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Molecular-cloning and characterization of a novel putative protein-serine kinase related to the cAMP-dependent and protein-kinase-C families
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A retroviral oncogene Akt, encoding a serine-threonine kinase containing an SH2-like region
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Belacossa A, Testa JR, Staal SP, Tsichlis PN. A retroviral oncogene Akt, encoding a serine-threonine kinase containing an SH2-like region. Science. 254:1991;244-247.
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Belacossa, A.1
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0025882091
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Molecular cloning and identification of a serine threonine protein-kinase of the 2nd-messenger subfamily
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Jones PF, Jakubowicz T, Pitossi FJ, Maurer F, Hemmings BA. Molecular cloning and identification of a serine threonine protein-kinase of the 2nd-messenger subfamily. Proc Natl Acad Sci USA. 88:1991;4171-4175.
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Jones, P.F.1
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Hemmings, B.A.5
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4
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0026667730
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Akt2, a putative oncogene encoding a member of a subfamily of protein-serine threonine kinases, is amplified in human ovarian carcinomas
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Cheng JQ, Godwin AK, Bellacosa A, Taguchi T, Franke TF, Hamilton TC, Tsichlis PN, Testa JR. Akt2, a putative oncogene encoding a member of a subfamily of protein-serine threonine kinases, is amplified in human ovarian carcinomas. Proc Natl Acad Sci USA. 89:1992;9267-9271.
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Cheng, J.Q.1
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Franke, T.F.5
Hamilton, T.C.6
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Testa, J.R.8
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5
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0028799420
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Molecular-cloning and characterization of a new member of the RAC protein-kinase family - Association of the Pleckstrin homology domain of 3 types of RAC protein-kinase with protein-kinase-C subspecies and βγ-subunits of G-protein-kinase-C subspecies and bg-subunits of G-proteins
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Konishi H, Kuroda S, Tanaka M, Matsuzaki H, Ono Y, Kameyama K, Haga T, Kikkawa U. Molecular-cloning and characterization of a new member of the RAC protein-kinase family - association of the Pleckstrin homology domain of 3 types of RAC protein-kinase with protein-kinase-C subspecies and βγ-subunits of G-protein-kinase-C subspecies and bg-subunits of G-proteins. Biochem Biophys Res Comm. 216:1995;526-534.
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Konishi, H.1
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Tanaka, M.3
Matsuzaki, H.4
Ono, Y.5
Kameyama, K.6
Haga, T.7
Kikkawa, U.8
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0029939448
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PH domains: Diverse sequences with a common fold recruit signalling molecules to the cell surface
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Lemmon M, Ferguson KM, Schlessinger J. PH domains: diverse sequences with a common fold recruit signalling molecules to the cell surface. Cell. 85:1996;621-624.
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Lemmon, M.1
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The pleckstrin-homolgy domain, an intrguing multifunctional protein module
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Shaw, G.1
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The protein-kinase encoded by the Akt protooncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
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Franke TF, Yang SI, Chan TO, Datta K, Kazlauskas A, Morrison DK, Kaplan DR, Tsichlis PN. The protein-kinase encoded by the Akt protooncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 81:1995;727-736.
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Franke, T.F.1
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Kazlauskas, A.5
Morrison, D.K.6
Kaplan, D.R.7
Tsichlis, P.N.8
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0029160069
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Protein-kinase-B (c-Akt) in phosphatidylinositol-3-OH kinase signal-transduction
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Burgering BMT, Coffer PJ. Protein-kinase-B (c-Akt) in phosphatidylinositol-3-OH kinase signal-transduction. Nature. 376:1995;599-602.
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Burgering, B.M.T.1
Coffer, P.J.2
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0029143388
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Insulin stimulates the kinase-activity of RAC-PK, a pleckstrin-homology domain-containing Ser/Thr kinase
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Kohn AD, Kovacina KS, Roth RA. Insulin stimulates the kinase-activity of RAC-PK, a pleckstrin-homology domain-containing Ser/Thr kinase. EMBO J. 14:1995;4288-4295.
