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Volumn 192, Issue , 2003, Pages 7-20

The PI-3 kinase/Akt pathway and T cell activation: Pleiotropic pathways downstream of PIP3

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PROTEIN KINASE B; T LYMPHOCYTE RECEPTOR;

EID: 0038578823     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2003.00008.x     Document Type: Review
Times cited : (223)

References (139)
  • 2
    • 0032881288 scopus 로고    scopus 로고
    • Akt/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan TO, Rittenhouse SE, Tsichlis PN. Akt/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu Rev Biochem 1999;68:965-1014.
    • (1999) Annu Rev Biochem , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 3
    • 0036199607 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in immunological systems
    • Fruman DA, Cantley LC. Phosphoinositide 3-kinase in immunological systems. Semin Immunol 2002;14:7-18.
    • (2002) Semin Immunol , vol.14 , pp. 7-18
    • Fruman, D.A.1    Cantley, L.C.2
  • 4
    • 0026502874 scopus 로고
    • Regulation of D3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigen receptor
    • Ward SG, Ley SC, MacPhee C, Cantrell D. Regulation of D3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigen receptor. Eur J Immunol 1992;22:45-49.
    • (1992) Eur J Immunol , vol.22 , pp. 45-49
    • Ward, S.G.1    Ley, S.C.2    MacPhee, C.3    Cantrell, D.4
  • 5
    • 0028304998 scopus 로고
    • Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation
    • Exley M, Varticovski L, Peter M, Sancho J, Terhorst C. Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation. J Biol Chem 1994;269:15140-15146.
    • (1994) J Biol Chem , vol.269 , pp. 15140-15146
    • Exley, M.1    Varticovski, L.2    Peter, M.3    Sancho, J.4    Terhorst, C.5
  • 6
    • 0030820813 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells
    • de Aos I, et al. Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells. J Biol Chem 1997;272:25310-25318.
    • (1997) J Biol Chem , vol.272 , pp. 25310-25318
    • De Aos, I.1
  • 7
    • 0029938675 scopus 로고    scopus 로고
    • The protein interactions of the immunoglobulin receptor family tyrosine-based activation motifs present in the T cell receptor zeta subunits and the CD3 gamma, delta and epsilon chains
    • Osman N, Turner H, Lucas S, Reif K, Cantrell DA. The protein interactions of the immunoglobulin receptor family tyrosine-based activation motifs present in the T cell receptor zeta subunits and the CD3 gamma, delta and epsilon chains. Eur J Immunol 1996;26:1063-1068.
    • (1996) Eur J Immunol , vol.26 , pp. 1063-1068
    • Osman, N.1    Turner, H.2    Lucas, S.3    Reif, K.4    Cantrell, D.A.5
  • 8
    • 0029081182 scopus 로고
    • T cell activation-dependent association between the p85 subunit of the phosphatidylinositol 3-kinase and Grb2/phospholipase C-gamma 1-binding phosphotyrosyl protein pp36/38
    • Fukazawa T, et al. T cell activation-dependent association between the p85 subunit of the phosphatidylinositol 3-kinase and Grb2/phospholipase C-gamma 1-binding phosphotyrosyl protein pp36/38. J Biol Chem 1995;270:20177-20182.
    • (1995) J Biol Chem , vol.270 , pp. 20177-20182
    • Fukazawa, T.1
  • 9
    • 0032479864 scopus 로고    scopus 로고
    • T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane
    • Bruyns E, et al. T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane. J Exp Med 1998;188:561-575.
    • (1998) J Exp Med , vol.188 , pp. 561-575
    • Bruyns, E.1
  • 10
    • 0033826512 scopus 로고    scopus 로고
    • New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway
    • Gu H, et al. New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway. Mol Cell Biol 2000;20:7109-7120.
    • (2000) Mol Cell Biol , vol.20 , pp. 7109-7120
    • Gu, H.1
  • 11
    • 0033912699 scopus 로고    scopus 로고
    • The T-cell receptor regulates Akt (protein kinase B) via a pathway involving Rac1 and phosphatidylinositide 3-kinase
    • Genot EM, Arrieumerlou C, Ku G, Burgering BM, Weiss A, Kramer IM. The T-cell receptor regulates Akt (protein kinase B) via a pathway involving Rac1 and phosphatidylinositide 3-kinase. Mol Cell Biol 2000;20:5469-5478.
    • (2000) Mol Cell Biol , vol.20 , pp. 5469-5478
    • Genot, E.M.1    Arrieumerlou, C.2    Ku, G.3    Burgering, B.M.4    Weiss, A.5    Kramer, I.M.6
  • 12
    • 0027436140 scopus 로고
    • Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: The p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase
    • Prasad KV, et al. Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase. Mol Cell Biol 1993;13:7708-7717.
