The coordinate regulation of the p53 and mTOR pathways in cells
Open accessAbstract
Cell growth and proliferation requires an intricate coordination between the stimulatory signals arising from nutrients and growth factors and the inhibitory signals arising from intracellular and extracellular stresses. Alteration of the coordination often causes cancer. In mammals, the mTOR (mammalian target of rapamycin) protein kinase is the central node in nutrient and growth factor signaling, and p53 plays a critical role in sensing genotoxic and other stresses. The results presented here demonstrate that activation of p53 inhibits mTOR activity and regulates its downstream targets, including autophagy, a tumor suppression process. Moreover, the mechanisms by which p53 regulates mTOR involves AMP kinase activation and requires the tuberous sclerosis (TSC) 1/TSC2 complex, both of which respond to energy deprivation in cells. In addition, glucose starvation not only signals to shut down mTOR, but also results in the transient phosphorylation of the p53 protein. Thus, p53 and mTOR signaling machineries can cross-talk and coordinately regulate cell growth, proliferation, and death.
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p53 activation is able to inhibit the activity of mTOR through a pathway involving the subsequent activation of TSC1 and TSC2.
“Furthermore, reports showed that p53 activation is able to inhibit the activity of mTOR through a pathway involving the subsequent activation of TSC gene products TSC1 and TSC2, which are tumour suppressors and negative regulators of mTOR [78, 103–105].”
From PKR, the double stranded RNA‐dependent protein kinase as a critical target in Alzheimer's disease (2009) · cites this paper as [105]
AMPK, which p53 activates by direct activation of PRKAB1, blocks the mammalian target of rapamycin (mTOR) pathway, and leads to autophagy.
“AMPK, which p53 activates by direct activation of PRKAB1, blocks the mammalian target of rapamycin (mTOR) pathway, and leads to autophagy.201, 210”
From Census and evaluation of p53 target genes (2017) · cites this paper as [210]
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- Authors
- Feng, Z., Zhang, H., Levine, A. J., & Jin, S.
- Affiliations
- Institute for Advanced Study (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2005-05-31
- Volume
- 102
- Issue
- 23
- Pages
- 8204-8209
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1142118
- OpenAlex
- W2042461504
- Cited by
- 1,235
- References
- 33
- Citations by year
- 2026: 14 · 2025: 23 · 2024: 28 · 2023: 54 · 2022: 59 · 2021: 59 · 2020: 57 · 2019: 57 · 2018: 64 · 2017: 57 · 2016: 60 · 2015: 83 · 2014: 66 · 2013: 82 · 2012: 98
- FWCI
- 17.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- p53, mTOR signaling, AMP kinase, TSC1/TSC2 complex, autophagy, glucose deprivation, energy deprivation, nutrient signaling, growth factor signaling, p53 phosphorylation, tumor suppression, cell growth and proliferation, stress signaling, signaling crosstalk
- MeSH terms
- Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Animals, Autophagy, Enzyme Activation, Fibroblasts, Glucose, Multienzyme Complexes, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphoserine, Protein Kinases, Repressor Proteins, RNA, Messenger, Signal Transduction, Up-Regulation, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Tumor Suppressor Proteins, Multiprotein Complexes, PTEN Phosphohydrolase, Mice, AMP-Activated Protein Kinases, TOR Serine-Threonine Kinases
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