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Kohn, A.D.1
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Roth, R.A.3
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11
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Activation of the PKBβ and PKBγ isoforms by insulin in vivo and PDK1 in vitro: Comparison with PKBα
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in press
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Walker KS, Deak M, Paterson A, Hudson K, Cohen P, Alessi DR. Activation of the PKBβ and PKBγ isoforms by insulin in vivo and PDK1 in vitro: comparison with PKBα Biochem J. 1998;. in press.
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Walker, K.S.1
Deak, M.2
Paterson, A.3
Hudson, K.4
Cohen, P.5
Alessi, D.R.6
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0030663666
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Inositol lipid 5-phosphatases - Traffic signals and signal traffic
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Woscholski R, Parker PJ. Inositol lipid 5-phosphatases - traffic signals and signal traffic. Trends Biochem Sci. 22:1997;427-431.
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Woscholski, R.1
Parker, P.J.2
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14
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Specific binding of the Akt-1 protein-kinase to phosphatidylinositol, 3,4,5-trisphosphate without subsequent activation
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James SR, Downes CP, Gigg R, Grove SJA, Holmes AB, Alessi DR. Specific binding of the Akt-1 protein-kinase to phosphatidylinositol, 3,4,5-trisphosphate without subsequent activation. Biochem J. 315:1996;709-713.
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James, S.R.1
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Gigg, R.3
Grove, S.J.A.4
Holmes, A.B.5
Alessi, D.R.6
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15
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0030991386
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High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin-homology domain of RAC/Protein kinase B and their influence on the kinase activity
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Frech M, Andjelkovic M, Falck JR, Hemmings BA. High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin-homology domain of RAC/Protein kinase B and their influence on the kinase activity. J Biol Chem. 272:1996;8474-8478.
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Frech, M.1
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Falck, J.R.3
Hemmings, B.A.4
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0031015986
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A specific product of phosphatidyinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
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Klippel A, Kavanaugh WM, Pot D, Williams LT. A specific product of phosphatidyinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol Cell Biol. 17:1997;338-344.
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Klippel, A.1
Kavanaugh, W.M.2
Pot, D.3
Williams, L.T.4
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0031039024
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Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
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Franke TF, Kaplan DR, Cantley LC, Toker A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science. 275:1997;665-668.
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Franke, T.F.1
Kaplan, D.R.2
Cantley, L.C.3
Toker, A.4
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18
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0031127305
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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B α
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of outstanding interest. This paper describes for the first time the identification of PDK1 and its purification from skeletal muscle and the characterisation of its biochemical properties. PDK1 phosphorylates Thr308 of PKB resulting in up to a 30-fold activation of this kinase only in the presence of lipid vesicles containing either the Ptdlns(3,4,5)P3 or Ptdlns(3,4)P2 lipid second messengers.
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Alessi DR, James SR, Downes CP, Holmes AB, Gaffney PRJ, Reese CB, Cohen P. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B α of outstanding interest Curr Biol. 7:1997;261-269 This paper describes for the first time the identification of PDK1 and its purification from skeletal muscle and the characterisation of its biochemical properties. PDK1 phosphorylates Thr308 of PKB resulting in up to a 30-fold activation of this kinase only in the presence of lipid vesicles containing either the Ptdlns(3,4,5)P3 or Ptdlns(3,4)P2 lipid second messengers.
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(1997)
Curr Biol
, vol.7
, pp. 261-269
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Alessi, D.R.1
James, S.R.2
Downes, C.P.3
Holmes, A.B.4
Gaffney, P.R.J.5
Reese, C.B.6
Cohen, P.7
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19
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0030799706
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Dual role of phosphatidyinositiol-3,4,5-trisphosphate in the activation of protein kinase B
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of outstanding interest. This paper describes an activity present in brain extracts that has similar properties to that of PDK1. It demonstrates that mutants of PKB which cannot interact with Ptdlns(3,4,5)P3 are not phosphorylated by PDK1. In contrast to the findings reported in [24], the rate at which PDK1 phosphorylated a PKBα mutant lacking the PH domain is claimed to be further increased by the addition of Ptdlns(3,4,5)P3.