    • (1993) Mol Cell Biol , vol.13 , pp. 7708-7717
    • Prasad, K.V.1
  • 13
    • 0031148668 scopus 로고    scopus 로고
    • A negative role for phosphoinositide 3-kinase in T-cell antigen receptor function
    • Reif K, Lucas S, Cantrell D. A negative role for phosphoinositide 3-kinase in T-cell antigen receptor function. Curr Biol 1997;7:285-293.
    • (1997) Curr Biol , vol.7 , pp. 285-293
    • Reif, K.1    Lucas, S.2    Cantrell, D.3
  • 14
    • 0027980250 scopus 로고
    • T cell receptor-associated alpha-phosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56lck
    • Carrera AC, Rodriguez-Borlado L, Martinez-Alonso C, Merida I. T cell receptor-associated alpha-phosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56lck. J Biol Chem 1994;269:19435-19440.
    • (1994) J Biol Chem , vol.269 , pp. 19435-19440
    • Carrera, A.C.1    Rodriguez-Borlado, L.2    Martinez-Alonso, C.3    Merida, I.4
  • 15
    • 0033817762 scopus 로고    scopus 로고
    • Targets of B-cell antigen receptor signaling: The phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase-3 signaling pathway and the Rap1 GTPase
    • Gold MR, et al. Targets of B-cell antigen receptor signaling: the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase-3 signaling pathway and the Rap1 GTPase. Immunol Rev 2000;176:47-68.
    • (2000) Immunol Rev , vol.176 , pp. 47-68
    • Gold, M.R.1
  • 16
    • 20244366689 scopus 로고    scopus 로고
    • Requirement of Gab2 for mast cell development and KitL/c-Kit signaling
    • Nishida K, et al. Requirement of Gab2 for mast cell development and KitL/c-Kit signaling. Blood 2002;99:1866-1869.
    • (2002) Blood , vol.99 , pp. 1866-1869
    • Nishida, K.1
  • 17
    • 0033559311 scopus 로고    scopus 로고
    • Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors
    • Nishida K, et al. Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors. Blood 1999;93:1809-1816.
    • (1999) Blood , vol.93 , pp. 1809-1816
    • Nishida, K.1
  • 18
    • 0033672473 scopus 로고    scopus 로고
    • Lymphocytes with a complex: Adapter proteins in antigen receptor signaling
    • Tomlinson MG, Lin J, Weiss A. Lymphocytes with a complex: adapter proteins in antigen receptor signaling. Immunol Today 2000;21:584-591.
    • (2000) Immunol Today , vol.21 , pp. 584-591
    • Tomlinson, M.G.1    Lin, J.2    Weiss, A.3
  • 19
    • 0035849822 scopus 로고    scopus 로고
    • Essential role for Gab2 in the allergic response
    • Gu H, et al. Essential role for Gab2 in the allergic response. Nature 2001;412:186-190.
    • (2001) Nature , vol.412 , pp. 186-190
    • Gu, H.1
  • 20
    • 0034667783 scopus 로고    scopus 로고
    • Cutting edge: Gab2 mediates an inhibitory phosphatidylinositol 3′-kinase pathway in T cell antigen receptor signaling
    • Pratt JC, et al. Cutting edge: gab2 mediates an inhibitory phosphatidylinositol 3′-kinase pathway in T cell antigen receptor signaling. J Immunol 2000;165:4158-4163.
    • (2000) J Immunol , vol.165 , pp. 4158-4163
    • Pratt, J.C.1
  • 21
    • 0035059417 scopus 로고    scopus 로고
    • Complexities of CD28/BY: CTLA-4- costimulatory pathways in autoimmunity and transplantation
    • Salomon B, Bluestone JA. Complexities of CD28/BY: CTLA-4- costimulatory pathways in autoimmunity and transplantation. Annu Rev Immunol 2001;19:225-252.
    • (2001) Annu Rev Immunol , vol.19 , pp. 225-252
    • Salomon, B.1    Bluestone, J.A.2
  • 23
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif
    • Prasad KV, et al. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif. Proc Natl Acad Sci USA 1994;91:2834-2838.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2834-2838
    • Prasad, K.V.1
  • 24
    • 0028211126 scopus 로고
    • The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidyl-inositol 3′-kinase
    • Stein PH, Fraser JD, Weiss A. The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidyl-inositol 3′-kinase. Mol Cell Biol 1994;14:3392-3402.
    • (1994) Mol Cell Biol , vol.14 , pp. 3392-3402
    • Stein, P.H.1    Fraser, J.D.2    Weiss, A.3
  • 25
    • 0028118512 scopus 로고
    • Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells
    • Truitt KE, Hicks CM, Imboden JB. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells. J Exp Med 1994;179:1071-1076.
