Journal article

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Leucyl-tRNA synthetase controls TORC1 via the EGO complex

  • Bonfils, Grégory Department of Biology, Division of Biochemistry, University of Fribourg, Switzerland
  • Jaquenoud, Malika Department of Biology, Division of Biochemistry, University of Fribourg, Switzerland
  • Bontron, Séverine Department of Biology, Division of Biochemistry, University of Fribourg, Switzerland
  • Ostrowicz, Clemens Department of Biology and Chemistry, Biochemistry Section, University of Osnabrück, Germany
  • Ungermann, Christian Department of Biology and Chemistry, Biochemistry Section, University of Osnabrück, Germany
  • De Virgilio, Claudio Department of Biology, Division of Biochemistry, University of Fribourg, Switzerland
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    15.03.2012
Published in:
  • Molecular Cell. - 2012, vol. 46, no. 1, p. 105–110
English 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 tRNALeu. Thus, the EGOC-TORC1 signaling module samples, via the LeuRS-intrinsic editing domain, the fidelity of tRNALeu aminoacylation as a proxy for leucine availability.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/302233
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