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Stokoe D, Stephens LR, Copeland T, Gaffney PRJ, Reese CB, Painter GF. Dual role of phosphatidyinositiol-3,4,5-trisphosphate in the activation of protein kinase B. of outstanding interest Science. 277:1997;567-570 This paper describes an activity present in brain extracts that has similar properties to that of PDK1. It demonstrates that mutants of PKB which cannot interact with Ptdlns(3,4,5)P3 are not phosphorylated by PDK1. In contrast to the findings reported in [24], the rate at which PDK1 phosphorylated a PKBα mutant lacking the PH domain is claimed to be further increased by the addition of Ptdlns(3,4,5)P3.
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(1997)
Science
, vol.277
, pp. 567-570
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Stokoe, D.1
Stephens, L.R.2
Copeland, T.3
Gaffney, P.R.J.4
Reese, C.B.5
Painter, G.F.6
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20
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0029804116
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Mechanism of activation of protein kinase B by insulin and IGF1
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of special interest. This paper demonstrates that insulin or IGF1 stimulation of cells leads to the phosphorylation of PKBα at two residues namely Thr308 and Ser473. The phosphorylation of both residues was prevented by inhibitors of PI3-kinase. It is shown that phosphorylation of Thr308 and Ser473 act synergistically to activate PKB. This paper establishes that PKB is activated by upstream protein kinase(s) and provided the framework for the discovery of PDK1.
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Alessi DR, Andjelkovic M, Caudwell FB, Cron P, Morrice N, Cohen P, Hemmings B. Mechanism of activation of protein kinase B by insulin and IGF1. of special interest EMBO J. 15:1996;6541-6551 This paper demonstrates that insulin or IGF1 stimulation of cells leads to the phosphorylation of PKBα at two residues namely Thr308 and Ser473. The phosphorylation of both residues was prevented by inhibitors of PI3-kinase. It is shown that phosphorylation of Thr308 and Ser473 act synergistically to activate PKB. This paper establishes that PKB is activated by upstream protein kinase(s) and provided the framework for the discovery of PDK1.
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(1996)
EMBO J
, vol.15
, pp. 6541-6551
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Alessi, D.R.1
Andjelkovic, M.2
Caudwell, F.B.3
Cron, P.4
Morrice, N.5
Cohen, P.6
Hemmings, B.7
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21
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0029810181
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Akt, a pleckstrin homology domain-containing kinase, is activated primarily by phosphorylation
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Kohn AD, Takeuchi F, Roth RA. Akt, a pleckstrin homology domain-containing kinase, is activated primarily by phosphorylation. J Biol Chem. 271:1996;21920-21926.
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(1996)
J Biol Chem
, vol.271
, pp. 21920-21926
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Kohn, A.D.1
Takeuchi, F.2
Roth, R.A.3
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22
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15644381754
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Role of translocation in the activation and function of protein kinase B
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of special interest. This paper demonstrates that the recruitment of PKB to the plasma membrane following insulin/IGF1 stimulation of cells most likely plays a key role in enabling it to become phosphorylated by PDK1 and PDK2. It also reports that once activated. PKBα then translocates to the nucleus.
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Andjelkovic M, Alessi DR, Meier R, Fernandez A, Lamb NJC, Frech M, Cron P, Cohen P, Lucocq JM, Hemming BA. Role of translocation in the activation and function of protein kinase B. of special interest J Biol Chem. 272:1997;31324-31515 This paper demonstrates that the recruitment of PKB to the plasma membrane following insulin/IGF1 stimulation of cells most likely plays a key role in enabling it to become phosphorylated by PDK1 and PDK2. It also reports that once activated. PKBα then translocates to the nucleus.
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(1997)
J Biol Chem
, vol.272
, pp. 31324-31515
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Andjelkovic, M.1
Alessi, D.R.2
Meier, R.3
Fernandez, A.4
Lamb, N.J.C.5
Frech, M.6
Cron, P.7
Cohen, P.8
Lucocq, J.M.9
Hemming, B.A.10
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23
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0030727172
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Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ
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Meier R, Alessi D, Cron P, Hemmings BA. Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ J Biol Chem. 272:1997;30491-30497.
