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Am J Physiol Cell Physiol 279: C1587-C1594, 2000;
0363-6143/00 $5.00
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Vol. 279, Issue 5, C1587-C1594, November 2000

Amino acid deprivation induces translation of branched-chain alpha -ketoacid dehydrogenase kinase

Christopher B. Doering1 and Dean J. Danner2

2 Department of Genetics, 1 Program in Genetics and Molecular Biology, Emory University School of Medicine, Atlanta, Georgia 30322

Leucine, isoleucine, and valine are used by cells for protein synthesis or are catabolized into sources for glucose and lipid production. These branched-chain amino acids influence proteolysis, hormone release, and cell cycle progression along with their other metabolic roles. The branched-chain amino acids play a central role in regulating cellular protein turnover by reducing autophagy. These essential amino acids are committed to their catabolic fate by the activity of the branched-chain alpha -ketoacid dehydrogenase complex. Activity of the branched-chain alpha -ketoacid dehydrogenase complex is regulated by phosphorylation/inactivation of the alpha -subunit performed by a complex specific kinase. Here we show that elimination of the branched-chain amino acids from the medium of cultured cells results in a two- to threefold increased production of the branched-chain alpha -ketoacid dehydrogenase kinase with a decrease in the activity state of the branched-chain alpha -ketoacid dehydrogenase complex. The mechanism cells use to increase kinase production under these conditions involves recruitment of the kinase mRNA into polyribosomes. Promoter activity and the steady-state concentration of the mRNA are unchanged by these conditions.

posttranscriptional regulation; polyribosomes; regulation of catabolism


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