Leucyl-tRNA Synthetase Controls TORC1 via the EGO Complex

Autor(en): Bonfils, Gregory
Jaquenoud, Malika
Bontron, Severine
Ostrowicz, Clemens
Ungermann, Christian 
De Virgilio, Claudio
Stichwörter: ACTIVATION; AMINO-ACID; Biochemistry & Molecular Biology; CANCER; Cell Biology; EXPRESSION; GROWTH; MTORC1; RAG GTPASES; SACCHAROMYCES-CEREVISIAE; TARGET; YEAST
Erscheinungsdatum: 2012
Herausgeber: CELL PRESS
Journal: MOLECULAR CELL
Volumen: 46
Ausgabe: 1
Startseite: 105
Seitenende: 110
Zusammenfassung: 
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..
ISSN: 10972765
DOI: 10.1016/j.molcel.2012.02.009

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