Cited by 1,673PI3K/AKT/mTOR signaling in cancerAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase

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Zoncu, Roberto, Bar-Peled, Liron, Efeyan, Alejo, Wang, Shuyu, Sancak, Yasemin, Sabatini, David M.·2011·Science

Abstract

Cellular sensing of amino acids occurs at the lysosome and is mediated by the vacuolar proton pump.

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Crossref · 10.1126/science.1207056

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  • The interaction between Ragulator and the Rag heterodimers has been suggested to be dependent on the v-ATPase, which is thought to transmit intra-lysosomal amino acid signals to the Rags by affecting Ragulator GEF activity.

    “The interaction between Ragulator and the Rag heterodimers has been suggested to be dependent on the v-ATPase (Zoncu et al., 2011), which is thought to transmit intra-lysosomal amino acid signals to the Rags by affecting Ragulator GEF activity.”

    From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Zoncu et al., 2011

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  1. [20]Hurtado-Lorenzo A Nat Cell Biol 2006 Feb 8 124 16415858

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Authors
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M.
Affiliations
  • Broad Institute (US)
  • Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.
  • Whitehead Institute for Biomedical Research (US)
Corresponding author
Sabatini, David M.
Venue
Science
Published
2011-11-04
Volume
334
Issue
6056
Pages
678-683
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2111607026
Cited by
1,673
References
26
Citations by year
2026: 72 · 2025: 78 · 2024: 75 · 2023: 104 · 2022: 98 · 2021: 141 · 2020: 130 · 2019: 113 · 2018: 135 · 2017: 127 · 2016: 139 · 2015: 153 · 2014: 120 · 2013: 114 · 2012: 70
FWCI
39.82
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-sa)
  • PMC
Funders
  • Howard Hughes Medical Institute
  • National Cancer Institute (CA103866, R01CA103866, R01CA129105)
  • National Institute of General Medical Sciences (T32GM007753)
  • National Institute of Allergy and Infectious Diseases (R37AI047389, AI47389), R01AI047389)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords
mTORC1, amino acid sensing, vacuolar H+-ATPase, Rag GTPases, lysosomal translocation, inside-out signaling, ATP hydrolysis, cell growth regulation
MeSH terms
Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Cell Line, Drosophila, Humans, Lysosomes, Proteins, Signal Transduction, GTP Phosphohydrolases, Vacuolar Proton-Translocating ATPases, RNA Interference, Multiprotein Complexes, TOR Serine-Threonine Kinases

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