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Biomolecules 2017, 7(3), 48;

The Architecture of the Rag GTPase Signaling Network

Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland
Novartis Institutes for Biomedical Research, NIBR, Novartis Pharma AG, 4002 Basel, Switzerland
Author to whom correspondence should be addressed.
Academic Editors: Kazuhiro Shiozaki and Ted Powers
Received: 23 May 2017 / Revised: 22 June 2017 / Accepted: 27 June 2017 / Published: 30 June 2017
(This article belongs to the Special Issue TOR Signaling Pathway)
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The evolutionarily conserved target of rapamycin complex 1 (TORC1) couples an array of intra- and extracellular stimuli to cell growth, proliferation and metabolism, and its deregulation is associated with various human pathologies such as immunodeficiency, epilepsy, and cancer. Among the diverse stimuli impinging on TORC1, amino acids represent essential input signals, but how they control TORC1 has long remained a mystery. The recent discovery of the Rag GTPases, which assemble as heterodimeric complexes on vacuolar/lysosomal membranes, as central elements of an amino acid signaling network upstream of TORC1 in yeast, flies, and mammalian cells represented a breakthrough in this field. Here, we review the architecture of the Rag GTPase signaling network with a special focus on structural aspects of the Rag GTPases and their regulators in yeast and highlight both the evolutionary conservation and divergence of the mechanisms that control Rag GTPases. View Full-Text
Keywords: Rag GTPases; EGO complex; target of rapamycin complex 1 (TORC1); amino acid signaling; budding yeast; SEACIT; SEACAT; Lst4–Lst7 Rag GTPases; EGO complex; target of rapamycin complex 1 (TORC1); amino acid signaling; budding yeast; SEACIT; SEACAT; Lst4–Lst7

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Nicastro, R.; Sardu, A.; Panchaud, N.; De Virgilio, C. The Architecture of the Rag GTPase Signaling Network. Biomolecules 2017, 7, 48.

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