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The TSC1–TSC2 complex: a molecular switchboard controlling cell growth
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TSC1 and TSC2 are the tumour-suppressor genes mutated in the tumour syndrome TSC (tuberous sclerosis complex). Their gene products form a complex that has become the focus of many signal transduction researchers. The TSC1–TSC2 (hamartin–tuberin) complex, through its GAP (GTPase-activating protein) activity towards the small G-protein Rheb (Ras homologue enriched in brain), is a critical negative regulator of mTORC1 (mammalian target of rapamycin complex 1). As mTORC1 activity controls anabolic processes to promote cell growth, it is exquisitely sensitive to alterations in cell growth conditions. Through numerous phosphorylation events, the TSC1–TSC2 complex has emerged as the sensor and integrator of these growth conditions, relaying signals from diverse cellular pathways to properly modulate mTORC1 activity. In the present review we focus on the molecular details of TSC1–TSC2 complex regulation and function as it relates to the control of Rheb and mTORC1.
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“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 Huang and Manning, 2008
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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
RetractedPhosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
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Self-citationTOR signaling in growth and metabolism
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Upstream and downstream of mTOR
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TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
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TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
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“In contrast, the TSC1-TSC2 complex, which suppresses mTORC1 activity, may promote mTORC2 signaling [10].”
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The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits
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“To further explore the significance of this activation to mTOR signaling, we examined the phosphorylation of the AMPK target TSC2 at Ser1387, which enhances the inhibitory effects of TSC on mTOR (Huang and Manning, 2008; Inoki et al., 2003).”
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BackgroundSubependymal Giant Cell Astrocytomas in Patients With Tuberous Sclerosis Complex:
Wheless, J. W., & Klimo, P. D. (2013) · Journal of Child Neurology · doi:10.1177/0883073813501870 · Cited by 24
“The hamartin-tuberin heterodimer negatively regulates mTORC1 activity by inhibiting the G-protein Rheb (Ras homologue enriched in brain).(7,10) Thus, mutation or deletion of either protein of the hamartin-tuberin dimer leads to overactivation of mTORC1 and tumor growth.”
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“In contrast, TSC2 phosphorylation on Ser1387, regulated in part by AMPK (Huang and Manning, 2008), was increased in eWAT from alcohol-fed mice (Figure 5B, 5F), and this was consistent with the activation of AMPK as evidenced by increased AMPK phosphorylated on Thr172 (Figure 5B, 5G).”
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“The TSC1/TSC2 complex acts as a negative regulator of mTORCs upstream, RHEB, but can be activated by AKT kinase (which belongs to IIS pathway) [36].”
BackgroundOsteocyte TSC1 promotes sclerostin secretion to restrain osteogenesis in mice
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“TSC1/2 is capable of inhibiting Rheb, a small GTPase protein that activates mTOR (63, 64).”
BackgroundmTOR and Epileptogenesis in Developmental Brain Malformations
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Advances in Immunosuppressive Agents Based on Signal Pathway
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Bakar, N. A., Ibrahim, W. N. W., Abdullah, C. A. C., Ramlan, N. F., Shaari, K., Shohaimi, S., Mediani, A., Nasruddin, N. S., Kim, C., & Faudzi, S. M. M. (2022) · Toxics · doi:10.3390/toxics10090493 · Cited by 25
“Downregulation of the tsc1b gene in As2O3-exposed larvae may involve overstimulation of the mammalian target of rapamycin (mTORC1), leading to metabolic overactivity and excessive cell growth, causing many of the multisystem effects of tsc [96,97].”
BackgroundmTOR and its tight regulation for iNKT cell development and effector function
Yang, W., Gorentla, B. K., Zhong, X., & Shin, J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.07.022 · Cited by 23
“Ma L, Chen Z, Erdjument-Bromage H, Tempst P, Pandolfi PP. Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis.”
BackgroundInfluentialLocalization of avβ6 integrin-TGF-β1/Smad3, mTOR and PPARγ in experimental colorectal fibrosis
Latella, G., Vetuschi, A., Sferra, R., Speca, S., & Gaudio, E. (2013) · European Journal of Histochemistry · doi:10.4081/ejh.2013.e40 · Cited by 23
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Protein Phosphorylation as a Key Mechanism of mTORC1/2 Signaling Pathways
Tchevkina, E. M., & Komelkov, A. V. (2012) · InTech eBooks · doi:10.5772/48274 · Cited by 26
mTOR and Akt Signaling in Cancer: SGK Cycles In
Toker, A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.007 · Cited by 23
“The signaling mechanisms leading to mTOR activation have been elucidated in both nutrient and growth factor signaling (Huang and Manning, 2008).”
