reported. Here we report the identification of a somatic mutation in human breast, colorectal and ovarian cancers that results in a glutamic acid to lysine substitution at amino acid 17 (E17K) in the lipid-binding pocket of AKT1. Lys 17 alters the electrostatic interactions of the pocket and forms new hydrogen bonds with a phosphoinositide ligand. This mutation activates AKT1 by means of pathological localization to the plasma membrane, stimulates downstream signalling, transforms cells and induces leukaemia in mice. This mechanism indicates a direct role of AKT1 in human cancer, and adds to the known genetic alterations that promote oncogenesis through the phosphatidylinositol-3-OH kinase/AKT pathway. Furthermore, the E17K substitution decreases the sensitivity to an allosteric kinase inhibitor, so this mutation may have important clinical utility for AKT drug development. The AKT/protein kinase B signalling pathway regulates cell proliferation and growth and is involved in cellular processes, including apoptosis and glucose metabolism. While activating mutations in other pathway components have been found, no cancer-activating AKT point mutations were known. But now a mutation in AKT1 has been found in human breast, colorectal and ovarian cancers which activates this kinase by enhancing its membrane association, implicating AKT1 directly in cancer causation. A recurrent mutation found in the akt1 gene has been identified in breast, ovarian and colorectal tumours. The crystal structure of the mutant protein is determined and it is found that the protein displays in increased plasma membrane localization and functions as an oncogene in vitro and in a mouse model for leukaemia.
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