    • (1994) J Exp Med , vol.179 , pp. 1071-1076
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 26
    • 0028981212 scopus 로고
    • p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: Implications for T-cell costimulation
    • Raab M, Cai YC, Bunnell SC, Heyeck SD, Berg LJ, Rudd CE. p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: implications for T-cell costimulation. Proc Natl Acad Sci USA 1995;92:8891-8895.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8891-8895
    • Raab, M.1    Cai, Y.C.2    Bunnell, S.C.3    Heyeck, S.D.4    Berg, L.J.5    Rudd, C.E.6
  • 27
    • 0029885108 scopus 로고    scopus 로고
    • Structural requirements for CD28-mediated costimulation of IL-2 production in Jurkat T cells
    • Truitt KE, Nagel T, Suen LF, Imboden JB. Structural requirements for CD28-mediated costimulation of IL-2 production in Jurkat T cells. J Immunol 1996;156:4539-4541.
    • (1996) J Immunol , vol.156 , pp. 4539-4541
    • Truitt, K.E.1    Nagel, T.2    Suen, L.F.3    Imboden, J.B.4
  • 28
    • 0029814079 scopus 로고    scopus 로고
    • CD28: A signaling perspective
    • Ward SG. CD28: a signaling perspective. Biochem J 1996;318:361-377.
    • (1996) Biochem J , vol.318 , pp. 361-377
    • Ward, S.G.1
  • 29
    • 0029965232 scopus 로고    scopus 로고
    • PI 3-kinase: A pivotal pathway in T-cell activation?
    • Ward SG, June CH, Olive D. PI 3-kinase: a pivotal pathway in T-cell activation? Immunol Today 1996;17:187-197.
    • (1996) Immunol Today , vol.17 , pp. 187-197
    • Ward, S.G.1    June, C.H.2    Olive, D.3
  • 30
    • 0035367805 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in T lymphocyte activation
    • Ward SG, Cantrell DA. Phosphoinositide 3-kinases in T lymphocyte activation. Curr Opin Immunol 2001;13:332-338.
    • (2001) Curr Opin Immunol , vol.13 , pp. 332-338
    • Ward, S.G.1    Cantrell, D.A.2
  • 31
    • 0033662376 scopus 로고    scopus 로고
    • The CD28 and CTLA-4 receptors associate with the serine/threonine phosphatase PP2A
    • Chuang E, et al. The CD28 and CTLA-4 receptors associate with the serine/threonine phosphatase PP2A. Immunity 2000;13:313-322.
    • (2000) Immunity , vol.13 , pp. 313-322
    • Chuang, E.1
  • 33
    • 0028802706 scopus 로고
    • Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation
    • Cai YC, Cefai D, Schneider H, Raab M, Nabavi N, Rudd CE. Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation. Immunity 1995;3:417-426.
    • (1995) Immunity , vol.3 , pp. 417-426
    • Cai, Y.C.1    Cefai, D.2    Schneider, H.3    Raab, M.4    Nabavi, N.5    Rudd, C.E.6
  • 34
    • 0033212986 scopus 로고    scopus 로고
    • Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition
    • Poy F, et al. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol Cell 1999;4:555-561.
    • (1999) Mol Cell , vol.4 , pp. 555-561
    • Poy, F.1
  • 35
    • 0028972712 scopus 로고
    • CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation
    • Crooks ME, Littman DR, Carter KH, Fearon DT, Weiss A, Stein PH. CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation. Mol Cell Biol 1995;15:6820-6828.
    • (1995) Mol Cell Biol , vol.15 , pp. 6820-6828
    • Crooks, M.E.1    Littman, D.R.2    Carter, K.H.3    Fearon, D.T.4    Weiss, A.5    Stein, P.H.6
  • 36
    • 0033811659 scopus 로고    scopus 로고
    • Deficiency of PTEN in Jurkat T cells causes constitutive localization of itk to the plasma membrane and hyperresponsiveness to CD3 stimulation
    • Shan X, et al. Deficiency of PTEN in Jurkat T cells causes constitutive localization of itk to the plasma membrane and hyperresponsiveness to CD3 stimulation. Mol Cell Biol 2000;20:6945-6957.
    • (2000) Mol Cell Biol , vol.20 , pp. 6945-6957
    • Shan, X.1
  • 37
    • 0035451761 scopus 로고    scopus 로고
    • PI 3-K and T-cell activation: Limitations of T-leukemic cell lines as signaling models
    • Astoul E, Cantrell DA, Edmunds C, Ward SG. PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models. Trends Immunol 2001;22:490-496.
    • (2001) Trends Immunol , vol.22 , pp. 490-496
    • Astoul, E.1    Cantrell, D.A.2    Edmunds, C.3    Ward, S.G.4
  • 38
    • 0033574429 scopus 로고    scopus 로고
    • Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110alpha subunit of phosphoinositide 3-kinase
    • Bi L, Okabe I, Bernard DJ, Wynshaw-Boris A, Nussbaum RL. Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110alpha subunit of phosphoinositide 3-kinase. J Biol Chem 1999;274:10963-10968.
    • (1999) J Biol Chem , vol.274 , pp. 10963-10968
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Wynshaw-Boris, A.4    Nussbaum, R.L.5
  • 39
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85 subunit of phosphoinositide 3-kinase
    • Suzuki H, et al. Xid-like immunodeficiency in mice with disruption of the p85 subunit of phosphoinositide 3-kinase. Science 1999;283:390-392.