BackgroundSrivastava, V. K., Hiney, J. K., & Dees, W. L. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft195 · Cited by 23
“, 2009), and their respective ability to mediate nutrient signaling (Huang and Manning, 2008; Tee et al., 2003; Wullschleger et al., 2006) and divalent metal transporter 1 (DMT1), which is associated with Mn transport (Jiang et al.”
BackgroundMethodInfluentialErden, M., & Oktay, K. (2025) · Human Reproduction · doi:10.1093/humrep/deaf024 · Cited by 23
Chiang, Y.-J., Liao, W.-T., Ho, K.-C., Wang, S., Chen, Y., Ho, C., Huang, S.-F. K., Shih, L., Yang‐Yen, H., & Yen, J. J.-Y. (2018) · Oncogene · doi:10.1038/s41388-018-0507-6 · Cited by 22
Tsc1 regulates tight junction independent of mTORC1
Lai, M., Zou, W., Han, Z., Zhou, L., Qiu, Z., Chen, J., Zhang, S., Lai, P., Li, K., Zhang, Y., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020891118 · Cited by 22
Autophagy and Metabolism in Normal and Malignant Hematopoiesis
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Elias, M. G., Mehanna, S., Elias, E., Khnayzer, R. S., & Daher, C. F. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109644 · Cited by 23
Electroconvulsive seizure inhibits the mTOR signaling pathway via AMPK in the rat frontal cortex
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The heat shock connection: skeletal muscle hypertrophy and atrophy
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Constitutive and induced functions of the p53 gene
Zheltukhin, A. O., & Chumakov, P. M. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910130110 · Cited by 23
Mitochondrial Stress Tests Using Seahorse Respirometry on Intact Dictyostelium discoideum Cells
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“GTPase, Rheb, which positively regulates mTORC1 (13), is”
Randell, E., McNamara, R. L., Davies, D. M., Owen-Jones, E., Kirby, N., Angel, L., Drew, C., Cannings-John, R. L., Smalley, M., Saxena, A., et al. (2016) · Trials · doi:10.1186/s13063-016-1446-6 · Cited by 21
“The effects of this have been demonstrated in immunohistochemical and immunoblotting studies that have shown activation of the downstream effectors of mTORC1, S6 kinase and phospho-S6 in tuberous sclerosis lesions in both pre-clinical models and patients [7].”
BackgroundNikolaeva, I., Kazdoba, T. M., Crowell, B., & D’Arcangelo, G. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.04.026 · Cited by 22
Luu, B. E., Wijenayake, S., Zhang, J., Tessier, S. N., Quintero‐Galvis, J. F., Gaitán‐Espitía, J. D., Nespolo, R. F., & Storey, K. B. (2017) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.12.006 · Cited by 22
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“Other sgRNAs enriched under drug treatment targeted PTEN, DDIT4 (36), AKT1S1 (37), and RALGAPB (38).”
BackgroundPathogenesis of TSC in the Brain
Crino, P. B., Mehta, R. I., & Vinters, H. V. (2010) · doi:10.1002/9783527630073.ch9 · Cited by 22
The role of TSC1 and TSC2 proteins in neuronal axons
Karalis, V., Wood, D., Teaney, N. A., & Sahin, M. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02402-7 · Cited by 21
Mechanosensitive mTORC1 signaling maintains lymphatic valves
Saygili Demir, C., Sabine, A., Gong, M., Dormond, O., & Petrova, T. V. (2023) · Journal of Cell Biology · doi:10.1083/jcb.202207049 · Cited by 24
“The heterodimeric TSC1/2 protein complex negatively regulates mTORC1 signaling by exerting its GTPase-activating activity on RHEB, which is a direct activator of mTORC1 (Huang and Manning, 2008; Liu and Sabatini, 2020).”
BackgroundTreating non-small cell lung cancer by targeting the PI3K signaling pathway
Jiang, L., Zhang, J., Xu, Y., Xu, H., & Wang, M. (2022) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002195 · Cited by 23
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“When either TSC1 or TSC2 is deficient, mTORC1 is constitutively up-regulated, leading to abnormal cellular growth, proliferation, and protein synthesis [6].”
