Leucyl-tRNA synthetase controls TORC1 via the EGO complex

Bonfils, Grégory; Jaquenoud, Malika; Bontron, Séverine; Ostrowicz, Clemens; Ungermann, Christian; De Virgilio, Claudio

doi:10.1016/j.molcel.2012.02.009

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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

15.03.2012

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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 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.

Faculty

Faculté des sciences et de médecine

Department

Département de Biologie

Language