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1
  • 40
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α
    • Fruman DA, et al. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85α. Science 1999;283:393-397.
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1
  • 41
    • 0036143774 scopus 로고    scopus 로고
    • Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival
    • Ueki K, Fruman DA, Brachmann SM, Tseng YH, Cantley LC, Kahn DR. Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival. Mol Cell Biol 2002;22:965-977.
    • (2002) Mol Cell Biol , vol.22 , pp. 965-977
    • Ueki, K.1    Fruman, D.A.2    Brachmann, S.M.3    Tseng, Y.H.4    Cantley, L.C.5    Kahn, D.R.6
  • 42
    • 0036142957 scopus 로고    scopus 로고
    • Reduced expression of the murine p85alpha subunit of phosphoinositide 3-kinase improves insulin signaling and ameliorates diabetes
    • Mauvais-Jarvis F, et al. Reduced expression of the murine p85alpha subunit of phosphoinositide 3-kinase improves insulin signaling and ameliorates diabetes. J Clin Invest 2002;109:141-149.
    • (2002) J Clin Invest , vol.109 , pp. 141-149
    • Mauvais-Jarvis, F.1
  • 43
    • 0034635264 scopus 로고    scopus 로고
    • Function of PI3Kgamma in thymocyte development, T cell activation, and neutrophil migration
    • Sasaki T, et al. Function of PI3Kgamma in thymocyte development, T cell activation, and neutrophil migration. Science 2000;287:1040-1046.
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1
  • 44
    • 0037047590 scopus 로고    scopus 로고
    • Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice
    • Okkenhaug K, et al. Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice. Science 2002;297:1031-1034.
    • (2002) Science , vol.297 , pp. 1031-1034
    • Okkenhaug, K.1
  • 45
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma
    • Lopez-Ilasaca M, Crespo P, Pellici PG, Gutkind JS, Wetzker R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma. Science 1997;275:394-397.
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 46
    • 0030920653 scopus 로고    scopus 로고
    • Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: Structure-activity analysis and interactions with wortmannin
    • Stoyanova S, et al. Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: structure-activity analysis and interactions with wortmannin. Biochem J 1997;324:489-495.
    • (1997) Biochem J , vol.324 , pp. 489-495
    • Stoyanova, S.1
  • 47
    • 0032478066 scopus 로고    scopus 로고
    • Aggregation of the human high affinity immunoglobulin G receptor (FcgammaRI) activates both tyrosine kinase and G protein-coupled phosphoinositide 3-kinase isoforms
    • Melendez AJ, Gillooly DJ, Harnett MM, Allen JM. Aggregation of the human high affinity immunoglobulin G receptor (FcgammaRI) activates both tyrosine kinase and G protein-coupled phosphoinositide 3-kinase isoforms. Proc Natl Acad Sci USA 1998;95:2169-2174.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2169-2174
    • Melendez, A.J.1    Gillooly, D.J.2    Harnett, M.M.3    Allen, J.M.4
  • 48
    • 0030612144 scopus 로고    scopus 로고
    • p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes
    • Chantry D, et al. p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem 1997;272:19236-19241.
    • (1997) J Biol Chem , vol.272 , pp. 19236-19241
    • Chantry, D.1
  • 49
    • 0030611198 scopus 로고    scopus 로고
    • P110delta, a novel phosphoinositide 3-kinase in leukocytes
    • Vanhaesebroeck B, et al. P110delta, a novel phosphoinositide 3-kinase in leukocytes. Proc Natl Acad Sci USA 1997;94:4330-4335.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4330-4335
    • Vanhaesebroeck, B.1
  • 50
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon MA, Ferguson KM. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem J 2000;350:1-18.
    • (2000) Biochem J , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 51
    • 0035850897 scopus 로고    scopus 로고
    • Specificity in pleckstrin homology (PH) domain membrane targeting: A role for a phosphoinositide-protein co-operative mechanism
    • Maffucci T, Falasca M. Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism. FEBS Lett 2001;506:173-179.
    • (2001) FEBS Lett , vol.506 , pp. 173-179
    • Maffucci, T.1    Falasca, M.2
  • 52
    • 0035473464 scopus 로고    scopus 로고
    • Vav proteins, adaptors and cell signaling
    • Bustelo XR. Vav proteins, adaptors and cell signaling. Oncogene 2001;20:6372-6381.
    • (2001) Oncogene , vol.20 , pp. 6372-6381
    • Bustelo, X.R.1
  • 53
    • 0031896945 scopus 로고    scopus 로고
    • Two distinct regions of the CD28 intracytoplasmic domain are involved in the tyrosine phosphorylation of Vav and GTPase activating protein-associated p62 protein
    • Klasen S, Pages F, Peyron JF, Cantrell DA, Olive D. Two distinct regions of the CD28 intracytoplasmic domain are involved in the tyrosine phosphorylation of Vav and GTPase activating protein-associated p62 protein. Int Immunol 1998;10:481-489.