BackgroundConsequences of interrupted Rheb-to-AMPK feedback signaling in tuberous sclerosis complex and cancer
Lacher, M. D., Pincheira, R., & Castro, A. F. (2011) · Small GTPases · doi:10.4161/sgtp.2.4.16703 · Cited by 21
“Considering that cell proliferation is typically dependent on cell growth, it is not surprising that alterations in critical components of the cell growth control machinery frequently contribute to proliferative diseases such as tuberous sclerosis complex (TSC), Peutz-Jeghers syndrome, neurofibromatosis type 1, Cowden…”
BackgroundInfluentialCohen, J. D., Gard, J. M. C., Nagle, R. B., Dietrich, J. D., Monks, T. J., & Lau, S. S. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr203 · Cited by 21
“The hierarchical phosphorylation of 4EBP1, on four prolinedirected sites (ser/thr-pro), suppresses 4EBP1’s ability to bind and inhibit eIF4E, allowing for the formation of the eIF4E complex and subsequent initiation of translation (Beugnet et al., 2003; Gingras et al., 1999, 2001; Huang and Manning, 2008).”
BackgroundInfluentialTargeted Therapy in Pediatric Low-Grade Glioma
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Mechanism of Brassica oleracea performance in bovine infectious mastitis by bioinformatic analysis
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The Roles of Oxidative Stress in Regulating Autophagy in Methylmercury-induced Neurotoxicity
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mTOR-Dependent Spine Dynamics in Autism
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“Therefore deletion, mutation or rearrangement of the Tsc genes leads to a loss of activity of the complex and overactivation of the mTORC1 pathway (Huang and Manning, 2008; Portocarrero et al., 2018).”
BackgroundDu, T. Y., Hall, S. R., Chung, F., Kurdyukov, S., Crittenden, E., Patel, K., Dawson, C. A., Westhorpe, A., Bartlett, K. E., Rasmussen, S. A., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adk4802 · Cited by 20
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“In the presence of nutrients, growth factors, or cytokines, receptor-mediated signals inhibit TSC activity and active GTP-bound Rheb promotes mTORc1 activity by stimulating mTOR phosphorylation at Ser2448 (30, 31).”
BackgroundLkb1 regulates granule cell migration and cortical folding of the cerebellar cortex
Ryan, K. E., Kim, P. S., Fleming, J. T., Brignola, E., Cheng, F. Y., Litingtung, Y., & Chiang, C. C. (2017) · Developmental Biology · doi:10.1016/j.ydbio.2017.09.036 · Cited by 19
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Lack of association of rare functional variants in TSC1/TSC2 genes with autism spectrum disorder
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“Hamartin and tuberin form a complex that functions as a critical negative regulator of mammalian target of rapamycin complex 1 (mTORC1)-mediated signaling [6,7].”
Franz, D. N., & Capal, J. K. (2016) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s91248 · Cited by 20
“On a molecular level, TSC results from aberrant hyperactivity of mammalian target of rapamycin (mTOR) that is caused by a mutation in one of two TSC genes, TSC1 and TSC2, which results in an increased cellular proliferation and tumor growth.(2) TSC affects multiple major organ systems, including the brain, skin, heart…”
BackgroundKlover, P. J., Thangapazham, R. L., Kato, J., Wang, J.-A., Anderson, S. A., Hoffmann, V. J., Steagall, W. K., Li, S., McCart, E. A., Nathan, N. R., et al. (2017) · eLife · doi:10.7554/elife.23202 · Cited by 20
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Identification of mTORC2 as a Necessary Component of HRG/ErbB2-Dependent Cellular Transformation
Lin, M.-C. J., Rojas, K. S., Cerione, R. A., & Wilson, K. F. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0555 · Cited by 19
“The phosphorylation of S473 on AKT by mTORC2 is thought to contribute to the activation of AKT and its downstream signaling targets TSC2 and mTORC1 (28, 34, 35).”
BackgroundInfluentialTargeting mTOR in the Context of Diet and Whole-body Metabolism
Koundouros, N., & Blenis, J. (2022) · Endocrinology · doi:10.1210/endocr/bqac041 · Cited by 22
Loss of TSC2 confers resistance to ceramide and nutrient deprivation
Guenther, G., Liu, G., Ramirez, M. U., McMonigle, R. J., Kim, S. M., McCracken, A. N., Joo, Y., Ushach, I., Nguyen, N., & Edinger, A. L. (2013) · Oncogene · doi:10.1038/onc.2013.139 · Cited by 18
Norrby, M., & Tågerud, S. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22023 · Cited by 19
“Akt also mediates phosphorylation of Foxo1 which aids in sequestering Foxo1 in the cytoplasm (Brunet et al., 1999; Jacinto et al., 2006; Huang and Tindall, 2007).”
