Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2.

@article{Anthony2004PreservationOL,
  title={Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2.},
  author={Tracy G Anthony and Brent J McDaniel and Rachel L Byerley and Barbara C. McGrath and Douglas R Cavener and Margaret A. McNurlan and Ronald C Wek},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 35},
  pages={
          36553-61
        }
}
In eukaryotic cells, amino acid depletion reduces translation by a mechanism involving phosphorylation of eukaryotic initiation factor-2 (eIF2). Herein we describe that mice lacking the eIF2 kinase, general control nonderepressible 2 (GCN2) fail to alter the phosphorylation of this initiation factor in liver, and are moribund in response to dietary leucine restriction. Wild-type (GCN2(+/+)) and two strains of GCN2 null (GCN2(-/-)) mice were provided a nutritionally complete diet or a diet… CONTINUE READING
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