The TSC1–TSC2 complex: a molecular switchboard controlling cell growth

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216

AKT/PKB signaling: navigating downstream

Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115

TOR 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

Upstream and downstream of mTOR

Hay, N., & Sonenberg, N. (2004) · Genes & Development · doi:10.1101/gad.1212704 · Cited by 4,181

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

Defining the role of mTOR in cancer

Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833

Rictor, a Novel Binding Partner of mTOR, Defines a Rapamycin-Insensitive and Raptor-Independent Pathway that Regulates the Cytoskeleton

Sarbassov, D. D., Ali, S. M., Kim, D.-H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., & Sabatini, D. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.054 · Cited by 2,665

Prolonged 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

Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097

Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast

Heitman, J., Movva, N. R., & Hall, M. N. (1991) · Science · doi:10.1126/science.1715094 · Cited by 2,010

Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling

Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911

Two TOR Complexes, Only One of which Is Rapamycin Sensitive, Have Distinct Roles in Cell Growth Control

Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., Oppliger, W., Jenoe, P., & Hall, M. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00636-6 · Cited by 1,886

The Tuberous Sclerosis Complex

Crino, P. B., Nathanson, K. L., & Henske, E. P. (2006) · New England Journal of Medicine · doi:10.1056/nejmra055323 · Cited by 1,793

Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity

Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677

Identification of the Tuberous Sclerosis Gene TSC1 on Chromosome 9q34

Slegtenhorst, M. V., Hoogt, R. D., Hermans, C., Nellist, M., Janssen, B., Verhoef, S., Lindhout, D., Ouweland, A. V. D., Halley, D., Young, J., et al. (1997) · Science · doi:10.1126/science.277.5327.805 · Cited by 1,648

Identification and characterization of the tuberous sclerosis gene on chromosome 16

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Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway

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

Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex

Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes & Development · doi:10.1101/gad.1256804 · Cited by 1,384

TSC2 Integrates Wnt and Energy Signals via a Coordinated Phosphorylation by AMPK and GSK3 to Regulate Cell Growth

Inoki, K., Ouyang, H., Zhu, T., Lindvall, C., Wang, Y., Zhang, X., Yang, Q., Bennett, C., Harada, Y., Stankunas, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.055 · Cited by 1,377

Amino Acid Sufficiency and mTOR Regulate p70 S6 Kinase and eIF-4E BP1 through a Common Effector Mechanism

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

Phosphorylation and Functional Inactivation of TSC2 by Erk

Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268

Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression

Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,264

Sirolimus for Angiomyolipoma in Tuberous Sclerosis Complex or Lymphangioleiomyomatosis

Bissler, J. J., McCormack, F. X., Young, L. R., Elwing, J., Chuck, G., Leonard, J. M., Schmithorst, V. J., Laor, T., Brody, A. S., Bean, J. A., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa063564 · Cited by 1,250

PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase

Sancak, Y., Thoreen, C. C., Peterson, T. R., Lindquist, R. A., Kang, S. A., Spooner, E., Carr, S. A., & Sabatini, D. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.003 · Cited by 1,236

RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1

Burnett, P. E., Barrow, R. K., Cohen, N. A., Snyder, S. H., & Sabatini, D. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1432 · Cited by 1,130

The TSC1-2 tumor suppressor controls insulin–PI3K signaling via regulation of IRS proteins

Harrington, L. S., Findlay, G. M., Gray, A., Толкачева, Т. А., Wigfield, S., Rebholz, H., Barnett, J., Leslie, N. R., Cheng, S., Shepherd, P. R., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403069 · Cited by 1,123

The LKB1 tumor suppressor negatively regulates mTOR signaling

Shaw, R. J., Bardeesy, N. M., Manning, B. D., Lopez, L. V., Kosmatka, M., DePinho, R. A., & Cantley, L. C. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.06.007 · Cited by 1,107

Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E

Fingar, D. C., Salama, S., Tsou, C., Harlow, E., & Blenis, J. (2002) · Genes & Development · doi:10.1101/gad.995802 · Cited by 1,093

