Hagiwara, A., Cornu, M., Cybulski, N., Polak, P., Betz, C., Trapani, F., Terracciano, L., Heim, M.H., Ruegg, M.A. and Hall, M.N. (2012) Hepatic mTORC2 activates glycolysis and lipogenesis through Akt, glucokinase and SREBP1c. Cell Metabolism, 15, 725-738. http://dx.doi.org/10.1016/j.cmet.2012.03.015

has been cited by the following article:

• TITLE: Inhibitory roles of protein kinase B and peroxisome proliferator-activated receptor gamma coactivator on hepatic HMG-CoA reductase promoter activity

  AUTHORS: Gene C. Ness, Jeffrey L. Edelman

  KEYWORDS: In Vivo Electroporation; HMG-CoA Reductase; Insulin; Protein Kinase B; Peroxisome Proliferator-Activated Receptor γ Coactivator; Tristetraprolin

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.10B, September 12, 2013

  ABSTRACT: Since we had previously demonstrated that siRNAs to tristetraprolin (TTP) markedly inhibited insulin stimulation of hepatic HMG-CoA reductase (HMGR) transcription, we investigated the effects of transfecting rat liver with TTP constructs. We found that transfecting diabetic rats with TTP did not increase HMGR transcription but rather led to modest inhibition. We then investigated whether co-transfection with protein kinase B, hepatic form (AKT2), might lead to phosphorylation and result in activation of HMGR transcription. We found that this treatment resulted in near complete inhibition of transcription. Transfection with peroxisome proliferator-activated receptor g coactivator (PGC-1a) also inhibited HMGR transcription. These results show that although TTP is needed for activation of HMGR transcription, it cannot by itself activate this process. AKT2 and PGC-1a, which mediate the activation of gluconeogenic genes by insulin, exert the opposite effect on HMGR.