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Leucyl-tRNA synthetase controls TORC1 via the EGO complex.

Molecular cell | Apr 13, 2012

http://www.ncbi.nlm.nih.gov/pubmed/22424774

The target of rapamycin complex 1 (TORC1) is an essential regulator of eukaryotic cell growth that responds to growth factors, energy levels, and amino acids. The mechanisms through which the preeminent amino acid leucine signals to the TORC1-regulatory Rag GTPases, which activate TORC1 within the yeast EGO complex (EGOC) or the structurally related mammalian Rag-Ragulator complex, remain elusive. We find that the leucyl-tRNA synthetase (LeuRS) Cdc60 interacts with the Rag GTPase Gtr1 of the EGOC in a leucine-dependent manner. This interaction is necessary and sufficient to mediate leucine signaling to TORC1 and is disrupted by the engagement of Cdc60 in editing mischarged tRNA(Leu). Thus, the EGOC-TORC1 signaling module samples, via the LeuRS-intrinsic editing domain, the fidelity of tRNA(Leu) aminoacylation as a proxy for leucine availability.

Pubmed ID: 22424774 RIS Download

Mesh terms: Leucine | Leucine-tRNA Ligase | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Signal Transduction | Transcription Factors

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