AMPK phosphosite profiling by label-free mass spectrometry reveals a multitude of mTORC1-regulated substrates
The metabolic kinase AMPK regulates transcription in response to nutrient status. AMPK is highly phosphorylated at position Ser184 in the regulatory beta2-subunit, however it's function is unknown. Our preliminary data indicate AMPK dephosphorylated at beta2-Ser184 has elevated nuclear activity and down-regulates apoptotic pathways in response to environmental insult. Here we compare transcriptomes of HEK293T cells expressing either endogenous level beta2 WT or the non-phosphorylatable mutant beta2-Ser182Ala, to gain insight into functional effects of elevated nuclear AMPK activity Overall design: To investigate alternation in gene expression and cell signalling network between WT and AMPK B2S184A KI of Hek 293T cell using data obtained from RNA-seq from 4 replicates each.