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(1997)
J Biol Chem
, vol.272
, pp. 30491-30497
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Meier, R.1
Alessi, D.2
Cron, P.3
Hemmings, B.A.4
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24
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12644301164
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3-phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase
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of outstanding interest. This paper describes the cloning and characterisation of PDK1 as a novel PH-containing protein kinase that belongs to the same subfamily of kinase as PKB. It is established that the interaction of Ptdlns(3,4,5)P3 with the PH domain of PKBα is critical in enabling PDK1 to phosphorylate and activate PKBα. A Drosophila homologue of PDK1 is also shown to phosphorylate PKBα on Thr308 in a Ptdlns(3,4,5)P3 or Ptdlns(3,4)P2 dependent manner.
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Alessi DR, Deak M, Casamayor A, Caudwell FB, Morrice N, Norman DG, Gaffney P, Reese CB, MacDougall CN, Harbison D, et al. 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. of outstanding interest Curr Biol. 7:1997;776-789 This paper describes the cloning and characterisation of PDK1 as a novel PH-containing protein kinase that belongs to the same subfamily of kinase as PKB. It is established that the interaction of Ptdlns(3,4,5)P3 with the PH domain of PKBα is critical in enabling PDK1 to phosphorylate and activate PKBα. A Drosophila homologue of PDK1 is also shown to phosphorylate PKBα on Thr308 in a Ptdlns(3,4,5)P3 or Ptdlns(3,4)P2 dependent manner.
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(1997)
Curr Biol
, vol.7
, pp. 776-789
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Alessi, D.R.1
Deak, M.2
Casamayor, A.3
Caudwell, F.B.4
Morrice, N.5
Norman, D.G.6
Gaffney, P.7
Reese, C.B.8
MacDougall, C.N.9
Harbison, D.10
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25
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0030890933
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Transduction of interleukin-2 anti-apoptotic and proliferative signals via Akt protein kinase
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Ahmed NN, Grimes HL, Bellacosa A, Chan TO, Tsichlis PN. Transduction of interleukin-2 anti-apoptotic and proliferative signals via Akt protein kinase. Proc Natl Acad Sci USA. 94:1997;3627-3632.
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Proc Natl Acad Sci USA
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Ahmed, N.N.1
Grimes, H.L.2
Bellacosa, A.3
Chan, T.O.4
Tsichlis, P.N.5
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26
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0030820857
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Regulation of protein kinase B in rat adipocytes by insulin, vanadate, and peroxovanadate - Membrane translocation in response to peroxovanadate
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Wijkander J, Holst LS, Rahn T, Resjo S, Castan I, Manganiello V, Belfrage P, Degerman E. Regulation of protein kinase B in rat adipocytes by insulin, vanadate, and peroxovanadate - membrane translocation in response to peroxovanadate. J Biol Chem. 272:1997;21520-21526.
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J Biol Chem
, vol.272
, pp. 21520-21526
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Wijkander, J.1
Holst, L.S.2
Rahn, T.3
Resjo, S.4
Castan, I.5
Manganiello, V.6
Belfrage, P.7
Degerman, E.8
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27
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0028811653
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Protein-kinase-C structure, function and regulation
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Newton AC. Protein-kinase-C structure, function and regulation. J Biol Chem. 270:1995;28495-28498.
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J Biol Chem
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Newton, A.C.1
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28
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0029789678
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The P160 RHOA-binding kinase ROK-α is a member of a kinase family and is involved in the reorganization of the cytoskeleton
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Leung T, Chen XQ, Manser E, Lim L. The P160 RHOA-binding kinase ROK-α is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol Cell Biol. 16:1996;5313-5327.
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Leung, T.1
Chen, X.Q.2
Manser, E.3
Lim, L.4
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The modular phosphorylation and activation of p70(S6K)
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Pullen N, Thomas G. The modular phosphorylation and activation of p70(S6K). FEBS Lett. 410:1997;78-82.
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Pullen, N.1
Thomas, G.2
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Requirement for Ras in Raf activation is overcome by targeting RAF to the plasma-membrane
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Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting RAF to the plasma-membrane. Nature. 369:1994;411-414.
