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Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Open accessAbstract
Tuberous sclerosis complex (TSC) is a genetic disease caused by mutation in either TSC1 or TSC2 . The TSC1 and TSC2 gene products form a functional complex and inhibit phosphorylation of S6K and 4EBP1. These functions of TSC1/TSC2 are likely mediated by mTOR. Here we report that TSC2 is a GTPase-activating protein (GAP) toward Rheb, a Ras family GTPase. Rheb stimulates phosphorylation of S6K and 4EBP1. This function of Rheb is blocked by rapamycin and dominant-negative mTOR. Rheb stimulates the phosphorylation of mTOR and plays an essential role in regulation of S6K and 4EBP1 in response to nutrients and cellular energy status. Our data demonstrate that Rheb acts downstream of TSC1/TSC2 and upstream of mTOR to regulate cell growth.
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In the citing paper
“mTORC1-TFEB signaling governs lysosomal biogenesis (Laplante and Sabatini 2012), (Inoki et al. 2003), (Tee et al. 2003), (Sardiello et al. 2009), (Settembre et al. 2012), (Settembre et al. 2013), (Sardiello et al. 2009), (Martina et al. 2014), and TFEB targets include several genes, including MCOLN1 (Nnah et al. 2019).”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Inoki et al. 2003
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“The TSC complex (TSCC) acts as a GTPase activating protein (GAP) for Rheb, employing a GAP domain within the TSC2 subunit”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Inoki et al., 2003
In the citing paper
“Activation of mTORC1 by Rheb downstream of growth-factor signaling (Inoki et al. 2003), (Tee et al. 2003), controls lysosomal and autophagosome biogenesis via TFEB and the CLEAR gene network (Sardiello et al. 2009), (Settembre et al. 2012).”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Inoki et al. 2003
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Cites
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
Self-citationeIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
Gingras, A., Raught, B., & Sonenberg, N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.913 · Cited by 2,103
Identification and characterization of the tuberous sclerosis gene on chromosome 16
(1993) · Cell · doi:10.1016/0092-8674(93)90618-z · Cited by 1,645
Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., & Cantley, L. C. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00568-3 · Cited by 1,555
Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,370
A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211
FUNCTION AND REGULATION OF RAS
Lowy, D. R., & Willumsen, B. M. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004223 · Cited by 1,164
Phosphatidic 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
Mammalian TOR: a homeostatic ATP sensor
Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., & Thomas, G. (2001) · Science · doi:10.1126/science.1063518 · Cited by 962
Tee, A. R., Fingar, D. C., Manning, B. D., Kwiatkowski, D. J., Cantley, L. C., & Blenis, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202476899 · Cited by 827
Flagged first, then by citations
Research works printed but not linked: 1
- 2002, Cancer Res., 62, 5645
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Sorted by citations
Items 901–1,000 of 1,009
Grech, G., Blázquez-Domingo, M., Kolbus, A., Bakker, W. J., Müllner, E. W., Beug, H., & Lindern, M. V. (2008) · Blood · doi:10.1182/blood-2008-01-133140 · Cited by 39
Coffey, R., Shi, Y., Long, M. J. C., Marr, M. T., & Hedstrom, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691584 · Cited by 36
Muscle atrophy in transgenic mice expressing a human TSC1 transgene
Wan, M., Wu, X., Guan, K., Han, M., Zhuang, Y., & Xu, T. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.09.008 · Cited by 38
Self-citationEnvironmental control of cell size at division
Davie, E., & Petersen, J. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.08.003 · Cited by 34
Spatial regulation of the mTORC1 system in amino acids sensing pathway
Suzuki, T., & Inoki, K. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr066 · Cited by 36
Self-citationLoss of hepatic DEPTOR alters the metabolic transition to fasting
Caron, A., Mouchiroud, M., Gautier, N., Labbé, S. M., Villot, R., Turcotte, L., Secco, B., Lamoureux, G., Shum, M., Gélinas, Y., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.02.005 · Cited by 36
Amino acid and small GTPase regulation of mTORC1
Nguyen, T. P., Frank, A. R., & Jewell, J. L. (2017) · Cellular Logistics · doi:10.1080/21592799.2017.1378794 · Cited by 37
Kang, T., Jensen, P., Huang, H., Christensen, G. L., Billestrup, N., & Larsen, M. R. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000217 · Cited by 34
Chen, J., Hsieh, M., Lin, C., Lin, C.-C., Hsi, Y., Lo, Y., Chuang, Y., Hsieh, M.-J., & Chen, M. (2017) · Oncotarget · doi:10.18632/oncotarget.22444 · Cited by 35
mTOR Inhibitors in Advanced Biliary Tract Cancers
Wu, C., Chen, M., & Yeh, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030500 · Cited by 35
Čokić, V. P., Mossuz, P., Han, J., Socoro-Yuste, N., Beleslin‐Čokić, B. B., Ajtić, O. M., Subotički, T., Diklić, M., Leković, D., Gotić, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135463 · Cited by 37
Autophagy induced by farnesyltransferase inhibitors in cancer cells
Pan, J., Chen, B., Su, C., Zhao, R., Xu, Z., Sun, L., Lee, M., & Yeung, S. J. (2008) · Cancer Biology & Therapy · doi:10.4161/cbt.7.10.6661 · Cited by 35
Autophagy: Cancer Therapy’s Friend or Foe?
