Ten years of protein kinase B signalling: a hard Akt to follow

Brazil, Derek P.; Hemmings, Brian A.

doi:10.1016/s0968-0004(01)01958-2

Cited by 1,177PI3K/AKT/mTOR signaling in cancerMetabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase Signaling

Ten years of protein kinase B signalling: a hard Akt to follow

Brazil, Derek P., Hemmings, Brian A.·2001·Trends in Biochemical Sciences

DOI 10.1016/s0968-0004(01)01958-2

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Abstract

It is ten years since the publication of three papers describing the cloning of a new proto-oncogene serine/threonine kinase termed protein kinase B (PKB)/Akt. Key roles for this protein kinase in cellular processes such as glucose metabolism, cell proliferation, apoptosis, transcription and cell migration are now well established. The explosion of publications involving PKB/Akt in the past three years emphasizes the high level of current interest in this signalling molecule. This review focuses on tracing the characterization of this kinase, through the elucidation of its mechanism of regulation, to its role in regulating physiological and pathophysiological processes, to our current understanding of the biology of PKB/Akt, and prospects for the future.

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Elevated PKB activity via amplification of PI3K and PKB genes, mutational loss of PTEN, or activation of oncogenic receptor tyrosine kinase is a common feature of many human cancers.
“Elevated PKB activity via amplification of PI3K and PKB genes, mutational loss of PTEN, or activation of oncogenic receptor tyrosine kinase is a common feature of many human cancers (1,4,43).”
From Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation (2004) · cites this paper as [4]