Tuberous Sclerosis Complex Gene Products, Tuberin and Hamartin, Control mTOR Signaling by Acting as a GTPase-Activating Protein Complex toward Rheb

Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00506-2 · Cited by 1,080

Insulin Activation of Rheb, a Mediator of mTOR/S6K/4E-BP Signaling, Is Inhibited by TSC1 and 2

Garami, A., Zwartkruis, F. J. T., Nobukuni, T., Joaquin, M., Roccio, M., Stocker, H., Kozma, S. C., Hafen, E., Bos, J. L., & Thomas, G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00220-x · Cited by 1,043

Rheb Binds and Regulates the mTOR Kinase

Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005

Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR

Neshat, M. S., Mellinghoff, I. K., Tran, C., Stiles, B. L., THOMAS, G. V., Petersen, R., Frost, P., Gibbons, J. J., Wu, H., & Sawyers, C. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171076798 · Cited by 971

mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways

Majumder, P. K., Febbo, P. G., Bikoff, R., Berger, R., Xue, Q., McMahon, L. M., Manola, J., Brugarolas, J., McDonnell, T. J., Golub, T. R., et al. (2004) · Nature Medicine · doi:10.1038/nm1052 · Cited by 964

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

Akt regulates growth by directly phosphorylating Tsc2

Potter, C. J., Pedraza, L. G., & Xu, T. (2002) · Nature Cell Biology · doi:10.1038/ncb840 · Cited by 959

Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins

Zhang, Y., Gao, X., Saucedo, L. J., Ru, B., Edgar, B. A., & Pan, D. (2003) · Nature Cell Biology · doi:10.1038/ncb999 · Cited by 924

Hierarchical phosphorylation of the translation inhibitor 4E-BP1

Gingras, A.-C., Raught, B., Gygi, S. P., Niedzwiecka, A., Miron, M., Burley, S. K., Polakiewicz, R. D., Wyslouch-Cieszynska, A., Aebersold, R., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.912401 · Cited by 883

Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling

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

Inappropriate Activation of the TSC/Rheb/mTOR/S6K Cassette Induces IRS1/2 Depletion, Insulin Resistance, and Cell Survival Deficiencies

Shah, O. J., Wang, Z., & Hunter, T. R. (2004) · Current Biology · doi:10.1016/j.cub.2004.08.026 · Cited by 800

Drosophila S6 kinase: a regulator of cell size.

Montagne, J., Stewart, M. J., Stocker, H., Hafen, E., Kozma, S., & Thomas, G. (1999) · Science · doi:10.1126/science.285.5436.2126 · Cited by 785

Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase

Nobukuni, T., Joaquin, M., Roccio, M., Dann, S. G., Kim, S. Y., Gulati, P., Byfield, M. P., Backer, J., Natt, F., Bos, J. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506925102 · Cited by 775

Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase

Roux, P. P., Ballif, B. A., Anjum, R., Gygi, S. P., & Blenis, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405659101 · Cited by 750

Hypoxia regulates TSC1/2–mTOR signaling and tumor suppression through REDD1-mediated 14–3–3 shuttling

DeYoung, M. P., Horak, P., Sofer, A., Sgroi, D., & Ellisen, L. W. (2008) · Genes & Development · doi:10.1101/gad.1617608 · Cited by 710

Tsc tumour suppressor proteins antagonize amino-acid–TOR signalling

Gao, X., Zhang, Y., Arrazola, P., Hino, O., Kobayashi, T., Yeung, R. S. W., Ru, B., & Pan, D. (2002) · Nature Cell Biology · doi:10.1038/ncb847 · Cited by 689

A mouse model of TSC1 reveals sex-dependent lethality from liver hemangiomas, and up-regulation of p70S6 kinase activity in Tsc1 null cells

Kwiatkowski, D. J. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.5.525 · Cited by 674

Rheb promotes cell growth as a component of the insulin/TOR signalling network

Saucedo, L. J., Gao, X., Chiarelli, D. A., Li, L., Pan, D., & Edgar, B. A. (2003) · Nature Cell Biology · doi:10.1038/ncb996 · Cited by 658