BackgroundModerate-intensity treadmill exercise training decreases murine cardiomyocyte cross-sectional area
Sturgeon, K. M., Muthukumaran, G., Ding, D., Bajulaiye, A., Ferrari, V. A., & Libonati, J. R. (2015) · Physiological Reports · doi:10.14814/phy2.12406 · Cited by 19
Dysregulation of translational control signaling in autism spectrum disorders
Hooshmandi, M., Wong, C., & Khoutorsky, A. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109746 · Cited by 17
Reciprocity Between Skeletal Muscle AMPK Deletion and Insulin Action in Diet-Induced Obese Mice
Admin, A., Lantier, L., Williams, I. M., Williams, I. M., Guérin, A., Bracy, D. P., Goelzer, M., Foretz, M., Viollet, B., Hughey, C. C., et al. (2020) · Diabetes · doi:10.2337/db19-1074 · Cited by 21
“TSC2 is a negative regulator for mTOR, and its activity is regulated by numerous phosphorylation sites (25).”
BackgroundSegreto, R., Bazafkan, H., Millinger, J., Schenk, M., Atanasova, L., Doppler, M., Bueschl, C., Boeckstaens, M., Diaz, S. S., Schreiner, U., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0262180 · Cited by 17
“In mammalian and S. pombe cells, TSC1 and TSC2 have been shown to form the heterodimeric TSC complex that negatively regulates the activity of Rheb and TORC1 by catalyzing GTP hydrolysis on Rheb [24, 42].”
BackgroundInfluentialA Current Viewpoint of Lymphangioleiomyomatosis Supporting Immunotherapeutic Treatment Options
Dilling, D. F., Gilbert, E. R., Picken, M. M., Eby, J. M., Love, R. B., & Poole, I. C. L. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0215tr · Cited by 18
“In tuberous sclerosis, patients can present with neurological disorders, including epilepsy, autism, and mental retardation, and with tumors in multiple organs, including renal angiomyolipomas, ash-leaf shaped depigmentation patterns of the skin, and pulmonary LAM (25).”
BackgroundRahman, A., & Haugh, J. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.761205 · Cited by 18
Sparagana, S. P., Franz, D. N., Krueger, D. A., Bissler, J. J., Berkowitz, N. C., Burock, K., & Kingswood, J. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186235 · Cited by 18
FOXOs Maintaining the Equilibrium for Better or for Worse
van Doeselaar, S., & Burgering, B. M. T. (2018) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2017.10.003 · Cited by 17
Potential therapeutic effect of curcumin, a natural mTOR inhibitor, in tuberous sclerosis complex
Kuo, C.-J., Huang, C., Chou, S., Lo, Y., Kao, T., Huang, N., Lin, C. B., Lin, H.-C., Lin, H., & Lee, Y. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.09.203 · Cited by 18
Striatal Inhibition of MeCP2 or TSC1 Produces Sociability Deficits and Repetitive Behaviors
Lee, Y., Kim, H., & Han, P. (2018) · Experimental Neurobiology · doi:10.5607/en.2018.27.6.539 · Cited by 18
Pancreatic Neuroendocrine Tumor in a Young Child With Tuberous Sclerosis Complex 1
Mehta, S., Rusyn, L., Ginsburg, H. B., Hajdu, C. H., & Kohn, B. (2019) · Journal of the Endocrine Society · doi:10.1210/js.2019-00051 · Cited by 18
“The TSC1 and TSC2 proteins form a complex and function as tumor suppressors by inhibiting mTOR, which regulates the major cellular processes required for normal cell growth and differentiation, metabolism, and survival [13].”