    • (1998) Int Immunol , vol.10 , pp. 481-489
    • Klasen, S.1    Pages, F.2    Peyron, J.F.3    Cantrell, D.A.4    Olive, D.5
  • 54
    • 0034642534 scopus 로고    scopus 로고
    • Cbl-b regulates the CD28 dependence of T-cell activation
    • Chiang YJ, et al. Cbl-b regulates the CD28 dependence of T-cell activation. Nature 2000;403:216-220.
    • (2000) Nature , vol.403 , pp. 216-220
    • Chiang, Y.J.1
  • 55
    • 0033680925 scopus 로고    scopus 로고
    • Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells
    • Krawczyk C, et al. Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells. Immunity 2000;13:463-473.
    • (2000) Immunity , vol.13 , pp. 463-473
    • Krawczyk, C.1
  • 56
    • 0034674627 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 transcription
    • Hehner SP, Hofmann TG, Dienz O, Droge W, Schmitz ML. Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 transcription. J Biol Chem 2000;275:18160-18171.
    • (2000) J Biol Chem , vol.275 , pp. 18160-18171
    • Hehner, S.P.1    Hofmann, T.G.2    Dienz, O.3    Droge, W.4    Schmitz, M.L.5
  • 57
    • 0033959896 scopus 로고    scopus 로고
    • A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling
    • Rodrigues GA, Falasca M, Zhang Z, Ong SH, Schlessinger J. A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol Cell Biol 2000;20:1448-1459.
    • (2000) Mol Cell Biol , vol.20 , pp. 1448-1459
    • Rodrigues, G.A.1    Falasca, M.2    Zhang, Z.3    Ong, S.H.4    Schlessinger, J.5
  • 58
    • 0030686560 scopus 로고    scopus 로고
    • Ligation of the T cell co-stimulatory receptor CD28 activates the serine-threonine protein kinase protein kinase B
    • Parry RV, Reif K, Smith G, Sansom DM, Hemmings BA, Ward SG. Ligation of the T cell co-stimulatory receptor CD28 activates the serine-threonine protein kinase protein kinase B. Eur J Immunol 1997;27:2495-2501.
    • (1997) Eur J Immunol , vol.27 , pp. 2495-2501
    • Parry, R.V.1    Reif, K.2    Smith, G.3    Sansom, D.M.4    Hemmings, B.A.5    Ward, S.G.6
  • 59
    • 0034550280 scopus 로고    scopus 로고
    • The T cell antigen receptor activates phosphatidylinositol 3-kinase-regulated serine kinases protein kinase B and ribosomal S6 kinase 1
    • Lafont V, Astoul E, Laurence A, Liautard J, Cantrell D. The T cell antigen receptor activates phosphatidylinositol 3-kinase-regulated serine kinases protein kinase B and ribosomal S6 kinase 1. FEBS Lett 2000;486:38-42.
    • (2000) FEBS Lett , vol.486 , pp. 38-42
    • Lafont, V.1    Astoul, E.2    Laurence, A.3    Liautard, J.4    Cantrell, D.5
  • 60
    • 0035221568 scopus 로고    scopus 로고
    • Akt provides the CD28 co-stimulatory signal for upregulation of IL-2 and IFN-? but not Th2 cytokines
    • Kane LP, Andres PG, Howland KB, Abbas AK, Weiss A. Akt provides the CD28 co-stimulatory signal for upregulation of IL-2 and IFN-? but not Th2 cytokines. Nat Immunol 2001;2:37-44.
    • (2001) Nat Immunol , vol.2 , pp. 37-44
    • Kane, L.P.1    Andres, P.G.2    Howland, K.B.3    Abbas, A.K.4    Weiss, A.5
  • 61
    • 0036069699 scopus 로고    scopus 로고
    • The CD28 signaling pathway regulates glucose metabolism
    • Frauwirth KA, et al. The CD28 signaling pathway regulates glucose metabolism. Immunity 2002;16:769-777.
    • (2002) Immunity , vol.16 , pp. 769-777
    • Frauwirth, K.A.1
  • 62
    • 0037087472 scopus 로고    scopus 로고
    • CD28 costimulation mediates down-regulation of p27kip 1 and cell cycle progression by activation of the PI3K/PKB signaling pathway in primary human T cells
    • Appleman LJ, van Puijenbroek AA, Shu KM, Nadler LM, Boussiotis VA. CD28 costimulation mediates down-regulation of p27kip 1 and cell cycle progression by activation of the PI3K/PKB signaling pathway in primary human T cells. J Immunol 2002;168:2729-2736.
    • (2002) J Immunol , vol.168 , pp. 2729-2736
    • Appleman, L.J.1    Van Puijenbroek, A.A.2    Shu, K.M.3    Nadler, L.M.4    Boussiotis, V.A.5
  • 63
    • 0035914388 scopus 로고    scopus 로고
    • Akt 1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice
    • Cho H, Thorvaldsen JL, Chu Q, Feng F, Birnbaum MJ. Akt 1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice. J Biol Chem 2001;276:38349-38352.
