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
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 29055
- DOI 10.1016/j.molcel.2012.02.009
- Persistent URL
- https://folia.unifr.ch/unifr/documents/302233
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