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31
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0032518467
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3-phosphoinositide dependent protein kinase 1 (PDK1) phosphorylates and activates the p70S6 kinase in vivo and in vitro
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of outstanding interest. This paper demonstrates that PDK1 phosphorylates p70S6K at Thr252 in the T-loop of the kinase domain, leading to partial activation of this kinase. The phosphorylation of p70S6K by PDK1 is not dependent on Ptdlns(3,4,5)P3, and was greatly enhanced if Thr412 is mutated to Glu to mimic phosphorylation, and if the carboxy-terminal 104 residues are removed. This study establishes that the mechanism of p70S6K activation is analogous to that of PKB in that the phosphorylation of Thr252 and Thr412 - which lie in positions and sequences equivalent to Ser473 of PKB - act synergistically to activate the p70S6K.
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Alessi DR, Kozlowski MT, Weng QP, Morrice N, Avruch J. 3-phosphoinositide dependent protein kinase 1 (PDK1) phosphorylates and activates the p70S6 kinase in vivo and in vitro. of outstanding interest Curr Biol. 8:1998;69-81 This paper demonstrates that PDK1 phosphorylates p70S6K at Thr252 in the T-loop of the kinase domain, leading to partial activation of this kinase. The phosphorylation of p70S6K by PDK1 is not dependent on Ptdlns(3,4,5)P3, and was greatly enhanced if Thr412 is mutated to Glu to mimic phosphorylation, and if the carboxy-terminal 104 residues are removed. This study establishes that the mechanism of p70S6K activation is analogous to that of PKB in that the phosphorylation of Thr252 and Thr412 - which lie in positions and sequences equivalent to Ser473 of PKB - act synergistically to activate the p70S6K.
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Curr Biol
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Alessi, D.R.1
Kozlowski, M.T.2
Weng, Q.P.3
Morrice, N.4
Avruch, J.5
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32
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Molecular basis for the substrate specificity of protein kinase B; Comparison with MAPKAP kinase-1 and p70S6 kinase
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Alessi DR, Caudwell FB, Andjelkovic M, Hemmings BA, Cohen P. Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70S6 kinase. FEBS Lett. 399:1996;333-338.
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FEBS Lett
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Alessi, D.R.1
Caudwell, F.B.2
Andjelkovic, M.3
Hemmings, B.A.4
Cohen, P.5
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33
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Rapamycin-FKBP specifically blocks growth-dependent activation of and signalling by the 70 KD S6 protein-kinases
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Chung, J.1
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PD-098059 is a specific inhibitor of the activation of mitogen-activated protein-kinase in vitro and in vivo
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Alessi DR, Cuenda A, Cohen P, Dudley DT, Saltiel AR. PD-098059 is a specific inhibitor of the activation of mitogen-activated protein-kinase in vitro and in vivo. J Biol Chem. 270:1995;27489-27494.
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Alessi, D.R.1
Cuenda, A.2
Cohen, P.3
Dudley, D.T.4
Saltiel, A.R.5
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35
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Inhibition of glycogen-synthase kinase-3 by insulin is mediated by protein-kinase B
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Cross DAE, Alessi DR, Cohen P, Andjelkovic M, Hemmings BA. Inhibition of glycogen-synthase kinase-3 by insulin is mediated by protein-kinase B. Nature. 378:1995;785-789.
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Cross, D.A.E.1
Alessi, D.R.2
Cohen, P.3
Andjelkovic, M.4
Hemmings, B.A.5
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36
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0030712317
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Further evidence that the inhibition of glycogen synthase kinase-3β by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216
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Shaw M, Cohen P, Alessi DR. Further evidence that the inhibition of glycogen synthase kinase-3β by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216. FEBS Lett. 416:1997;307-311.
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FEBS Lett
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Shaw, M.1
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Cohen P, Alessi DR, Cross DAE. PDK1, the missing link in insulin signal transduction? FEBS Lett. 410:1997;3-10.
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Regulation of eukaryotic initiation factor eIF 2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
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Welsh GI, Miller CM, Loughlin AJ, Price NT, Proud CG. Regulation of eukaryotic initiation factor eIF 2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett. 421:1998;125-130.
