The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Upstream and downstream of mTOR
Open accessAbstract
The evolutionarily conserved checkpoint protein kinase, TOR (target of rapamycin), has emerged as a major effector of cell growth and proliferation via the regulation of protein synthesis. Work in the last decade clearly demonstrates that TOR controls protein synthesis through a stunning number of downstream targets. Some of the targets are phosphorylated directly by TOR, but many are phosphorylated indirectly. In this review, we summarize some recent developments in this fast-evolving field. We describe both the upstream components of the signaling pathway(s) that activates mammalian TOR (mTOR) and the downstream targets that affect protein synthesis. We also summarize the roles of mTOR in the control of cell growth and proliferation, as well as its relevance to cancer and synaptic plasticity.
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“This pathway is an important regulator of cell proliferation and metabolism (Hay and Sonenberg, 2004; Guertin and Sabatini, 2007).”
From Efficient genetic editing of human intestinal organoids using ribonucleoprotein-based CRISPR (2023) · cites this paper as Hay and Sonenberg, 2004
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“In the brain, mTORC1 tightly coordinates different synaptic plasticities -long-term potentiation (LTP) and long-term depression (LTD) -the molecular correlates of learning and memory (2)(3)(4)(5).”
From Analysis of proteins that rapidly change upon mechanistic/mammalian target of rapamycin complex 1 (mTORC1) repression identifies parkinson protein 7 (PARK7) as a novel protein aberrantly expressed in tuberous sclerosis complex (TSC) (2016) · cites this paper as [4]
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Citations
Cites
Targeting HIF-1 for cancer therapy
Semenza, G. L. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1187 · Cited by 6,717
Rheb 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
Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00636-6 · Cited by 1,886
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
Self-citationPhosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling
Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., & Chen, J. (2001) · Science · doi:10.1126/science.1066015 · Cited by 1,055
Majumder, P. K., Febbo, P. G., Bikoff, R., Berger, R., Xue, Q., McMahon, L. M., Manola, J., Brugarolas, J., McDonnell, T. J., Golub, T. R., et al. (2004) · Nature Medicine · doi:10.1038/nm1052 · Cited by 964
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Self-citationIsolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells
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RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.
Chiu, M. I., Katz, H., & Berlin, V (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12574 · Cited by 481
Castro, A. F., Rebhun, J. F., Clark, G. J., & Quilliam, L. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300226200 · Cited by 381
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Shumway, S. D., Li, Y., & Xiong, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200499200 · Cited by 74 · cited 1×
“In contrast, other studies showed that 14–3–3 proteins bind to other sites that were not phosphorylated by Akt (Li et al. 2002; Shumway et al. 2003).”
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200 of 203 shown
Cited by
Sorted by citations
TOR signaling in growth and metabolism
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Thoreen, C. C., Chantranupong, L., Keys, H. R., Wang, T., Gray, N. S., & Sabatini, D. M. (2012) · Nature · doi:10.1038/nature11083 · Cited by 1,477
Metadata
- Authors
- Hay, N., & Sonenberg, N.
- Affiliations
- University of Illinois Chicago (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-08-15
- Volume
- 18
- Issue
- 16
- Pages
- 1926-1945
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2129585918
- Cited by
- 4,181
- References
- 13
- Citations by year
- 2026: 40 · 2025: 75 · 2024: 94 · 2023: 144 · 2022: 145 · 2021: 188 · 2020: 208 · 2019: 184 · 2018: 216 · 2017: 219 · 2016: 249 · 2015: 265 · 2014: 280 · 2013: 274 · 2012: 284
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@McGill (McGill) (submittedVersion, cc-by-nc)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- mTOR, TOR signaling, protein synthesis regulation, cell growth, cell proliferation, downstream targets, phosphorylation, cancer, synaptic plasticity
- MeSH terms
- Animals, Cell Division, Energy Metabolism, Growth Substances, Neoplasms, Peptide Initiation Factors, Phosphorylation, Protein Kinases, Transcription, Genetic, Protein Biosynthesis, Ribosomal Protein S6 Kinases, TOR Serine-Threonine Kinases
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