The sequence of the human genome
Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., Holt, R. A., et al. (2001) · Science · doi:10.1126/science.1058040 · Cited by 13,909 · see citing works
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 6,535 · see citing works
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689 · see citing works
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244 · see citing works
Self-citation
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216 · see citing works
The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104 · see citing works
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha.
Alessi, D., James, S., Downes, C., Holmes, A. B., Gaffney, P., Reese, C., & Cohen, P. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00122-9 · Cited by 3,047 · see citing works
Mechanism of activation of protein kinase B by insulin and IGF‐1.
Alessi, D. R., Andjelković, M., Caudwell, B., Cron, P. D., MORRICE, N. A., Cohen, P., & Hemmings, B. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01045.x · Cited by 3,007 · see citing works
Self-citation
Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
Stambolic, V., Suzuki, A., de la Pompa, J. L., Brothers, G. M., Mirtsos, C., Sasaki, T., Ruland, J., Penninger, J. M., Siderovski, D. P., & Mak, T. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81780-8 · Cited by 2,551 · see citing works
Regulation of neuronal survival by the serine-threonine protein kinase Akt
Dudek, H., Datta, S. R., Franke, T. F., Birnbaum, M. J., Yao, R., Cooper, G. M., Segal, R. A., Kaplan, D. R., & Greenberg, M. E. (1997) · Science · doi:10.1126/science.275.5300.661 · Cited by 2,436 · see citing works
Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
del Peso, L., González‐García, M., Page, C., Herrera, R., & Núñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 2,213 · see citing works
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
Burgering, B. M. T., & Coffer, P. J. (1995) · Nature · doi:10.1038/376599a0 · Cited by 2,113 · see citing works
New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
Cantley, L. C., & Neel, B. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4240 · Cited by 2,007 · see citing works
The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
Franke, T. F., Yang, S., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., & Tsichlis, P. N. (1995) · Cell · doi:10.1016/0092-8674(95)90534-0 · Cited by 2,006 · see citing works
Insulin Resistance and a Diabetes Mellitus-Like Syndrome in Mice Lacking the Protein Kinase Akt2 (PKBβ)
Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,837 · see citing works
Pten is essential for embryonic development and tumour suppression
Cristofano, A. D., Pesce, B., Cordon‐Cardo, C., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/1235 · Cited by 1,518 · see citing works
Requirement for Phosphatidylinositol-3 Kinase in the Prevention of Apoptosis by Nerve Growth Factor
Yao, R., & Cooper, G. M. (1995) · Science · doi:10.1126/science.7701324 · Cited by 1,390 · see citing works
Expression of a Constitutively Active Akt Ser/Thr Kinase in 3T3-L1 Adipocytes Stimulates Glucose Uptake and Glucose Transporter 4 Translocation
Kohn, A. D., Summers, S. A., Birnbaum, M. J., & Roth, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31372 · Cited by 1,284 · see citing works
Dual Role of Phosphatidylinositol-3,4,5-trisphosphate in the Activation of Protein Kinase B
Stokoe, D., Stephens, L. R., Copeland, T., Gaffney, P. R. J., Reese, C. B., Painter, G. F., Holmes, A. B., McCormick, F. P., & Hawkins, P. T. (1997) · Science · doi:10.1126/science.277.5325.567 · Cited by 1,202 · see citing works
The Multiple Roles of PTEN in Tumor Suppression
Di Cristofano, A., & Pandolfi, P. P. (2000) · Cell · doi:10.1016/s0092-8674(00)80674-1 · Cited by 1,182 · see citing works
The lipid phosphatase activity of PTEN is critical for its tumor supressor function
Myers, M. P., Pass, I., Batty, I. H., KAAY, J. V. D., Stolarov, J. P., Hemmings, B. A., Wigler, M. H., Downes, C. P., & Tonks, N. K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13513 · Cited by 1,161 · see citing works
Self-citation
Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
Arcaro, A., & Wymann, M. P. (1993) · Biochemical Journal · doi:10.1042/bj2960297 · Cited by 1,146 · see citing works
Phosphatidylinositol 3-Kinase Activation Is Required for Insulin Stimulation of pp70 S6 Kinase, DNA Synthesis, and Glucose Transporter Translocation
Cheatham, B., Vlahos, C. J., Cheatham, L. A., Wang, L., Blenis, J., & Kahn, C. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4902-4911.1994 · Cited by 1,067 · see citing works
Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B
Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061 · see citing works
Role of Translocation in the Activation and Function of Protein Kinase B
Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31515 · Cited by 1,051 · see citing works
Self-citation
A Retroviral Oncogene, akt , Encoding a Serine-Threonine Kinase Containing an SH2-Like Region
