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Leucyl-tRNA synthetase controls TORC1 via the EGO complex.

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

Authors

  • Bonfils G
  • Jaquenoud M
  • Bontron S
  • Ostrowicz C
  • Ungermann C
  • De Virgilio C

Journal

Molecular cell

Publication Data

April 13, 2012

Associated Grants

None

Mesh Terms

  • Leucine
  • Leucine-tRNA Ligase
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
  • Transcription Factors