Mutations in the tuberous sclerosis complex gene TSC2 are a cause of sporadic pulmonary lymphangioleiomyomatosis

Carsillo, T., Astrinidis, A., & Henske, E. P. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.11.6085 · Cited by 648

IKKβ Suppression of TSC1 Links Inflammation and Tumor Angiogenesis via the mTOR Pathway

Lee, D., Kuo, H.-P., Chen, C., Hsu, J.-M., Chou, C., Wei, Y., Sun, H., Li, L., Ping, B., Huang, W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.058 · Cited by 639

Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase‐1 and p70 S6 kinase

Alessi, D. R., Barry Caudwell, F., Andjelkovic, M., Hemmings, B. A., & Cohen, P. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01370-1 · Cited by 628

Rapamycin causes regression of astrocytomas in tuberous sclerosis complex

Franz, D. N., Leonard, J. M., Tudor, C., Chuck, G., Caré, M. M., Sethuraman, G., Dinopoulos, A., Thomas, G., & Crone, K. R. (2006) · Annals of Neurology · doi:10.1002/ana.20784 · Cited by 609

Hypoxia-induced energy stress regulates mRNA translation and cell growth

Liu, L., Cash, T. P., Jones, R. G., Keith, B., Thompson, C. B., & Simon, M. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.010 · Cited by 607

The NF1 tumor suppressor critically regulates TSC2 and mTOR

Johannessen, C. M., Reczek, E. E., James, M. F., Brems, H., Legius, E., & Cichowski, K. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503224102 · Cited by 605

An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Pten +/− mice

Podsypanina, K., Lee, R. T., Politis, C., Hennessy, I., Crane, A., Puc, J., Neshat, M. S., Wang, H., Yang, L., Gibbons, J., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171060098 · Cited by 568

Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products

van Slegtenhorst, M. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.6.1053 · Cited by 565

Loss of Tsc1/Tsc2 activates mTOR and disrupts PI3K-Akt signaling through downregulation of PDGFR

Zhang, H., Cicchetti, G., Onda, H., Koon, H. B., Asrican, K., Bajraszewski, N., Vázquez, F., Carpenter, C. L., & Kwiatkowski, D. J. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17222 · Cited by 545

The Drosophila Tuberous Sclerosis Complex Gene Homologs Restrict Cell Growth and Cell Proliferation

Tapon, N., Ito, N., Dickson, B. J., Treisman, J. E., & Hariharan, I. K. (2001) · Cell · doi:10.1016/s0092-8674(01)00332-4 · Cited by 542

hVps34 Is a Nutrient-regulated Lipid Kinase Required for Activation of p70 S6 Kinase

Byfield, M. P., Murray, J. T., & Backer, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507201200 · Cited by 540

Rheb is an essential regulator of S6K in controlling cell growth in Drosophila

Stocker, H., Radimerski, T., Schindelholz, B., Wittwer, F., Belawat, P., Daram, P., Breuer, S., Thomas, G., & Hafen, E. (2003) · Nature Cell Biology · doi:10.1038/ncb995 · Cited by 530

Drosophila Tsc1 Functions with Tsc2 to Antagonize Insulin Signaling in Regulating Cell Growth, Cell Proliferation, and Organ Size

Potter, C. J., Huang, H., & Xu, T. (2001) · Cell · doi:10.1016/s0092-8674(01)00333-6 · Cited by 522

The TSC1-TSC2 Complex Is Required for Proper Activation of mTOR Complex 2

Huang, J., Dibble, C. C., Matsuzaki, M., & Manning, B. D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-08 · Cited by 520

Balancing Akt with S6K

Manning, B. D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408161 · Cited by 485

TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth.Preprint

Gao, X., & Pan, D. (2001) · Genes & Development · doi:10.1101/gad.901101 · Cited by 484

Loss of Tsc1/Tsc2 activates mTOR and disrupts PI3K-Akt signaling through downregulation of PDGFR

Zhang, H., Cicchetti, G., Onda, H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317222 · Cited by 482