BackgroundLatest progress on the molecular mechanisms of idiopathic pulmonary fibrosis
Fang, Y., Tian, J., Fan, Y., & Cao, P. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-06000-6 · Cited by 20
Sestrin2 and mitochondrial quality control: Potential impact in myogenic differentiation
Piochi, L. F., Machado, I. F., Palmeira, C. M., & Rolo, A. P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101309 · Cited by 21
mTOR regulates TLR-induced c-fos and Th1 responses to HBV and HCV vaccines
He, L., Zang, A., Du, M., Ma, D., Yuan, C., Zhou, C., Mu, J., Shi, H., Li, D., Huang, X., et al. (2015) · Virologica Sinica · doi:10.1007/s12250-015-3606-3 · Cited by 18
Carbonell-Roig, J., Aaltonen, A., Wilson, K., Molinari, M., Cartocci, V., McGuirt, A. F., Mosharov, E. V., Kehr, J., Lieberman, O. J., Sulzer, D., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114997 · Cited by 17
Rojas, M. L. R.-F., Feucht, M., Macaya, A., Wilken, B., Hahn, A., Maamari, R., Hirschberg, Y., Ridolfi, A., & Kingswood, J. C. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.802334 · Cited by 17
The crosstalk between MYC and mTORC1 during osteoclastogenesis
Bae, S., Oh, B., Tsai, J., Park, P. S. U., Greenblatt, M. B., Γιαννοπούλου, Ε., & Park‐Min, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.920683 · Cited by 17
“The heterodimeric tuberous sclerosis complex (TSC) 1/2 complex negatively regulates mTORC1 activity by targeting its upstream Rheb GTPase, and the deletion of TSC1 or TSC2 leads to hyperactivation of mTORC1 (Zhang et al., 2003; Huang and Manning, 2008).”
BackgroundMethodSmolen, K. A., Papke, C. M., Swingle, M. R., Musiyenko, A., Li, C., Salter, E. A., Camp, A. D., Honkanen, R. E., & Kettenbach, A. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105154 · Cited by 17
Hari, A. S., Banerji, R., Liang, L., Fulton, R. E., Huynh, C. Q., Fabisiak, T., McElroy, P. B., Roede, J. R., & Patel, M. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102895 · Cited by 17
“Interestingly, the results indicated that ~20 – 30% each of TSC1 (~20.1%), TSC2 (~30.3%), and TBC1D7 (~27.6”
BackgroundInfluentialSpampatti, M. P. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i29.10038 · Cited by 17
AMPKγ3 is dispensable for skeletal muscle hypertrophy induced by functional overload
Riedl, I., Osler, M. E., Björnholm, M., Egan, B., Nader, G. A., Chibalin, A., & Zierath, J. R. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00387.2015 · Cited by 16
Analysis of TSC1 mutation spectrum in mucosal melanoma
Ma, M., Dai, J., Xu, T., Yu, S., Yu, H., Tang, H., Yan, J., Wu, X., Yu, J., Chi, Z., et al. (2017) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-017-2550-z · Cited by 17
Mayer, K. A., Smole, U., Zhu, C., Derdak, S. V., Minervina, A. A., Salnikova, M. A., Witzeneder, N., Christamentl, A., Boucheron, N., Waidhofer‐Söllner, P., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202001763rr · Cited by 18
Beyond Protein Synthesis; The Multifaceted Roles of Tuberin in Cell Cycle Regulation
da Silva, E. F., Fong, J., Roye‐Azar, A., Nadi, A., Drouillard, C., Pillon, A., & Porter, L. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.806521 · Cited by 17
Autophagy defects in Lafora disease
Puri, R., & Ganesh, S. (2012) · Autophagy · doi:10.4161/auto.8.2.19010 · Cited by 17
Metadata
- Authors
- Huang, J., & Manning, B. D.
- Affiliations
- Harvard University (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2008-05-14
- Volume
- 412
- Issue
- 2
- Pages
- 179-190
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2735030
- OpenAlex
- W1993431258
- Cited by
- 1,237
- References
- 133
- Citations by year
- 2026: 26 · 2025: 58 · 2024: 53 · 2023: 62 · 2022: 77 · 2021: 83 · 2020: 77 · 2019: 69 · 2018: 74 · 2017: 79 · 2016: 68 · 2015: 82 · 2014: 70 · 2013: 72 · 2012: 73
- FWCI
- 5.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA122617, P01CA120964)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Genetics (clinical) › Tuberous Sclerosis Complex Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Keywords
- TSC1/TSC2 complex, hamartin, tuberin, tuberous sclerosis complex, Rheb, GTPase-activating protein, mTORC1, cell growth regulation, signal transduction, phosphorylation, anabolic processes, tumor suppressor
- MeSH terms
- Ras Homolog Enriched in Brain Protein, Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Amino Acid Sequence, Animals, Cell Cycle, Humans, Insulin, Insulin-Like Growth Factor I, Molecular Sequence Data, Neuropeptides, Protein Kinases, Transcription Factors, Signal Transduction, Genes, Tumor Suppressor, Sequence Alignment, Ribosomal Protein S6 Kinases, Monomeric GTP-Binding Proteins, Tumor Suppressor Proteins, Intercellular Signaling Peptides and Proteins, Cell Growth Processes, TOR Serine-Threonine Kinases
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