    • (2001) J Biol Chem , vol.276 , pp. 38349-38352
    • Cho, H.1    Thorvaldsen, J.L.2    Chu, Q.3    Feng, F.4    Birnbaum, M.J.5
  • 64
    • 0035448879 scopus 로고    scopus 로고
    • Growth retardation and increased apoptosis in mice with homozygous disruption of the akt1 gene
    • Chen WS, et al. Growth retardation and increased apoptosis in mice with homozygous disruption of the akt1 gene. Genes Dev 2001;15:2203-2208.
    • (2001) Genes Dev , vol.15 , pp. 2203-2208
    • Chen, W.S.1
  • 65
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta)
    • Cho H, et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science 2001;292:1728-1731.
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1
  • 66
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • Klippel A, Reinhard C, Kavanaugh WM, Apell G, Escobedo MA, Williams LT. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol Cell Biol 1996;16:4117-4127.
    • (1996) Mol Cell Biol , vol.16 , pp. 4117-4127
    • Klippel, A.1    Reinhard, C.2    Kavanaugh, W.M.3    Apell, G.4    Escobedo, M.A.5    Williams, L.T.6
  • 67
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 1997;15:707-747.
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 68
    • 0036604985 scopus 로고    scopus 로고
    • New insights into the regulation and functions of Tec family tyrosine kinases in the immune system
    • Miller AT, Berg LJ. New insights into the regulation and functions of Tec family tyrosine kinases in the immune system. Curr Opin Immunol 2002;14:331-340.
    • (2002) Curr Opin Immunol , vol.14 , pp. 331-340
    • Miller, A.T.1    Berg, L.J.2
  • 69
    • 0037080536 scopus 로고    scopus 로고
    • PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2
    • Lynch DK, Daly RJ. PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2. EMBO J 2002;21:72-82.
    • (2002) EMBO J , vol.21 , pp. 72-82
    • Lynch, D.K.1    Daly, R.J.2
  • 70
    • 0033104502 scopus 로고    scopus 로고
    • Autophosphorylation of p110delta phosphoinositide 3-kinase: A new paradigm for the regulation of lipid kinases in vitro and in vivo
    • Vanhaesebroeck B, et al. Autophosphorylation of p110delta phosphoinositide 3-kinase: a new paradigm for the regulation of lipid kinases in vitro and in vivo. EMBO J 1999;18:1292-1302.
    • (1999) EMBO J , vol.18 , pp. 1292-1302
    • Vanhaesebroeck, B.1
  • 72
  • 73
    • 0033517190 scopus 로고    scopus 로고
    • NF-κB is a target of AKT in anti-apoptotic PDGF signalling
    • Romashkova JA, Makarov SS. NF-κB is a target of AKT in anti-apoptotic PDGF signalling. Nature 1999;401:86-90.
    • (1999) Nature , vol.401 , pp. 86-90
    • Romashkova, J.A.1    Makarov, S.S.2
  • 74
    • 0037039665 scopus 로고    scopus 로고
    • Distinct roles of the Ikappa B kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-kappa B) from Ikappa B and in phosphorylating the p65 subunit of NF-kappa B
    • Sizemore N, Lerner N, Dombrowski N, Sakurai H, Stark GR. Distinct roles of the Ikappa B kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-kappa B) from Ikappa B and in phosphorylating the p65 subunit of NF-kappa B. J Biol Chem 2002;277:3863-3869.
    • (2002) J Biol Chem , vol.277 , pp. 3863-3869
    • Sizemore, N.1    Lerner, N.2    Dombrowski, N.3    Sakurai, H.4    Stark, G.R.5
  • 76
    • 0030882666 scopus 로고    scopus 로고
    • Oncogenic Ha-Ras-induced signaling activates NF-kappaB transcriptional activity, which is required for cellular transformation
    • Finco TS, Westwick JK, Norris JL, Der Beg AACJ, Baldwin AS Jr. Oncogenic Ha-Ras-induced signaling activates NF-kappaB transcriptional activity, which is required for cellular transformation. J Biol Chem 1997;272:24113-24116.
    • (1997) J Biol Chem , vol.272 , pp. 24113-24116
    • Finco, T.S.1    Westwick, J.K.2    Norris, J.L.3    Der Beg, A.A.C.J.4    Baldwin A.S., Jr.5
  • 77
    • 0034658320 scopus 로고    scopus 로고
    • Protein kinase B regulates T lymphocyte survival, nuclear factor kappaB activation, and Bcl-X(L) levels in vivo
    • Jones RG, et al. Protein kinase B regulates T lymphocyte survival, nuclear factor kappaB activation, and Bcl-X(L) levels in vivo. J Exp Med 2000;191:1721-1734.
