Bonfils, Grégory Jaquenoud, Malika Bontron, Séverine Ostrowicz, Clemens Ungermann, Christian De Virgilio, Claudio 2012-03-15 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. application/pdf https://folia.unifr.ch/global/documents/302233 https://folia.unifr.ch/documents/302233/files/vir_lts.pdf https://folia.unifr.ch/documents/302233/files/vir_lts_sm.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcel.2012.02.009 info:eu-repo/semantics/openAccess License undefined Molecular Cell. - 2012, vol. 46, no. 1, p. 105–110 info:eu-repo/classification/udc/57 Leucyl-tRNA synthetase controls TORC1 via the EGO complex http://purl.org/coar/resource_type/c_6501