Grandér, D., & Panaretakis, T. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.09.155 · Cited by 35
The insulin signalling network
Burchfield, J. G., Díaz‐Vegas, A., & James, D. E. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01349-z · Cited by 39
Lv, X., Ma, X., & Hu, Y. (2013) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2013.800479 · Cited by 34
Mi, R., Ma, J., Zhang, D., Li, L., & Zhang, H. (2009) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/s1673-8527(08)60124-1 · Cited by 34
Guanylyl Cyclase C in Colorectal Cancer: Susceptibility Gene and Potential Therapeutic Target
Lin, J. E., Li, P., Pitari, G. M., Schulz, S., & Waldman, S. A. (2009) · Future Oncology · doi:10.2217/fon.09.14 · Cited by 35
Sánchez, F. G., Romero, S., & Smitz, J. E. J. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.111.091744 · Cited by 34
Spatial regulation of mTORC1 signalling: Beyond the Rag GTPases
Carroll, B. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.02.007 · Cited by 33
Zhang, R., Zhang, H., Li, P.-Y., Li, C., Gao, J., Li, J., Xu, T., Wang, X., Wang, C.-L., Zhang, H.-C., et al. (2021) · Virology Journal · doi:10.1186/s12985-020-01484-x · Cited by 33
Self-citationLesma, E. A., Sirchia, S. M., Ancona, S., Carelli, S., Bòsari, S., Ghelma, F., Montanari, E., Giulio, A. M. D., & Gorio, A. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080799 · Cited by 34
Jacobs, B. L., McNally, R. M., Kim, K., Blanco, R., Privett, R. E., You, J., & Hornberger, T. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.777805 · Cited by 34
Lina, T. T., Luo, T., Velayutham, T. S., Das, S., & McBride, J. W. (2017) · Infection and Immunity · doi:10.1128/iai.00690-17 · Cited by 33
Tuberous Sclerosis and Insulin Resistance: Unlikely Bedfellows Reveal A TORrid Affair
Shah, O. J., & Hunter, T. R. (2004) · Cell Cycle · doi:10.4161/cc.4.1.1343 · Cited by 34
Scheidenhelm, D. K., Cresswell, J. R., Haipek, C. A., Fleming, T. P., Mercer, R. W., & Gutmann, D. H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3151-3162.2005 · Cited by 34
Genomic characterization of a well-differentiated grade 3 pancreatic neuroendocrine tumorPreprint
Williamson, L., Steel, M. J., Grewal, J., Thibodeau, M. L., Stutheit-Zhao, E. Y., Loree, J. M., Yang, K., Gorski, S. M., Mungall, A. J. J., Mungall, K., et al. (2019) · Molecular Case Studies · doi:10.1101/mcs.a003814 · Cited by 34
Ring domains are essential for GATOR2-dependent mTORC1 activation
Jiang, C., Dai, X., He, S., Zhou, H., Fang, L., Guo, J., Liu, S., Zhang, T., Pan, W., Yu, H., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.021 · Cited by 35
The rapid proximity labeling system PhastID identifies ATP6AP1 as an unconventional GEF for Rheb
Feng, R., Liu, F., Li, R., Zhou, Z., Lin, Z., Song, L., Deng, S., Li, Y., Nong, B., Xia, Y., et al. (2024) · Cell Research · doi:10.1038/s41422-024-00938-z · Cited by 34
Self-citationNutrient sensing of mTORC1 signaling in cancer and aging
Jiang, C., Tan, X., Liu, N., Yan, P., Hou, T., & Wei, W. (2024) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2024.08.001 · Cited by 35
Disruption of the Rag-Ragulator Complex by c17orf59 Inhibits mTORC1
Schweitzer, L. D., Comb, W. C., Bar‐Peled, L., & Sabatini, D. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.052 · Cited by 36
Role of Rab GTPases and their interacting proteins in mediating metabolic signalling and regulation
Chua, C. E. L., & Tang, B. L. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1862-x · Cited by 35
Zhang, H.-M., Diaz, V., Walsh, M. E., & Zhang, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-00970-7 · Cited by 31
Varusai, T., & Nguyen, L. K. (2018) · Scientific Reports · doi:10.1038/s41598-017-18400-z · Cited by 33
Mechanistic Target of Rapamycin Pathway in Epileptic Disorders
Kim, J., & Lee, J. H. (2019) · Journal of Korean Neurosurgical Society · doi:10.3340/jkns.2019.0027 · Cited by 35