    • (2000) J Exp Med , vol.191 , pp. 1721-1734
    • Jones, R.G.1
  • 78
    • 0036316344 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappaB-dependent transcription
    • Kane LP, Mollenauer MN, Xu Z, Turck SW, Weiss A. Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappaB-dependent transcription. Mol Cell Biol 2002;22:5962-5974.
    • (2002) Mol Cell Biol , vol.22 , pp. 5962-5974
    • Kane, L.P.1    Mollenauer, M.N.2    Xu, Z.3    Turck, S.W.4    Weiss, A.5
  • 79
    • 0036679733 scopus 로고    scopus 로고
    • It's all Rel-ative: NF-kappaB and CD28 costimulation of T-cell activation
    • Kane LP, Lin J, Weiss A. It's all Rel-ative: NF-kappaB and CD28 costimulation of T-cell activation. Trends Immunol 2002;23:413-420.
    • (2002) Trends Immunol , vol.23 , pp. 413-420
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 80
    • 0037007092 scopus 로고    scopus 로고
    • Genetic evidence for Shc requirement in TCR-induced c-Rel nuclear translocation and IL-2 expression
    • Iwashima M, et al. Genetic evidence for Shc requirement in TCR-induced c-Rel nuclear translocation and IL-2 expression. Proc Natl Acad Sci USA 2002;99:4544-4549.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4544-4549
    • Iwashima, M.1
  • 81
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: A hard Akt to follow
    • Brazil DP, Hemmings BA. Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem Sci 2001;26:657-664.
    • (2001) Trends Biochem Sci , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 82
    • 0032054551 scopus 로고    scopus 로고
    • A phosphoinositide-binding sequence is shared by PH domain target molecules - A model for the binding of PH domains to proteins
    • Alberti S. A phosphoinositide-binding sequence is shared by PH domain target molecules - a model for the binding of PH domains to proteins. Proteins 1998;31:1-9.
    • (1998) Proteins , vol.31 , pp. 1-9
    • Alberti, S.1
  • 83
    • 0028912932 scopus 로고
    • AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation
    • Datta K, et al. AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation. Mol Cell Biol 1995;15:2304-2310.
    • (1995) Mol Cell Biol , vol.15 , pp. 2304-2310
    • Datta, K.1
  • 85
    • 0035413614 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: Properties, functions, and regulation
    • Ali A, Hoeflich KP, Woodgett JR. Glycogen synthase kinase-3: properties, functions, and regulation. Chem Rev 2001;101:2527-2540.
    • (2001) Chem Rev , vol.101 , pp. 2527-2540
    • Ali, A.1    Hoeflich, K.P.2    Woodgett, J.R.3
  • 86
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation
    • Hoefilch KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR. Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation. Nature 2000;406:86-90.
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoefilch, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6
  • 87
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-(κ)B activity
    • Karin M, Ben-Neriah T. Phosphorylation meets ubiquitination: the control of NF-(κ)B activity. Annu Rev Immunol 2000;18:621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, T.2
  • 88
    • 0034600901 scopus 로고    scopus 로고
    • Negative regulation of T cell proliferation and interleukin 2 production by the serine threonine kinase GSK-3
    • Ohteki T, et al. Negative regulation of T cell proliferation and interleukin 2 production by the serine threonine kinase GSK-3. J Exp Med 2000;192:99-104.
    • (2000) J Exp Med , vol.192 , pp. 99-104
    • Ohteki, T.1
  • 89
    • 0036629251 scopus 로고    scopus 로고
    • Cell cycle and death control: Long live Forkheads
    • Burgering BM, Kops GJ. Cell cycle and death control: long live Forkheads. Trends Biochem Sci 2002;27:352-360.
    • (2002) Trends Biochem Sci , vol.27 , pp. 352-360
    • Burgering, B.M.1    Kops, G.J.2
  • 90
    • 0030659557 scopus 로고    scopus 로고
    • The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans
    • Ogg S, et al. The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans. Nature 1997;389:994-999.
    • (1997) Nature , vol.389 , pp. 994-999
    • Ogg, S.1
  • 91
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
    • Paradis 8, Ruvkun G. Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor. Genes Dev 1998;12:2488-2498.
    • (1998) Genes Dev , vol.12 , pp. 2488-2498
    • Paradis, B.1    Ruvkun, G.2
  • 92
    • 0030657540 scopus 로고    scopus 로고
    • daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans
    • Lin K, Dorman JB, Rodan A, Kenyon C. daf-16: an HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans. Science 1997;278:1319-1322.
    • (1997) Science , vol.278 , pp. 1319-1322
    • Lin, K.1    Dorman, J.B.2    Rodan, A.3    Kenyon, C.4
  • 93
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a forkhead transcription factor
    • Brunet A, et al. Akt promotes cell survival by phosphorylating and inhibiting a forkhead transcription factor. Cell 1999;96:857-868.
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 94
    • 0037094096 scopus 로고    scopus 로고
    • The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2
    • Stahl M, et al. The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2. J Immunol 2002;168:5024-5031.