Bellacosa, A., Testa, J. R., Staal, S. P., & Tsichlis, P. N. (1991) · Science · doi:10.1126/science.1833819 · Cited by 939 · see citing works
PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells
Auger, K. R., Serunian, L. A., Soltoff, S. P., Libby, P., & Cantley, L. C. (1989) · Cell · doi:10.1016/0092-8674(89)90182-7 · Cited by 910 · see citing works
Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP.
D'Mello, S. R., Galli, C., Ciotti, T., & Calissano, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10989 · Cited by 892 · see citing works
The Regulation and Activities of the Multifunctional Serine/Threonine Kinase Akt/PKB
Kandel, E., & Hay, N. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4690 · Cited by 867 · see citing works
P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase
Myers, M. P., Stolarov, J. P., Eng, C., Li, J., Wang, S. I., Wigler, M. H., Parsons, R. E., & Tonks, N. K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9052 · Cited by 775 · see citing works
Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma.
Staal, S. P. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.14.5034 · Cited by 772 · see citing works
Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
Harlan, J. E., Hajduk, P. J., Yoon, H. S., & Fesik, S. W. (1994) · Nature · doi:10.1038/371168a0 · Cited by 761 · see citing works
AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas.
Cheng, J. Q., Godwin, A. K., Bellacosa, A., Taguchi, T., Franke, T. F., Hamilton, T. C., Tsichlis, P. N., & Testa, J. R. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.19.9267 · Cited by 737 · see citing works
3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase
Alessi, D. R., Deák, M., Casamayor, A., Caudwell, F. B., MORRICE, N. A., Norman, D. G., Gaffney, P. R. J., Reese, C. B., MacDougall, C. N., Harbison, D., et al. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00336-8 · Cited by 737 · see citing works
PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase
Chung, J., Grammar, T. C., Lemon, K. P., Kazlauskas, A., & Blenis, J. (1994) · Nature · doi:10.1038/370071a0 · Cited by 719 · see citing works
Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression
Whang, Y. E., Wu, X., Suzuki, H., Reiter, R. E., Tran, C., Vessella, R. L., SAID, J. W., Isaacs, W. B., & Sawyers, C. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5246 · Cited by 639 · see citing works
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 · see citing works
Self-citation
Purification and characterization of phosphoinositide 3-kinase from rat liver.
Carpenter, C. L., Duckworth, B. C., Auger, K. R., Cohen, B. B., Schaffhausen, B. S., & Cantley, L. C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45429-9 · Cited by 627 · see citing works
Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.
Jones, P. F., Jakubowicz, T., Pitossi, F. J., Maurer, F., & Hemmings, B. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4171 · Cited by 532 · see citing works
Self-citation
Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors.
Andjelkovic, M., Jakubowicz, T., Cron, P., Ming, X., Han, J. W., & Hemmings, B. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.12.5699 · Cited by 525 · see citing works
Self-citation
Activation of phosphatidylinositol 3-kinase by insulin.
Ruderman, N. B., Kapeller, R., White, M. F., & Cantley, L. C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1411 · Cited by 511 · see citing works
Molecular cloning and characterisation of a novel putative protein‐serine kinase related to the cAMP‐dependent and protein kinase C families
Coffer, P. J., & Woodgett, J. R. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16305.x · Cited by 493 · see citing works
Pleckstrin domain homology
Haslam, R. J., Koide, H., & Hemmings, B. A. (1993) · Nature · doi:10.1038/363309b0 · Cited by 480 · see citing works
Self-citation
Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC
Haas-Kogan, D. A., Shalev, N., Wong, M. P., Mills, G. B., Yount, G. L., & Stokoe, D. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00493-9 · Cited by 477 · see citing works
The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
Williams, M. R., Arthur, J. S. C., Balendran, A., KAAY, J. V. D., Poli, V., Cohen, P., & Alessi, D. R. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00441-3 · Cited by 471 · see citing works
High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity
Frech, M., Andjelković, M., Ingley, E., Reddy, K. K., Falck, J. R., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8474 · Cited by 446 · see citing works
Self-citation
Membrane Localization of Phosphatidylinositol 3-Kinase Is Sufficient To Activate Multiple Signal-Transducing Kinase Pathways
Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M.-A., & Williams, L. T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4117 · Cited by 441 · see citing works
A putative modular domain present in diverse signaling proteins