A Novel Hypoxia-inducible Factor-independent Hypoxic Response Regulating Mammalian Target of Rapamycin and Its Targets

Arsham, A. M., Howell, J. J., & Simon, M. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212770200 · Cited by 463

Regulation of mTOR and Cell Growth in Response to Energy Stress by REDD1

Sofer, A., Lei, K., Johannessen, C. M., & Ellisen, L. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5834-5845.2005 · Cited by 449

The principal target of rapamycin‐induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

Pearson, R. B., Dennis, P. B., Han, J. W., Williamson, N. A., Kozma, S. C., Wettenhall, R. E., & Thomas, G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00212.x · Cited by 443

Tuberin Regulates p70 S6 Kinase Activation and Ribosomal Protein S6 Phosphorylation

Goncharova, E., Goncharov, D. A., Eszterhas, A., Hunter, D., Glassberg, M., Yeung, R. S., Walker, C., Noonan, D., Kwiatkowski, D., Chou, M. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202678200 · Cited by 433

Rheb Activates mTOR by Antagonizing Its Endogenous Inhibitor, FKBP38

Bai, X., Ma, D., Liu, A., Shen, X., Wang, Q. J., Liu, Y., & Jiang, Y. (2007) · Science · doi:10.1126/science.1147379 · Cited by 382

PDGFRs are critical for PI3K/Akt activation and negatively regulated by mTOR

Zhang, H., Bajraszewski, N., Wu, E., Wang, H., Moseman, A. P., Dabora, S. L., Griffin, J. D., & Kwiatkowski, D. J. (2007) · Journal of Clinical Investigation · doi:10.1172/jci28984 · Cited by 382

Rheb Binds Tuberous Sclerosis Complex 2 (TSC2) and Promotes S6 Kinase Activation in a Rapamycin- and Farnesylation-dependent Manner

Castro, A. F., Rebhun, J. F., Clark, G. J., & Quilliam, L. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300226200 · Cited by 381

Akt Activation Promotes Degradation of Tuberin and FOXO3a via the Proteasome

Plas, D. R., & Thompson, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213069200 · Cited by 378

Activity of TSC2 is inhibited by AKT-mediated phosphorylation and membrane partitioning

Cai, S.-L., Tee, A. R., Short, J. D., Bergeron, J. M., Kim, J., Shen, J., Guo, R., Johnson, C. L., Kiguchi, K., & Walker, C. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200507119 · Cited by 359

Identification of Tuberin, the Tuberous Sclerosis-2 Product. TUBERIN POSSESSES SPECIFIC Rap1GAP ACTIVITY

Wienecke, R., König, A., & DeClue, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.27.16409 · Cited by 357

The Tuberous Sclerosis Protein TSC2 Is Not Required for the Regulation of the Mammalian Target of Rapamycin by Amino Acids and Certain Cellular Stresses

Smith, E. M., FINN, S. G., Tee, A. R., Browne, G. J., & Proud, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414499200 · Cited by 354

Rheb Binding to Mammalian Target of Rapamycin (mTOR) Is Regulated by Amino Acid Sufficiency

Long, X., Ortiz-Vega, S., Lin, Y., & Avruch, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500169200 · Cited by 349

The Tuberous Sclerosis 2 Gene Product, Tuberin, Functions as a Rab5 GTPase Activating Protein (GAP) in Modulating Endocytosis

Xiao, G., Shoarinejad, F., Jin, F., Golemis, E. A., & Yeung, R. S. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6097 · Cited by 348

Linkage of an important gene locus for tuberous sclerosis to a chromosome 16 marker for polycystic kidney disease

Kandt, R. S., Haines, J. L., Smith, M., Northrup, H., Gardner, R. J. M., Short, M. P., Dumars, K., Roach, E. S., Steingold, S., Wall, S. A., et al. (1992) · Nature Genetics · doi:10.1038/ng0992-37 · Cited by 335

A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt

Aoki, M., Blazek, E., & Vogt, P. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.136 · Cited by 311

