The DOI matches its Crossref record; 121 of the 123 references it cites were found in a registry or an index.
TSC1/TSC2 signaling in the CNS
Open accessAbstract
Over the past several years, the study of a hereditary tumor syndrome, tuberous sclerosis complex (TSC), has shed light on the regulation of cellular proliferation and growth. TSC is an autosomal dominant disorder that is due to inactivating mutations in TSC1 or TSC2 and characterized by benign tumors (hamartomas) involving multiple organ systems. The TSC1/2 complex has been found to play a crucial role in an evolutionarily-conserved signaling pathway that regulates cell growth: the mTORC1 pathway. This pathway promotes anabolic processes and inhibits catabolic processes in response to extracellular and intracellular factors. Findings in cancer biology have reinforced the critical role for TSC1/2 in cell growth and proliferation. In contrast to cancer cells, in the CNS, the TSC1/2 complex not only regulates cell growth/proliferation, but also orchestrates an intricate and finely tuned system that has distinctive roles under different conditions, depending on cell type, stage of development, and subcellular localization. Overall, TSC1/2 signaling in the CNS, via its multi-faceted roles, contributes to proper neural connectivity. Here, we will review the TSC signaling in the CNS.
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In the citing paper
“This then binds and activates phosphoinositide-dependent protein kinase (PDK1), which in turn contributes to activation of the serine/threonine protein kinase Akt proteins.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
In the citing paper
“Activated Akt phosphorylates TSC2, reducing its GTPase activating protein (GAP) activity for the Ras family GTPase, Rheb.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
In the citing paper
“BDNF binding to TrkB activates the phosphatidylinositol-3-OH kinase (PI(3)K), which phosphorylates phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) at the 3′ position to generate phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3).”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
In the citing paper
“Thus, phosphorylation of TSC2 leads to Rheb activation, which in turn triggers activation of the protein kinase mTOR, contributing to the activation of protein synthesis (Fig. 4)67.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
In the citing paper
“This disorder is caused by mutations in TSC1 or TSC2 that encode tumour suppressor proteins which form the complex TSC1–TSC2 that regulate protein synthesis in a wide range of mammalian cell types, including neurons67.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
In the citing paper
“The binding of growth factors to receptor tyrosine kinases leads to phosphorylation of the TSC complex and subsequent activation of the mTOR, a positive regulator of protein synthesis67.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [67]
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Cites
1 retracted
Dan, H. C., Sun, M., Yang, L., Feldman, R. I., Sui, X.-M., Ou, C. C., Nellist, M. D., Yeung, R. S. W., Halley, D. J. J., Nicosia, S. V., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205838200 · Cited by 370
RetractedTOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
mTOR-Dependent Synapse Formation Underlies the Rapid Antidepressant Effects of NMDA Antagonists
Li, N., Lee, B., Liu, R.-J., Banasr, M., Dwyer, J. M., Iwata, M., Li, X.-Y., Aghajanian, G., & Duman, R. S. (2010) · Science · doi:10.1126/science.1190287 · Cited by 2,881
The 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
Molecular mechanisms of mTOR-mediated translational control
Ma, X. M., & Blenis, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2672 · Cited by 2,558
Sancak, 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 · cited 1×
“Rag complex at lysosomal membranes, and this creates a docking site for mTORC1 [42].”
BackgroundProlonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB
Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365
Promoting Axon Regeneration in the Adult CNS by Modulation of the PTEN/mTOR Pathway
Park, K. K., Liu, K., Hu, Y., Smith, P. D., Wang, C., Cai, B., Xu, B., Connolly, L., Kramvis, I., Sahin, M., et al. (2008) · Science · doi:10.1126/science.1161566 · Cited by 1,686
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Items 101–107 of 107
Aksoylu, I. S., Martin, P., Robert, F., Szkop, K. J., Redmond, N. E., Bhattacharyya, S., Wang, J., Chen, S., Beauchamp, R. L., Nobeli, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.24439501
Aksoylu, I. S., Martin, P., Robert, F., Szkop, K. J., Redmond, N. E., Bhattacharyya, S., Wang, J., Chen, S., Beauchamp, R. L., Nobeli, I., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24439424
Early cellular events induced by Sindbis virus via CD11b support viral infection
Zhao, L.-J., Tang, H.-L., Pan, Z.-D., Tang, W.-D., & Ren, R. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.116124
Severe Renal Phenotype Across A Multigenerational Tuberous Sclerosis Complex ( TSC ) Family
Tuller, E., Samuels, J., Northrup, H., & Richardson, K. (2026) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.70205
Les mécanismes antiépileptiques de l’AppCH2ppA dans la sclérose tubéreuse de Bourneville
Pons-Bennaceur, A. (2018) · theses.fr (ABES) · doi:10.70675/bc0fd846z6521z4538zb18cz82c70f31c458
Tryptophan-enriched diet improves social behavior in a mouse model of tuberous sclerosis complex
Pais, M., Fonseca, C., Martins, J., Fortuna, A. C., Castelo-Branco, M. S., & Gonçalves, J. (2026) · Nutritional Neuroscience · doi:10.1080/1028415x.2026.2734200
BindingDB (2019) · UC San Diego · doi:10.7270/q2377c5d
Metadata
- Authors
- Han, J. M., & Sahin, M.
- Affiliations
- Boston Children's Hospital (US)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2011-02-15
- Volume
- 585
- Issue
- 7
- Pages
- 973-980
- ISSN
- 0014-5793 (ISSN-L)
- PMC
- PMC3070766
- OpenAlex
- W2074197666
- Cited by
- 105
- References
- 123
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 10 · 2022: 6 · 2021: 5 · 2020: 6 · 2019: 5 · 2018: 2 · 2017: 10 · 2016: 4 · 2015: 9 · 2014: 13 · 2013: 14 · 2012: 10
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (R01NS058956)
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Tuberous Sclerosis Complex Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- tuberous sclerosis complex, TSC1, TSC2, mTORC1 signaling, central nervous system, neural cell proliferation, neural growth, neuronal connectivity, hamartoma, cell growth regulation
- MeSH terms
- Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Animals, Central Nervous System, Disease Models, Animal, Humans, Neurons, Tuberous Sclerosis, Signal Transduction, Tumor Suppressor Proteins
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