Mayer, B. J., Ren, R., Clark, K., & Baltimore, D. (1993) · Cell · doi:10.1016/0092-8674(93)90244-k · Cited by 440 · see citing works
Peptide and Protein Library Screening Defines Optimal Substrate Motifs for AKT/PKB
Obata, T., Yaffe, M. B., Leparc, G., Piro, E. T., Maegawa, H., Kashiwagi, A., Kikkawa, R., & Cantley, L. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005497200 · Cited by 388 · see citing works
Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ
Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30491 · Cited by 378 · see citing works
Self-citation
Insulin stimulates the kinase activity of RAC‐PK, a pleckstrin homology domain containing ser/thr kinase.
Kohn, A. D., Kovacina, K. S., & Roth, R. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00103.x · Cited by 355 · see citing works
Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
James, S. R., Downes, C. P., Gigg, R., Grove, S. J. A., Holmes, A. B., & Alessi, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3150709 · Cited by 339 · see citing works
Inhibition of Nuclear Import by Protein Kinase B (Akt) Regulates the Subcellular Distribution and Activity of the Forkhead Transcription Factor AFX
Brownawell, A. M., Kops, G. J. P. L., Macara, I. G., & Burgering, B. M. T. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3534-3546.2001 · Cited by 313 · see citing works
Isolation of transforming murine leukemia viruses from mice with a high incidence of spontaneous lymphoma.
Staal, S. P., Hartley, J. W., & Rowe, W. P. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.7.3065 · Cited by 282 · see citing works
Activation of Akt (Protein Kinase B) in Mammary Epithelium Provides a Critical Cell Survival Signal Required for Tumor Progression
Hutchinson, J. N., Jin, J., Cardiff, R. D., Woodgett, J. R., & Muller, W. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.2203-2212.2001 · Cited by 281 · see citing works
Carboxyl-Terminal Modulator Protein (CTMP), a Negative Regulator of PKB/Akt and v-Akt at the Plasma Membrane
Maira, S.-M., Galetić, I., Brazil, D. P., Kaech, S., Ingley, E., Thelen, M., & Hemmings, B. A. (2001) · Science · doi:10.1126/science.1062030 · Cited by 262 · see citing works
Self-citation
Activation of p70/p85 S6 kinase by a pathway independent of p21fi ras
Ming, X., Burgering, B. M. T., Wennström, S., Claesson, L., Heldin, C. H., Bos, J. L., Kozma, S. C., & Thomas, G. (1994) · Nature · doi:10.1038/371426a0 · Cited by 206 · see citing works
Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes.
Thelen, M., Wymann, M. P., & Langen, H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4960 · Cited by 206 · see citing works
Molecular cloning of a second form of rac protein kinase.
Jones, P. F., Jakubowicz, T., & Hemmings, B. A. (1991) · Cell Regulation · doi:10.1091/mbc.2.12.1001 · Cited by 187 · see citing works
Self-citation
AH/PH Domain-Mediated Interaction between Akt Molecules and Its Potential Role in Akt Regulation
Datta, K., Franke, T. F., Chan, T. O., Makris, A. M., Yang, S.-I., Kaplan, D. R., Morrison, D. K., Golemis, E. A., & Tsichlis, P. N. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.4.2304 · Cited by 164 · see citing works
Constitutive activation of protein kinase B and phosphorylation of p47 phox by a membrane-targeted phosphoinositide 3-kinase
Didichenko, S. A., Tilton, B., Hemmings, B. A., Ballmer‐Hofer, K., & Thelen, M. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70713-6 · Cited by 131 · see citing works
Self-citation
Mechanism of protein kinase B activation by insulin/insulin-like growth factor-1 revealed by specific inhibitors of phosphoinositide 3-kinase--significance for diabetes and cancer.
Galetic, I., Andjelkovic, M., Meier, R., Brodbeck, D., Park, J., & Hemmings, B. (1999) · Pharmacology and Therapeutics · doi:10.1016/s0163-7258(98)00071-0 · Cited by 122 · see citing works
Self-citation
Phosphoinositide-Regulated Kinases and Phosphoinositide Phosphatases
Leslie, N. R., Biondi, R. M., & Alessi, D. R. (2001) · Chemical Reviews · doi:10.1021/cr000091i · Cited by 121 · see citing works
Growth factor-dependent survival of rodent fibroblasts requires phosphatidylinositol 3-kinase but is independent of pp70S6K activity.
Yao, R., & Gm, C. (1996) · PubMed · Cited by 120 · see citing works
Structural Characterization of the Interaction between a Pleckstrin Homology Domain and Phosphatidylinositol 4,5-Bisphosphate
Harlan, J. E., Yoon, H. S., Hajduk, P. J., & Fesik, S. W. (1995) · Biochemistry · doi:10.1021/bi00031a006 · Cited by 118 · see citing works
Thymic lymphoma induction by the AKT8 murine retrovirus.
Staal, S. P., & Hartley, J. W. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.3.1259 · Cited by 100 · see citing works
Developmental Regulation of Expression and Activity of Multiple Forms of the Drosophila RAC Protein Kinase
Andjelković, M., Jones, P. F., Grossniklaus, U., Cron, P. D., Schier, A. F., Dick, M. S., Bilbe, G., & Hemmings, B. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.8.4066 · Cited by 57 · see citing works
Self-citation