Autophagy Inhibition in BRAF-Driven Cancers
Foth, M., & McMahon, M. (2021) · Cancers · doi:10.3390/cancers13143498 · Cited by 33
Lei, Y., Huang, Y. J., Wen, X., Yin, Z., Zhang, Z., & Klionsky, D. J. (2022) · Antioxidants · doi:10.3390/antiox11020304 · Cited by 36
Transcriptome profiling of tiger pufferfish (Takifugu rubripes) gills in response to acute hypoxia
Shang, F., Bao, M., Liu, F., Hu, Z., Wang, S., Yang, X., Yu, Y., Zhang, H., Jiang, C., Qiu, X., et al. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.738324 · Cited by 33
Wang, Y., Zhao, B., Zhang, Y., Tang, Z., Shen, Q., Zhang, Y., Zhang, W., Du, J., Chien, S., & Wang, N. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01734.x · Cited by 33
Xu, Y., Yan, W., & Chen, X. (2010) · Oncogene · doi:10.1038/onc.2010.159 · Cited by 33
Sato, T., Akasu, H., Shimono, W., Matsu, C., Fujiwara, Y., Shibagaki, Y., Heard, J. J., Tamanoi, F., & Hattori, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592402 · Cited by 33
Alterations in tubular epithelial cells in diabetic nephropathy
Habib, S. L. (2013) · Journal of Nephrology · doi:10.5301/jn.5000287 · Cited by 33
RasGRP1 is a causal factor in the development of l -DOPA–induced dyskinesia in Parkinson’s disease
Eshraghi, M., Ramírez-Jarquín, U. N., Shahani, N., Nuzzo, T., Rosa, A. D., Swarnkar, S., Galli, N., Rivera, O., Tsaprailis, G., Scharager-Tapia, C., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz7001 · Cited by 33
Faithfull Modeling of PTEN Loss Driven Diseases in the Mouse
Nardella, C., Carracedo, A., Salmena, L., & Pandolfi, P. P. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_62 · Cited by 34
Shi, F., & Collins, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411497 · Cited by 34
Lymphatic manifestations of lymphangioleiomyomatosis.
Gupta, R., Kitaichi, M., Inoue, Y., Kotloff, R. M., & McCormack, F. X. (2014) · PubMed · Cited by 32
Altman, M. K., Alshamrani, A. A., Jia, W. P., Nguyen, H. T., Fambrough, J. M., Tran, S. K., Patel, M. B., Hoseinzadeh, P., Beedle, A. M., & Murph, M. M. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.08.012 · Cited by 31
mTORC signaling in hematopoiesis
Wang, X., Chu, Y., Wang, W., & Yuan, W. (2016) · International Journal of Hematology · doi:10.1007/s12185-016-1944-z · Cited by 32
Rapiteanu, R., Davis, L. J., Williamson, J. C., Timms, R. T., Luzio, J. P., & Lehner, P. J. (2016) · Traffic · doi:10.1111/tra.12409 · Cited by 32
Snapshot: Implications for mTOR in Aging-related Ischemia/Reperfusion Injury
Liu, D., Xu, L., Zhang, X., Shi, C., Qiao, S., Ma, Z., & Yuan, J. (2018) · Aging and Disease · doi:10.14336/ad.2018.0501 · Cited by 34
Myeloid folliculin balances mTOR activation to maintain innate immunity homeostasis
Li, J., Wada, S., Weaver, L. K., Biswas, C., Behrens, E. M., & Arany, Z. P. (2019) · JCI Insight · doi:10.1172/jci.insight.126939 · Cited by 30
Rheb regulates nuclear mTORC1 activity independent of farnesylation
Zhong, Y., Zhou, X., Guan, K., & Zhang, J. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.02.006 · Cited by 34
Self-citationTherapeutic Potential of H11 Kinase for the Ischemic Heart
Danan, I. J., Rashed, E. R., & Depré, C. (2007) · Cardiovascular Drug Reviews · doi:10.1111/j.1527-3466.2007.00002.x · Cited by 32
Present and Future of EGFR Inhibitors for Head and Neck Squamous Cell Cancer
Baba, Y., Fujii, M., Tokumaru, Y., & Kato, Y. (2012) · Journal of Oncology · doi:10.1155/2012/986725 · Cited by 32
Yuan, J., Shan, Y., Chen, X., Tang, W., Luo, K., Ni, J., Wan, B., & Yu, L. (2005) · Molecular Biology Reports · doi:10.1007/s11033-005-0984-x · Cited by 32
Everolimus – a new approach in the treatment of renal cell carcinoma
Eisen, T. G. (2010) · Cancer Management and Research · doi:10.2147/cmar.s6047 · Cited by 32
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Cynober, L., & Harris, R. A. (2006) · Cited by 32
Ciclopirox olamine inhibits mTORC1 signaling by activation of AMPK
