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

被引:19
作者
Doering, CB
Danner, DJ
机构
[1] Emory Univ, Sch Med, Dept Genet, Atlanta, GA 30322 USA
[2] Emory Univ, Sch Med, Program Genet & Mol Biol, Atlanta, GA 30322 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2000年 / 279卷 / 05期
关键词
posttranscriptional regulation; polyribosomes; regulation of catabolism;
D O I
10.1152/ajpcell.2000.279.5.C1587
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:C1587 / C1594
页数:8
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