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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 · see citing works
Rules for Making Human Tumor Cells
Hahn, W. C., & Weinberg, R. A. (2002) · New England Journal of Medicine · doi:10.1056/nejmra021902 · Cited by 951 · see citing works
TRB3: A <i>tribbles</i> Homolog That Inhibits Akt/PKB Activation by Insulin in Liver
Du, K., Herzig, S., Kulkarni, R. N., & Montminy, M. (2003) · Science · doi:10.1126/science.1079817 · Cited by 842 · see citing works
Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis
Basu, S., Totty, N. F., Irwin, M. S., Sudol, M., & Downward, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00776-1 · Cited by 843 · see citing works
Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKBβ
Garofalo, R. S., Orena, S. J., Rafidi, K., Torchia, A. J., Stock, J. L., Hildebrandt, A. L., Coskran, T., Black, S. C., Brees, D. J., Wicks, J. R., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16885 · Cited by 726 · see citing works
FKBP51 Affects Cancer Cell Response to Chemotherapy by Negatively Regulating Akt
Pei, H., Li, L., Fridley, B. L., Jenkins, G. D., Kalari, K. R., Lingle, W., Petersen, G., Lou, Z., & Wang, L. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.07.016 · Cited by 709 · see citing works
IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works
PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms
Brognard, J., Sierecki, E., Gao, T., & Newton, A. C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.017 · Cited by 591 · see citing works
PGC-1 promotes insulin resistance in liver through PPAR-α-dependent induction of TRB-3
Koo, S.-H., Satoh, H., Herzig, S., Lee, C.-H., Hedrick, S., Kulkarni, R., Evans, R. M., Olefsky, J., & Montminy, M. (2004) · Nature Medicine · doi:10.1038/nm1044 · Cited by 550 · see citing works
Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539 · see citing works
How does diabetes accelerate Alzheimer disease pathology?
Sims-Robinson, C., Kim, B., Rosko, A., & Feldman, E. L. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.130 · Cited by 492 · see citing works
A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142166599 · Cited by 402 · see citing works
The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
Berwick, D. C., Hers, I., Heesom, K. J., Moule, S. K., & Tavareá, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204681200 · Cited by 383 · see citing works
Insulin signaling through Akt/protein kinase B analyzed by small interfering RNA-mediated gene silencing
Jiang, Z. Y., Zhou, Q. L., Coleman, K. A., Chouinard, M., Boese, Q., & Czech, M. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332633100 · Cited by 378 · see citing works
Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation
Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294 · see citing works
Self-citation
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Rochette-Egly, C. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00115-8 · Cited by 291 · see citing works
Extensive In Vivo Metabolite-Protein Interactions Revealed by Large-Scale Systematic Analyses
Li, X., Gianoulis, T. A., Yip, K. Y., Gerstein, M., & Snyder, M. (2010) · Cell · doi:10.1016/j.cell.2010.09.048 · Cited by 237 · see citing works
Stress increases vulnerability to inflammation in the rat prefrontal cortex
de Pablos, R. M., Villarán, R. F., Argüelles, S., Herrera, A. J., Venero, J. L., Ayala, A., Cano, J., & Machado, A. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0802-06.2006 · Cited by 215 · see citing works
Sixteen years and counting: The current understanding of fibroblast growth factor receptor 3 (FGFR3) signaling in skeletal dysplasias
Foldynova-Trantirkova, S., Wilcox, W. R., & Krejci, P. (2012) · Human Mutation · doi:10.1002/humu.21636 · Cited by 216 · see citing works
Use of RNA Interference-mediated Gene Silencing and Adenoviral Overexpression to Elucidate the Roles of AKT/Protein Kinase B Isoforms in Insulin Actions
Katome, T., Obata, T., Matsushima, R., Masuyama, N., Cantley, L. C., Gotoh, Y., Kishi, K., Shiota, H., & Ebina, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302094200 · Cited by 212 · see citing works
Practical uses for ecdysteroids in mammals including humans: and update
Lafont, R., & Dinan, L. (2003) · Journal of Insect Science · doi:10.1093/jis/3.1.7 · Cited by 196 · see citing works
Practical uses for ecdysteroids in mammals including humans: And update
Lafont, R., & Dinan, L. (2003) · Journal of Insect Science · doi:10.1673/031.003.0701 · Cited by 196 · see citing works
Cannabidiol, a non-psychoactive cannabinoid compound, inhibits proliferation and invasion in U87-MG and T98G glioma cells through a multitarget effect
Solinas, M., Massi, P., Cinquina, V., Valenti, M., Bolognini, D., Gariboldi, M., Monti, E., Rubino, T., & Parolaro, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076918 · Cited by 159 · see citing works
Stress is critical for LPS-induced activation of microglia and damage in the rat hippocampus
Espinosa-Oliva, A. M., de Pablos, R. M., Villarán, R. F., Argüelles, S., Venero, J. L., Machado, A., & Cano, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.01.012 · Cited by 151 · see citing works
Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: Implications for synaptic dysfunction and neuronal damage
Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147 · see citing works
Diabetes drugs in the fight against Alzheimer's disease
Boccardi, V., Murasecco, I., & Mecocci, P. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100936 · Cited by 142 · see citing works
Zoledronate Sensitizes Endothelial Cells to Tumor Necrosis Factor-induced Programmed Cell Death
Bezzi, M., Hasmim, M., Bieler, G., Dormond, O., & Rüegg, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308114200 · Cited by 139 · see citing works
Joggin’ the Noggin: Towards a Physiological Understanding of Exercise-Induced Cognitive Benefits
Stimpson, N. J., Davison, G., & Javadi, A.-H. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.03.018 · Cited by 134 · see citing works
Mechanism of B-Cell Receptor-Induced Phosphorylation and Activation of Phospholipase C-γ2
Kim, Y. J., Sekiya, F., Poulin, B., Bae, Y. S., & Rhee, S. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9986-9999.2004 · Cited by 126 · see citing works
Insight into the Role of the PI3K/Akt Pathway in Ischemic Injury and Post-Infarct Left Ventricular Remodeling in Normal and Diabetic Heart
Walkowski, B., Kleibert, M., Majka, M., & Wojciechowska, M. (2022) · Cells · doi:10.3390/cells11091553 · Cited by 117 · see citing works
TGF-β1 protects against Aβ-neurotoxicity via the phosphatidylinositol-3-kinase pathway
Caraci, F., Battaglia, G., Busceti, C., Biagioni, F., Mastroiacovo, F., Bosco, P., Drago, F., Nicoletti, F., Sortino, M. A., & Copani, A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.01.007 · Cited by 79 · see citing works
Persistent activation of ERK1/2 by lead acetate increases nucleotide excision repair synthesis and confers anti-cytotoxicity and anti-mutagenicity
Lin, Y.-W. (2003) · Carcinogenesis · doi:10.1093/carcin/24.1.53 · Cited by 51 · see citing works
A role for nuclear β-catenin in SNRI antidepressant-induced hippocampal cell proliferation
Mostany, R., Valdizán, E. M., & Pazos, A. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.04.012 · Cited by 47 · see citing works
Upstream signaling events leading to elevated production of pro-survival nitric oxide in photodynamically-challenged glioblastoma cells
Fahey, J. M., Korytowski, W., & Girotti, A. W. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.013 · Cited by 38 · see citing works
Geniposide Attenuates the Phosphorylation of Tau Protein in Cellular and Insulin‐deficient APP/PS1 Transgenic Mouse Model of Alzheimer's Disease
Zhang, Y., Yin, F., Liu, J., & Liu, Z. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12673 · Cited by 34 · see citing works
Artemisia scoparia Enhances Adipocyte Development and Endocrine Function In Vitro and Enhances Insulin Action In Vivo
Richard, A. J., Fuller, S., Fedorcenco, V., Beyl, R., Burris, T. P., Mynatt, R., Ribnicky, D. M., & Stephens, J. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098897 · Cited by 30 · see citing works