S6K1 Regulates GSK3 under Conditions of mTOR-Dependent Feedback Inhibition of Akt

Zhang, H. H., Lipovsky, A. I., Dibble, C. C., Şahin, M., & Manning, B. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.09.019 · Cited by 309

Proteomic Analysis Reveals Hyperactivation of the Mammalian Target of Rapamycin Pathway in Neurofibromatosis 1–Associated Human and Mouse Brain Tumors

Dasgupta, B., Yi, Y., Chen, D. Y., Weber, J. D., & Gutmann, D. H. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4058 · Cited by 308

The hypoxia-induced paralogs Scylla and Charybdis inhibit growth by down-regulating S6K activity upstream of TSC in DrosophilaPreprint

Reiling, J. H., & Hafen, E. (2004) · Genes & Development · doi:10.1101/gad.322704 · Cited by 306

Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase

Hsu, Y., Chern, J. J., Cai, Y., Liu, M., & Choi, K. (2007) · Nature · doi:10.1038/nature05528 · Cited by 303

Activated mammalian target of rapamycin pathway in the pathogenesis of tuberous sclerosis complex renal tumors.

Kenerson, H. L., Aicher, L. D., True, L. D., & Yeung, R. S. W. (2002) · PubMed · Cited by 282

A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of mTOR signalling

Findlay, G. M., Yan, L., Procter, J., Mieulet, V., & Lamb, R. F. (2007) · Biochemical Journal · doi:10.1042/bj20061881 · Cited by 267

Genetic control of cell size.

Stocker, H., & Hafen, E. (2000) · Current Opinion in Genetics and Development · doi:10.1016/s0959-437x(00)00123-4 · Cited by 257

New roles for the LKB1→AMPK pathway

Hardie, D. G. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.01.006 · Cited by 256

The tuberous sclerosis-1 (TSC1) gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination

Benvenuto, G., Li, S., Brown, S. J., Braverman, R., Vass, W. C., Cheadle, J. P., Halley, D. J. J., Sampson, J. R., Wienecke, R., & DeClue, J. E. (2000) · Oncogene · doi:10.1038/sj.onc.1204009 · Cited by 253

Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles.

Plank, T. L., Yeung, R. S. W., & Henske, E. P. (1998) · PubMed · Cited by 251

Akt deficiency impairs normal cell proliferation and suppresses oncogenesis in a p53-independent and mTORC1-dependent manner

Skeen, J. E., Bhaskar, P. T., Chen, C.-C., Chen, W. S., Peng, X.-D., Nogueira, V., Hahn-Windgassen, A., Kiyokawa, H., & Hay, N. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.022 · Cited by 236

Feedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2Preprint

Manning, B. D., Logsdon, M. N., Lipovsky, A. I., Abbott, D. W., Kwiatkowski, D. J., & Cantley, L. C. (2005) · Genes & Development · doi:10.1101/gad.1314605 · Cited by 236

TSC1 Stabilizes TSC2 by Inhibiting the Interaction between TSC2 and the HERC1 Ubiquitin Ligase

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Inactivation of the Tuberous Sclerosis Complex-1 and -2 Gene Products Occurs by Phosphoinositide 3-Kinase/Akt-dependent and -independent Phosphorylation of Tuberin

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Quantitative phosphorylation profiling of the ERK/p90 ribosomal S6 kinase-signaling cassette and its targets, the tuberous sclerosis tumor suppressors

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Sirolimus Therapy in Tuberous Sclerosis or Sporadic Lymphangioleiomyomatosis

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Tuberous sclerosis complex tumor suppressor–mediated S6 kinase inhibition by phosphatidylinositide-3-OH kinase is mTOR independent

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TORC1 Is Essential for NF1-Associated Malignancies

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Mutation in TSC2 and activation of mammalian target of rapamycin signalling pathway in renal angiomyolipoma

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Multiple Mechanisms Control Phosphorylation of PHAS-I in Five (S/T)P Sites That Govern Translational Repression

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Lethality of Drosophila lacking TSC tumor suppressor function rescued by reducing dS6K signalingPreprint

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Characterization of the Cytosolic Tuberin-Hamartin Complex

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Efficacy of a rapamycin analog (CCI‐779) and IFN‐γ in tuberous sclerosis mouse models

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The p38 and MK2 Kinase Cascade Phosphorylates Tuberin, the Tuberous Sclerosis 2 Gene Product, and Enhances Its Interaction with 14-3-3

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Loss of Tsc1 or Tsc2 induces vascular endothelial growth factor production through mammalian target of rapamycin.