Zhou, H., Shang, C., Wang, M., Shen, T., Kong, L., Yu, C., Ye, Z.-N., Luo, Y., Liu, L., Li, Y., et al. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.07.005 · Cited by 32
Self-citationRegulation of Reproductive Processes in Female Mosquitoes
Roy, S., Smýkal, V., Johnson, L., Saha, T. T., Zou, Z., & Raikhel, A. S. (2016) · Advances in insect physiology · doi:10.1016/bs.aiip.2016.05.004 · Cited by 34
Rheb Activation of mTOR and S6K1 Signaling
Hanrahan, J., & Blenis, J. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)07044-8 · Cited by 32
Gupta, I., & Gaykalova, D. A. (2024) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2024.08.004 · Cited by 31
An evaluation of sirolimus in renal transplantation
Halleck, F., Duerr, M., Waiser, J., Huber, L., Matz, M., Brakemeier, S., Liefeldt, L., Neumayer, H. ‐., & Budde, K. (2012) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2012.719874 · Cited by 31
Alam, M. S., Rallabandi, V. P. S., & Roy, P. K. (2016) · Frontiers in Neurology · doi:10.3389/fneur.2016.00094 · Cited by 33
Modulation of the secretory pathway by amino-acid starvation
van Leeuwen, W., van der Krift, F., & Rabouille, C. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201802003 · Cited by 34
Direct imaging of the recruitment and phosphorylation of S6K1 in the mTORC1 pathway in living cells
Ahmed, A. R., Owens, R. J., Stubbs, C. D., Parker, A. W., Hitchman, R. B., Yadav, R. B., Dumoux, M., Hawes, C. R., & Botchway, S. W. (2019) · Scientific Reports · doi:10.1038/s41598-019-39410-z · Cited by 36
The Rheb-TORC1 signaling axis functions as a developmental checkpoint
Duong, T., Rasmussen, N. R., Ballato, E., Mote, F. S., & Reiner, D. J. (2020) · Development · doi:10.1242/dev.181727 · Cited by 25
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Meng, D., Yang, Q., Melick, C. H., Park, B. C., Hsieh, T., Curukovic, A., Jeong, M., Zhang, J., James, N. G., & Jewell, J. L. (2021) · The EMBO Journal · doi:10.15252/embj.2020106412 · Cited by 36
Kim, K., Yoo, H. C., Kim, B., Kim, S., Sung, Y., Yoon, I., Yu, Y. C., Park, S. J., Kim, J. H., Myung, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30696-8 · Cited by 31
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Santini, E., & Klann, E. (2011) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2011.00076 · Cited by 34
A pharmacological activator of AMP-activated protein kinase (AMPK) induces astrocyte stellation
Favero, C. B., & Mandell, J. W. (2007) · Brain Research · doi:10.1016/j.brainres.2007.06.087 · Cited by 31
Murai, T., Nakase, Y., Fukuda, K., Chikashige, Y., Tsutsumi, C., Hiraoka, Y., & Matsumoto, T. (2009) · Genetics · doi:10.1534/genetics.109.105379 · Cited by 31
TORC1 Signaling Is Governed by Two Negative Regulators in Fission Yeast
Ma, N., Liu, Q., Zhang, L., Henske, E. P., & Ma, Y. (2013) · Genetics · doi:10.1534/genetics.113.154674 · Cited by 33
eIF4A inactivates TORC1 in response to amino acid starvation
Tsokanos, F., Albert, M., Demetriades, C., Spirohn, K., Boutros, M., & Teleman, A. A. (2016) · The EMBO Journal · doi:10.15252/embj.201593118 · Cited by 29
Translational control in brain pathologies: biological significance and therapeutic opportunities
Delaidelli, A., Jan, A., Herms, J. W., & Sorensen, P. H. B. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01971-8 · Cited by 31
Zhang, C., Wang, Y., Zhen, Z., Li, J., Su, J., & Wu, C. (2023) · Advanced Science · doi:10.1002/advs.202307206 · Cited by 31
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Mei, H., Wang, Y., Lin, Z., & Tong, Q. (2013) · Pediatric Hematology and Oncology · doi:10.3109/08880018.2013.798058 · Cited by 30
MicroRNA-185 induces potent autophagy via AKT signaling in hepatocellular carcinoma
Zhou, L., Liu, S., Han, M., Feng, S., Liang, J., Li, Z., Li, Y., Lu, H., Liu, T., Ma, Y., et al. (2017) · Tumor Biology · doi:10.1177/1010428317694313 · Cited by 32
Self-citationSirolimus in Liver Transplant Recipients with Hepatocellular Carcinoma: An Updated Meta-Analysis