The PI3K/Akt Pathway: Recent Progress in the Development of ATP-Competitive and Allosteric Akt Kinase Inhibitors
Lindsley, C. W., Barnett, S. F., Layton, M. E., et al. (2008) · Current Cancer Drug Targets · doi:10.2174/156800908783497096 · Cited by 87 · see citing works
Characterization of Akt overexpression in MiaPaCa-2 cells: prohibitin is an Akt substrate both in vitro and in cells.
Han, E. K.-H., McGonigal, T. P., Butler, C., et al. (2008) · PubMed · Cited by 49 · see citing works
Tumor cell sensitization to apoptotic stimuli by selective inhibition of specific Akt/PKB family members
Defeo-Jones, D., Barnett, S. F., Fu, S., Hancock, P. J., Haskell, K., Leander, K. R., McAvoy, E., Robinson, R., Duggan, M. E., Lindsley, C. W., et al. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.271.4.2 · Cited by 173 · see citing works
The activation of Akt/PKB signaling pathway and cell survival
Song, G., Ouyang, G., & Bao, S. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00337.x · Cited by 1,891 · see citing works
Isoform-Specific Role of Akt Kinase in Cancer and its Selective Targeting by Potential Anticancer Natural Agents
Roy, N. K., Monisha, J., Singh, A. K., et al. (2019) · The Natural Products Journal · doi:10.2174/2210315509666190314145257 · Cited by 5 · see citing works

Authors: Brazil, D. P., & Hemmings, B. A.
Affiliations: Friedrich Miescher Institute (CH)
ORCID: Brazil, Derek P.
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2001-11
Volume: 26
Issue: 11
Pages: 657-664
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/s0968-0004(01)01958-2
OpenAlex: W2020931266
Cited by: 1,177
References: 67
Citations by year: 2026: 8 · 2025: 19 · 2024: 20 · 2023: 18 · 2022: 18 · 2021: 24 · 2020: 44 · 2019: 21 · 2018: 29 · 2017: 39 · 2016: 29 · 2015: 40 · 2014: 44 · 2013: 43 · 2012: 56
FWCI: 7.29
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: Akt, serine/threonine kinase, proto-oncogenes, kinase regulation, glucose metabolism, cell proliferation, apoptosis, transcription, cell migration, signaling pathways
MeSH terms: Proto-Oncogene Mas, Amino Acid Sequence, Animals, Enzyme Activation, Humans, Models, Biological, Phosphorylation, Proto-Oncogene Proteins, Signal Transduction, Gene Expression Regulation, Enzymologic, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Lipid Metabolism, Proto-Oncogene Proteins c-akt

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Ten years of protein kinase B signalling: a hard Akt to follow

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