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Welsh, G.I.1
Miller, C.M.2
Loughlin, A.J.3
Price, N.T.4
Proud, C.G.5
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39
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0030748651
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Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase-B and other protein kinases of the insulin signalling cascades
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of special interest. This paper reports that PKB phosphorylates and activates the cardiac-specific isoform of 6-phosphofructo-2-kinase and, after GSK3, was the second putative in vivo substrate for PKB. This paper establishes the mechanism by which insulin stimulates the phosphorylation and activation of phosphofructo-2-kinase in cardiac muscle which leads to the activation of glycolysis in this tissue. It was previously known that this signalling pathway required PI3-kinase.
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Deprez J, Vertommen D, Alessi DR, Hue L, Rider MH. Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase-B and other protein kinases of the insulin signalling cascades. of special interest J Biol Chem. 272:1997;17269-17275 This paper reports that PKB phosphorylates and activates the cardiac-specific isoform of 6-phosphofructo-2-kinase and, after GSK3, was the second putative in vivo substrate for PKB. This paper establishes the mechanism by which insulin stimulates the phosphorylation and activation of phosphofructo-2-kinase in cardiac muscle which leads to the activation of glycolysis in this tissue. It was previously known that this signalling pathway required PI3-kinase.
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(1997)
J Biol Chem
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Deprez, J.1
Vertommen, D.2
Alessi, D.R.3
Hue, L.4
Rider, M.H.5
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40
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0029908016
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Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose-uptake and glucose-transporter-4 tanslocation
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Kohn AD, Summers SA, Birnbaum MJ, Roth RA. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose-uptake and glucose-transporter-4 tanslocation. J Biol Chem. 271:1996;31372-31378.
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Kohn, A.D.1
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Birnbaum, M.J.3
Roth, R.A.4
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41
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0344265910
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Protein kinase B mediates the insulin induced increase in glucose and amino acid uptake in L6 myotubes
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in press
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Hajduch E, Alessi DR, Hemmings BA, Hundal H. Protein kinase B mediates the insulin induced increase in glucose and amino acid uptake in L6 myotubes. Diabetes. 1998;. in press.
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Hajduch, E.1
Alessi, D.R.2
Hemmings, B.A.3
Hundal, H.4
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42
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0030738261
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A constitutively active version of the Ser/Thr kinase Akt induces production of the ob gene product, leptin, in 3T3-L1 adipocytes
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Barthel A, Kohn AD, Luo YN, Roth RA. A constitutively active version of the Ser/Thr kinase Akt induces production of the ob gene product, leptin, in 3T3-L1 adipocytes. Endocrinol. 183:1997;3559-3562.
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Barthel, A.1
Kohn, A.D.2
Luo, Y.N.3
Roth, R.A.4
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43
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0001457668
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Amplification of Akt2 in human pancreatic-cancer cells and inhibition of Akt2 expression and tumorigenicity by antisense RNA
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Cheng JQ, Ruggeri B Klein WM, Sonoda G, Altomare DA, Watson DK, Testa JR. Amplification of Akt2 in human pancreatic-cancer cells and inhibition of Akt2 expression and tumorigenicity by antisense RNA. Proc Natl Acad Sci USA. 93:1996;3636-3641.
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Cheng, J.Q.1
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Klein, W.M.3
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Altomare, D.A.5
Watson, D.K.6
Testa, J.R.7
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44
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0029127042
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Molecular alterations of the Akt2 oncogene in ovarian and breast carcinomas
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Bellacosa A, Defeo D, Godwin AK, Bell DW, Cheng JQ, Altomare DA, Wan MH, Dubeau L, Scambia G, Masciullo V. Molecular alterations of the Akt2 oncogene in ovarian and breast carcinomas. Intl J Cancer. 64:1995;280-285.
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Bellacosa, A.1
Defeo, D.2
Godwin, A.K.3
Bell, D.W.4
Cheng, J.Q.5
Altomare, D.A.6
Wan, M.H.7
Dubeau, L.8
Scambia, G.9
Masciullo, V.10
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45
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0031034574
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Anti-apoptotic signalling by the insulin-like growth factor receptor, phosphatidylinositol 3-kinase and Akt
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of special interest. This paper establishes that IGF1 protects fibroblasts from apoptosis induced by UV-B light through a PI3-kinase-dependent pathway. Overexpression of a constitutively active form of PKBα in these cells is sufficient to protect against apoptosis but a catalytically deficient PKBα does not.
