GCN2 kinase‐mediated upregulation of ubiquitin C maintains intracellular glutamine level and tRNAGln(CUG) charging under amino acid starvation

Author:

Tsukamoto Yusuke12ORCID,Nakamura Yumi12,Hirata Makoto3,Okuzaki Daisuke4ORCID,Sakate Ryuichi3,Kimura Tomonori1235ORCID

Affiliation:

1. Reverse Translational Research Project National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN) Ibaraki Japan

2. KAGAMI Project National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN) Ibaraki Japan

3. Laboratory of Rare Disease Resource Library National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN) Ibaraki Japan

4. Genome Information Research Center, Research Institute for Microbial Disease Osaka University Suita Japan

5. Department of Nephrology, Graduate School of Medicine Osaka University Suita Japan

Abstract

Each tRNA is aminoacylated (charged) with a genetic codon‐specific amino acid. It remains unclear what factors are associated with tRNA charging and how tRNA charging is maintained. By using the individual tRNA acylation PCR method, we found that the charging ratio of tRNAGln(CUG) reflects cellular glutamine level. When uncharged tRNAGln(CUG) increased under amino acid starvation, the kinase GCN2, which is a key stimulator of the integrated stress response, was activated. Activation of GCN2 led to the upregulation of ubiquitin C (UBC) expression. Upregulated UBC, in turn, suppressed the further reduction in tRNAGln(CUG) charging levels. Thus, tRNA charging is sensitive to intracellular nutrient status and is an important initiator of intracellular signaling.

Funder

Japan Agency for Medical Research and Development

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

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