Lysosomal recruitment of TSC2 is a universal response to cellular stress
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mTORC1 promotes cell growth and is therefore inactivated upon unfavourable growth conditions. Signalling pathways downstream of most cellular stresses converge on TSC1/2, which serves as an integration point that inhibits mTORC1. The TSC1/2 complex was shown to translocate to lysosomes to inactivate mTORC1 in response to two stresses: amino-acid starvation and growth factor removal. Whether other stresses also regulate TSC2 localization is not known. How TSC2 localization responds to combinations of stresses and other stimuli is also unknown. We show that both amino acids and growth factors are required simultaneously to maintain TSC2 cytoplasmic; when one of the two is missing, TSC2 relocalizes to lysosomes. Furthermore, multiple different stresses that inhibit mTORC1 also drive TSC2 lysosomal accumulation. Our findings indicate that lysosomal recruitment of TSC2 is a universal response to stimuli that inactivate mTORC1, and that the presence of any single stress is sufficient to cause TSC2 lysosomal localization.
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Overall, the localization of the TSC2 subunit is the main determinant of TSCC-mediated Rheb inhibition.
“Overall, it appears that the localization of the TSC2 subunit is the main determinant of TSCC-mediated Rheb inhibition (Demetriades et al., 2016).”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Demetriades et al., 2016
Whereas specific metabolites signal to mTORC1 through the Rag GTPase axis, stress conditions such as hypoxia, DNA damage stress, ER stress, and growth factor and survival signaling are filtered through to the Rheb GTPase through TSCC by post-translational modification.
“Whereas it appears that specific metabolites signal to mTORC1 through the Rag GTPase axis, stress conditions such as hypoxia, DNA damage stress, ER stress, and growth factor and survival signaling, are filtered through to the Rheb GTPase through TSCC by post-translational modification (Kwiatkowski, 2003; Huang and Manning, 2008; Tomasoni and Mondino, 2011; Demetriades et al., 2016).”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Demetriades et al., 2016
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- Authors
- Demetriades, C., Plescher, M., & Teleman, A. A.
- Affiliations
- German Cancer Research Center (DE)
- Corresponding author
- Demetriades, Constantinos
- Teleman, Aurelio A.
- Venue
- Nature Communications
- Published
- 2016-02-12
- Volume
- 7
- Issue
- 1
- Pages
- 10662-10662
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC4754342
- OpenAlex
- W2257158960
- Cited by
- 160
- References
- 69
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 14 · 2023: 17 · 2022: 18 · 2021: 25 · 2020: 24 · 2019: 14 · 2018: 12 · 2017: 11 · 2016: 10
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- European Commission
- FP7 Ideas: European Research Council (260602)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Physiology › Tuberous Sclerosis Complex Research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- TSC2, mTORC1, cellular stress, amino acid starvation, protein localization, cell growth regulation, TOR signaling
- MeSH terms
- Mechanistic Target of Rapamycin Complex 1, Tuberous Sclerosis Complex 2 Protein, Amino Acids, Animals, Cell Line, Chlorocebus aethiops, Cytoplasm, Fluorescent Antibody Technique, HeLa Cells, Humans, Lysosomes, Stress, Physiological, Blotting, Western, Microscopy, Confocal, COS Cells, Tumor Suppressor Proteins, Intercellular Signaling Peptides and Proteins, NIH 3T3 Cells, Cell Line, Tumor, Multiprotein Complexes, Immunoprecipitation, Mice, Hep G2 Cells, HEK293 Cells, TOR Serine-Threonine Kinases, MCF-7 Cells
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