HIF-independent role of prolyl hydroxylases in the cellular response to amino acids

Durán, R V, MacKenzie, E D, Boulahbel, H, Frezza, C, Heiserich, L, Tardito, S, Bussolati, O, Rocha, S +2 more·2013·Oncogene
DOI 10.1038/onc.2012.465

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    mTORC1 is recruited to the lysosome surface in amino acid-rich conditions. Rag guanosine triphosphatase (GTPase) heterodimers found on the lysosomes are the key players in the translocation of mTORC1 to the lysosome membrane by amino acids. In mammals, four Rag GTPase have been found, namely RagA, RagB, RagC, and RagD [53,54]. Unlike other small GTPases, Rag GTPases have no lipid anchor and they form a heterodimer that comprises RagA or RagB with either RagC or RagD. The GTP or GDP states in Rags are regulated by amino acids. RagA/B binds to GDP and RagC/D binds to GTP in amino acid-depleted conditions, whereas RagA/B binds to GTP and RagC/D binds to GDP in amino acid-rich conditions, the latter state being the active state of the Rag heterodimer. The active Rag heterodimer binds with Raptor in mTORC1, thereby leading to the localization of mTROC1 to the lysosome membrane [53]. Rag GTPases lack a lipid anchor; hence et al. · 2015 · Integrative Food Nutrition and Metabolism
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