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Kulik G, Klippel A, Weber MJ. Anti-apoptotic signalling by the insulin-like growth factor receptor, phosphatidylinositol 3-kinase and Akt. of special interest Mol Cell Biol. 17:1997;1595-1606 This paper establishes that IGF1 protects fibroblasts from apoptosis induced by UV-B light through a PI3-kinase-dependent pathway. Overexpression of a constitutively active form of PKBα in these cells is sufficient to protect against apoptosis but a catalytically deficient PKBα does not.
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Mol Cell Biol
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Kulik, G.1
Klippel, A.2
Weber, M.J.3
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46
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0031053586
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Regulation of neuronal survival by the Serine-Threonine protein kinase Akt
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of special interest. This paper describes a PI3-kinase-dependent signalling pathway by which IGF-1 promotes the survival of cerebellar neurons. Overexpression of PKB promoted growth factor-induces neuronal survival whereas overexpression of a dominant negative form of PKB induces apoptosis.
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Dudek H, Datta SR, Franke TF, Birnbarun MJ, Yao R, Cooper GM, Segal RA, Kaplan DR, Greenberg ME. Regulation of neuronal survival by the Serine-Threonine protein kinase Akt. of special interest Science. 275:1997;661-665 This paper describes a PI3-kinase-dependent signalling pathway by which IGF-1 promotes the survival of cerebellar neurons. Overexpression of PKB promoted growth factor-induces neuronal survival whereas overexpression of a dominant negative form of PKB induces apoptosis.
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(1997)
Science
, vol.275
, pp. 661-665
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Dudek, H.1
Datta, S.R.2
Franke, T.F.3
Birnbarun, M.J.4
Yao, R.5
Cooper, G.M.6
Segal, R.A.7
Kaplan, D.R.8
Greenberg, M.E.9
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47
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0031028730
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Suppression of c-Myc-Induced apoptosis by Ras signalling through PI(3)K and PKB
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of special interest. The role of PI3-kinase, Ras, and PKB in the modulation of apoptosis induced in fibroblasts by the oncoprotein c-Myc is investigated. Ras activation of PI3-kinase suppresses c-Myc-induced apoptosis through the activation of PKB but not the p70S6K. Ras is also found to be an effective promoter of apoptosis, through the Raf/MAP kinase pathway.
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Kauffmann Z, Rodriguez-Viciana P, Ulrich E, Gilbert C, Coffer P, Downward J, Evan G. Suppression of c-Myc-Induced apoptosis by Ras signalling through PI(3)K and PKB. of special interest Nature. 385:1997;544-548 The role of PI3-kinase, Ras, and PKB in the modulation of apoptosis induced in fibroblasts by the oncoprotein c-Myc is investigated. Ras activation of PI3-kinase suppresses c-Myc-induced apoptosis through the activation of PKB but not the p70S6K. Ras is also found to be an effective promoter of apoptosis, through the Raf/MAP kinase pathway.
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(1997)
Nature
, vol.385
, pp. 544-548
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Kauffmann, Z.1
Rodriguez-Viciana, P.2
Ulrich, E.3
Gilbert, C.4
Coffer, P.5
Downward, J.6
Evan, G.7
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48
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0030913673
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Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
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of special interest. Upon detachment of cells from the extracellular matrix, epithelial cells undergo apoptosis, a phenomenon known as anoikis. This ensures that cells are unable to survive in an inappropriate location. The PI3-kinase/PKB pathway is shown to protect cells attached to a matrix from apoptosis. Upon detachment of epithelial cells from the extracellular matrix, PI3-kinase and PKB are inactivated and cells undergo apoptosis. In Ras-transformed cells, PI3-kinase and PKB remain active after detachment of cells from their matrix and thus survive in an aberrant location.
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Khwaja A, Rodriguez-Viciana P, Wennstrom S, Warne PH, Downward J. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. of special interest EMBO J. 16:1997;2783-2793 Upon detachment of cells from the extracellular matrix, epithelial cells undergo apoptosis, a phenomenon known as anoikis. This ensures that cells are unable to survive in an inappropriate location. The PI3-kinase/PKB pathway is shown to protect cells attached to a matrix from apoptosis. Upon detachment of epithelial cells from the extracellular matrix, PI3-kinase and PKB are inactivated and cells undergo apoptosis. In Ras-transformed cells, PI3-kinase and PKB remain active after detachment of cells from their matrix and thus survive in an aberrant location.
