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mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase
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Cellular sensing of amino acids occurs at the lysosome and is mediated by the vacuolar proton pump.
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“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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Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
Self-citationThe Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773
Self-citationSancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464
Self-citationRheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626
Regulation of TORC1 by Rag GTPases in nutrient response
Kim, E., Goraksha-Hicks, P., Li, L., Neufeld, T. P., & Guan, K.-L. (2008) · Nature Cell Biology · doi:10.1038/ncb1753 · Cited by 1,349
Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00506-2 · Cited by 1,080
Requirement of Prorenin Receptor and Vacuolar H + -ATPase–Mediated Acidification for Wnt Signaling
Cruciat, C.-M., Ohkawara, B., Acebron, S. P., Karaulanov, E., Reinhard, C., Ingelfinger, D., Boutros, M., & Niehrs, C. (2010) · Science · doi:10.1126/science.1179802 · Cited by 516
Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
Peters, C., Bayer, M. J., Bühler, S., Andersen, J., Mann, M., & Mayer, A. (2001) · Nature · doi:10.1038/35054500 · Cited by 501
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Lin, J., Shi, S.-S., Zhang, J., Zhang, Y., Zhang, L., Liu, Y., Jin, P., Wei, P., Shi, R., Zhou, W., et al. (2016) · Small · doi:10.1002/smll.201601903 · Cited by 40
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Chen, Y., Navarrete, M. S., Wang, Y., McClintock, N. C., Sakurai, R., Wang, F., Chen, K. T., Chou, T., Rehan, V. K., Lee, D. J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-68615-w · Cited by 36
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Kingsbury, J. M., Sen, N. D., Maeda, T., Heitman, J., & Cardenas, M. E. (2014) · Genetics · doi:10.1534/genetics.114.161646 · Cited by 33
Zhang, X., Cao, J., Miller, S. P., Jing, H., & Lin, H. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00440 · Cited by 36
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Valenstein, M. L., Lalgudi, P. V., Gu, X., Kedir, J. F., Taylor, M. S., Chivukula, R. R., & Sabatini, D. M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322755121 · Cited by 34
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Duran, J., Salinas, J. E., Wheaton, R. P., Poolsup, S., Allers, L., Rosas‐Lemus, M., Chen, L., Cheng, Q., Pu, J., Salemi, M., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00292-1 · Cited by 35
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Metadata
- 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
- PMC
- PMC3211112
- 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
- green
- www.ncbi.nlm.nih.gov
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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