The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
By Y. Sancak, Timothy R. Peterson, Yoav D. Shaul, Robert A Lindquist, C. Thoreen, L. Bar-Peled, David M. Sabatini. Science, 2008
2,809 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/68c7a377260377ab6cf5da6fb56a60ed7da57c32
How researchers see this paper
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In Cell Biology
- David M. Sabatini
- Michael N. Hall
- M. Laplante
- Asier González González
- L. Bar-Peled
- R. A. Saxton
- K. Guan
- Young Chul Kim
In Molecular Biology
- David M. Sabatini
- M. Laplante
- Michael N. Hall
- K. Guan
- R. A. Saxton
- Asier González González
- L. Bar-Peled
- Young Chul Kim
Citations in the corpus
- MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB (2012, background): “This amino acid-dependent recruitment requires Rag GTPases and LAMTOR, a scaffolding complex that comprises the LAMTOR1/2/3 proteins and anchors the Rag GTPases to the lysosome.(25,26) Importantly, TFEB was capable to co-immunoprecipitate several components of the endogenous LAMTOR/RRAG/MTORC1 compl”
- TFEB at a glance (2016, background): “In the presence of nutrients, a mechanism involving the v-ATPase complex promotes the activation of the small Rag (Ras-related GTP-binding) GTPases, which recruit mTORC1 to the lysosomal membrane, thus promoting its activation through the small GTPase Rheb (Sancak et al., 2010, 2008; Zoncu et al., 2”
- Regulation of Immune Responses by mTOR (2011, background): “Although growth factor–induced activation of RHEB is essential for mTORC1 signaling, mTORC1 activation requires the presence of amino acids (33).”
- Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “The amino acid sensing, however, is mediated by a different pathway that involves the Rag GTPases (785, 1336) and one that requires translocation of the mTORC1 complex to the surface of the lysosomes (1335, 1829).”