Zhang, Z., Li, L. X., Li, P., Lv, S., Pan, B., & He, Q. (2018) · Journal of Investigative Surgery · doi:10.1080/08941939.2018.1447053 · Cited by 30
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Rakhmanova, V., Jin, M., & Shin, J. (2018) · Immune Network · doi:10.4110/in.2018.18.e18 · Cited by 29
TSC1 and DEPDC5 regulate HIV-1 latency through the mTOR signaling pathway
Jin, S., Liao, Q., Chen, J., Zhang, L., He, Q., Zhu, H., Zhang, X., & Xu, J. (2018) · Emerging Microbes & Infections · doi:10.1038/s41426-018-0139-5 · Cited by 31
Lymphatic Function and Dysfunction in the Context of Sex Differences
Trincot, C. E., & Caron, K. M. (2019) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.9b00051 · Cited by 33
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Zatyka, M., Sarkar, S., & Barrett, T. G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.012 · Cited by 30
Maity, S., Das, F., Kasinath, B. S., Ghosh‐Choudhury, N., & Choudhury, G. G. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014994 · Cited by 30
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Apken, L. H., & Oeckinghaus, A. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2020.10.005 · Cited by 30
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Krymskaya, V. P. (2007) · BioDrugs · doi:10.2165/00063030-200721020-00003 · Cited by 30
Jham, B. C., & Montaner, S. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22524 · Cited by 30
Weatherill, D. B., Dyer, J., & Sossin, W. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071142 · Cited by 30
Kubica, N., Crispino, J. L., Gallagher, J. W., Kimball, S. R., & Jefferson, L. S. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.04.010 · Cited by 32
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Kim, D.-D., & Eng, C. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.721353 · Cited by 31
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Vinod, P. K. U., & Venkatesh, K. V. (2009) · Molecular BioSystems · doi:10.1039/b816965a · Cited by 30
Gao, Y., Gartenhaus, R. B., Lapidus, R. G., Hussain, A., Zhang, Y., Wang, X., & Dan, H. C. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0213 · Cited by 31
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Metadata
- Authors
- Inoki, K., Li, Y., Xu, T., & Guan, K.-L.
- Affiliations
- University of Michigan (US)
- Howard Hughes Medical Institute (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2003-07-17
- Volume
- 17
- Issue
- 15
- Pages
- 1829-1834
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC196227
- OpenAlex
- W2056137479
- Cited by
- 1,911
- References
- 34
- Citations by year
- 2026: 44 · 2025: 68 · 2024: 75 · 2023: 78 · 2022: 72 · 2021: 107 · 2020: 103 · 2019: 73 · 2018: 97 · 2017: 112 · 2016: 111 · 2015: 127 · 2014: 92 · 2013: 101 · 2012: 94
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK124709)
- 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 › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- TSC2, GTPase-activating protein, mTOR signaling, tuberous sclerosis complex, S6K phosphorylation, 4E-BP1 phosphorylation, rapamycin, nutrient signaling, cellular energy status, cell growth regulation, Ras family GTPases
- MeSH terms
- Ras Homolog Enriched in Brain Protein, Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Antibiotics, Antineoplastic, Cell Division, Cell Line, Dose-Response Relationship, Drug, Genes, Dominant, Guanosine Triphosphate, Humans, Hydrolysis, Models, Biological, Mutation, Neuropeptides, Phosphorylation, Plasmids, Protein Binding, Protein Kinases, Proteins, Repressor Proteins, Time Factors, Protein Biosynthesis, Signal Transduction, Protein Structure, Tertiary, Sirolimus, GTP Phosphohydrolases, Monomeric GTP-Binding Proteins, Tumor Suppressor Proteins, Ribosomal Protein S6 Kinases, 70-kDa, TOR Serine-Threonine Kinases
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