Leucyl-tRNA Synthetase Controls TORC1 via the EGO Complex

200Citations
Citations of this article
212Readers
Mendeley users who have this article in their library.

Abstract

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. © 2012 Elsevier Inc.

Cite

CITATION STYLE

APA

Bonfils, G., Jaquenoud, M., Bontron, S., Ostrowicz, C., Ungermann, C., & De Virgilio, C. (2012). Leucyl-tRNA Synthetase Controls TORC1 via the EGO Complex. Molecular Cell, 46(1), 105–110. https://doi.org/10.1016/j.molcel.2012.02.009

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free