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DrosophilaRheb GTPase is required for cell cycle progression and cell growth

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The GAP-Related Domain of Tuberin, the Product of the TSC2 Gene, is a Target for Missense Mutations in Tuberous Sclerosis

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Identification of S664 TSC2 Phosphorylation as a Marker for Extracellular Signal-Regulated Kinase–Mediated mTOR Activation in Tuberous Sclerosis and Human Cancer

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Regulation of the small GTPase Rheb by amino acids

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AKT Activation in Human Glioblastomas Enhances Proliferation via TSC2 and S6 Kinase Signaling

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Rheb is in a high activation state and inhibits B-Raf kinase in mammalian cells

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Lhermitte-Duclos Disease: A Report of 31 Cases with Immunohistochemical Analysis of the PTEN/AKT/mTOR Pathway

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Suppression of tumorigenicity by the wild-type tuberous sclerosis 2 (Tsc2) gene and its C-terminal region.

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Pathological mutations in TSC1 and TSC2 disrupt the interaction between hamartin and tuberin

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Renal Angiomyolipomas from Patients with Sporadic Lymphangiomyomatosis Contain Both Neoplastic and Non-Neoplastic Vascular Structures

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Analysis of mTOR signaling by the small G‐proteins, Rheb and RhebL1

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TSC2 missense mutations inhibit tuberin phosphorylation and prevent formation of the tuberin-hamartin complex

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Identification of Dominant Negative Mutants of Rheb GTPase and Their Use to Implicate the Involvement of Human Rheb in the Activation of p70S6K

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Role of the Tsc1-Tsc2 Complex in Signaling and Transport Across the Cell Membrane in the Fission YeastSchizosaccharomyces pombe

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Tsc2 is not a critical target of Akt during normal Drosophila developmentPreprint

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Aberrant β-Catenin Signaling in Tuberous Sclerosis

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Molecular Pathogenesis of Tuber Formation in Tuberous Sclerosis Complex

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Cell size regulation by the human TSC tumor suppressor proteins depends on PI3K and FKBP38

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Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, Rheb, in fission yeast

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Cell Cycle-regulated Phosphorylation of Hamartin, the Product of the Tuberous Sclerosis Complex 1 Gene, by Cyclin-dependent Kinase 1/Cyclin B

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Identification and Characterization of the Interaction between Tuberin and 14-3-3ζ

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14-3-3β Binds to and Negatively Regulates the Tuberous Sclerosis Complex 2 (TSC2) Tumor Suppressor Gene Product, Tuberin

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Negative Regulation of TSC1-TSC2 by Mammalian D-Type Cyclins

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Suppression of Peutz-Jeghers Polyposis by Targeting Mammalian Target of Rapamycin Signaling

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Multicompartmental distribution of the tuberous sclerosis gene products, hamartin and tuberin

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Tuberous sclerosis preclinical studies: timing of treatment, combination of a rapamycin analog (CCI-779) and interferon-gamma, and comparison of rapamycin to CCI-779

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mTOR Signaling in Growth, Metabolism, and Disease

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Targeting PI3K signalling in cancer: opportunities, challenges and limitations

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Activation of a metabolic gene regulatory network downstream of mTOR complex 1

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Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways

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The LKB1-AMPK pathway: metabolism and growth control in tumour suppression

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The TSC1–TSC2 Complex

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Defining the biochemical functions of the TSC complex and its regulation of Rheb-mTORC1 signaling

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The tuberous sclerosis complex: balancing proliferation and survival

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TBC1D7 Is a Third Subunit of the TSC1-TSC2 Complex Upstream of mTORC1

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