Journal of Biological Chemistry · 2011 · 45 citations · 34 references
Life SciencesBiochemistryMolecular BiologyMolecular OncologyProtein TranslationSignal TransductionProtein Kinase CascadesProtein SynthesisSignal Transduction In CancerTranslation ControlTranslation RegulationTranslational RegulationImmortalization Of Cancer CellsInternal Ribosome Entry Site (Ires) - Mediated TranslationInternal Ribosome Entry SitesIres-trans-acting FactorsPhospholipase C SignalingRna Translation ControlTranslational ActivationTranslational Control In Cancer
We report that the activation level of AMP-dependent protein kinase AMPK is elevated in cancer cell lines as a hallmark of their transformed state. In OVCAR3 and A431 cells, c-Src signals through protein kinase Cα, phospholipase Cγ, and LKB1 to AMPK. AMPK controls internal ribosome entry site (IRES) dependent translation in these cells. We suggest that AMPK activation via PKC might be a general mechanism to regulate IRES-dependent translation in cancer cells. We report that the activation level of AMP-dependent protein kinase AMPK is elevated in cancer cell lines as a hallmark of their transformed state. In OVCAR3 and A431 cells, c-Src signals through protein kinase Cα, phospholipase Cγ, and LKB1 to AMPK. AMPK controls internal ribosome entry site (IRES) dependent translation in these cells. We suggest that AMPK activation via PKC might be a general mechanism to regulate IRES-dependent translation in cancer cells.
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