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(1997)
EMBO J
, vol.16
, pp. 2783-2793
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Khwaja, A.1
Rodriguez-Viciana, P.2
Wennstrom, S.3
Warne, P.H.4
Downward, J.5
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49
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0000440912
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Transformation of chicken cells by the gene encoding the catalytic subunit of PI3-kinase
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Chang HW, Aoki M, Fruman D, Auger KR, Bellacosa A, Tsichlis PN, Cantley LC, Roberts TM, Vogt PK. Transformation of chicken cells by the gene encoding the catalytic subunit of PI3-kinase. Science. 276:1997;1848-1850.
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Science
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Chang, H.W.1
Aoki, M.2
Fruman, D.3
Auger, K.R.4
Bellacosa, A.5
Tsichlis, P.N.6
Cantley, L.C.7
Roberts, T.M.8
Vogt, P.K.9
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50
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0030702123
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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
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of outstanding interest. This paper provides the first evidence for a mechanism by which PKB functions to protect cells from apoptosis. The authors demonstrate that growth factor activation of the PI3-kinase/PKB-signaling pathway culminates in the phosphorylation of the BAD protein at Ser136, thereby suppressing apoptosis and promoting cell survival
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Datta SR, Dudek H, Tao X, Masters S, Fu HA, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. of outstanding interest Cell. 91:1997;231-241 This paper provides the first evidence for a mechanism by which PKB functions to protect cells from apoptosis. The authors demonstrate that growth factor activation of the PI3-kinase/PKB-signaling pathway culminates in the phosphorylation of the BAD protein at Ser136, thereby suppressing apoptosis and promoting cell survival.
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Cell
, vol.91
, pp. 231-241
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Datta, S.R.1
Dudek, H.2
Tao, X.3
Masters, S.4
Fu, H.A.5
Gotoh, Y.6
Greenberg, M.E.7
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51
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Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
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DelPeso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science. 278:1997;687-689.
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Science
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Delpeso, L.1
Gonzalez-Garcia, M.2
Page, C.3
Herrera, R.4
Nunez, G.5
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52
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0030584088
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Serine phosphorylation of death agonist bad in response to survival factor results in binding to 14-3-3 not BCL-X(L)
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XL which induces of apoptosis in the absence of interleukin-2.
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XL which induces of apoptosis in the absence of interleukin-2.
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Zha, J.P.1
Harada, H.2
Yang, E.3
Jockel, J.4
Korsmeyer, S.J.5
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53
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0031952597
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Identification of the regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1α/p90Rsk that are inducible by MAPK
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Dalby KN, Morrice N, Caudwell FB, Avruch J, Cohen P. Identification of the regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1α/p90Rsk that are inducible by MAPK. J Biol Chem. 273:1998;1496-1505.
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J Biol Chem
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Dalby, K.N.1
Morrice, N.2
Caudwell, F.B.3
Avruch, J.4
Cohen, P.5
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54
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0032578999
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Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-triphosphate-dependent activation of protein kinase B
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Stephens L, Anderson K, Stokoe D, Erdjument H, Painter G, Holmes AB, Gaffney PRJ, Reese CB, McCormick F, et al. Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-triphosphate-dependent activation of protein kinase B. Science. 279:1998;710-714.
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Science
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Stephens, L.1
Anderson, K.2
Stokoe, D.3
Erdjument, H.4
Painter, G.5
Holmes, A.B.6
Gaffney, P.R.J.7
Reese, C.B.8
McCormick, F.9
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55
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Phosphorylation and activation of P70S6K by PDK1
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Pullen N, Dennis PB, Andjelkovic M, Dufner A, Kozma SC, Hemmings BA, Thomas G. Phosphorylation and activation of P70S6K by PDK1. Science. 279:1998;707-710.
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Science
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Pullen, N.1
Dennis, P.B.2
Andjelkovic, M.3
Dufner, A.4
Kozma, S.C.5
Hemmings, B.A.6
Thomas, G.7
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