    • (2002) J Immunol , vol.168 , pp. 5024-5031
    • Stahl, M.1
  • 95
    • 0036595050 scopus 로고    scopus 로고
    • T-cell signalling and autoimmunity: Molecular mechanisms of disease
    • Ohashi PS. T-cell signalling and autoimmunity: molecular mechanisms of disease. Nat Rev Immunol 2002;2:427-438.
    • (2002) Nat Rev Immunol , vol.2 , pp. 427-438
    • Ohashi, P.S.1
  • 96
    • 0034609737 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1
    • Dijkers PF, Medema RH, Lammers JW, Koenderman L, Coffer PJ. Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr Biol 2000;10:1201-1204.
    • (2000) Curr Biol , vol.10 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3    Koenderman, L.4    Coffer, P.J.5
  • 97
    • 0036069819 scopus 로고    scopus 로고
    • Activated T cell death in vivo mediated by proapoptotic bcl-2 family member bim
    • Hildeman DA, et al. Activated T cell death in vivo mediated by proapoptotic bcl-2 family member bim. Immunity 2002;16:759-767.
    • (2002) Immunity , vol.16 , pp. 759-767
    • Hildeman, D.A.1
  • 99
    • 0035793570 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibits the DNA binding activity of NFATc
    • Neal JW, Clipstone NA. Glycogen synthase kinase-3 inhibits the DNA binding activity of NFATc. J Biol Chem 2001;276:3666-3673.
    • (2001) J Biol Chem , vol.276 , pp. 3666-3673
    • Neal, J.W.1    Clipstone, N.A.2
  • 100
    • 0034292369 scopus 로고    scopus 로고
    • CD28 utilizes Vav-1 to enhance TCR-proximal signaling and NF-AT activation
    • Michel F, et al. CD28 utilizes Vav-1 to enhance TCR-proximal signaling and NF-AT activation. J Immunol 2000;165:3820-3829.
    • (2000) J Immunol , vol.165 , pp. 3820-3829
    • Michel, F.1
  • 101
    • 0037015038 scopus 로고    scopus 로고
    • Genomic expression programs and the integration of the CD28 costimulatory signal in T cell activation
    • Diehn M, et al. Genomic expression programs and the integration of the CD28 costimulatory signal in T cell activation. Proc Nat/Acad Sci USA 2002;99:11796-11801.
    • (2002) Proc Nat/Acad Sci USA , vol.99 , pp. 11796-11801
    • Diehn, M.1
  • 102
    • 0032534281 scopus 로고    scopus 로고
    • Nuclear factor of activated T cells and AP-1 are insufficient for IL-2 promoter activation: Requirement for CD28 up-regulation of KE/AP
    • Shapiro VS, Mollenauer MN, Weiss A. Nuclear factor of activated T cells and AP-1 are insufficient for IL-2 promoter activation: requirement for CD28 up-regulation of KE/AP. J Immunol 1998;161:6455-6458.
    • (1998) J Immunol , vol.161 , pp. 6455-6458
    • Shapiro, V.S.1    Mollenauer, M.N.2    Weiss, A.3
  • 103
    • 0037015055 scopus 로고    scopus 로고
    • Modulation of TCR-induced transcriptional profiles by ligation of CD28, ICOS, and CTLA-4 receptors
    • Riley JL, et al. Modulation of TCR-induced transcriptional profiles by ligation of CD28, ICOS, and CTLA-4 receptors. Proc Nad Acad Sci USA 2002;99:11790-11795.
    • (2002) Proc Nad Acad Sci USA , vol.99 , pp. 11790-11795
    • Riley, J.L.1
  • 104
    • 0032484019 scopus 로고    scopus 로고
    • CREB is a regulatory target for the protein kinase Akt/PKB
    • Du K, Montminy M. CREB is a regulatory target for the protein kinase Akt/PKB. J Biol Chem 1998;273:32377-32379.
    • (1998) J Biol Chem , vol.273 , pp. 32377-32379
    • Du, K.1    Montminy, M.2
  • 105
    • 0032772367 scopus 로고    scopus 로고
    • The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB
    • Wang JM, Chao JR, Chen W, Kuo ML, Yen JJ, Yang-Yen HR. The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB. Mol Cell Biol 1999;19:6195-6206.
    • (1999) Mol Cell Biol , vol.19 , pp. 6195-6206
    • Wang, J.M.1    Chao, J.R.2    Chen, W.3    Kuo, M.L.4    Yen, J.J.5    Yang-Yen, H.R.6
  • 106
    • 0035898449 scopus 로고    scopus 로고
    • Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-kappaB, Bad, or caspase activation
    • Liu H, Perlman H, Pagliari LJ, Pope RM. Constitutively activated Akt-1 is vital for the survival of human monocyte-differentiated macrophages. Role of Mcl-1, independent of nuclear factor (NF)-kappaB, Bad, or caspase activation. J Exp Med 2001;194:113-126.
    • (2001) J Exp Med , vol.194 , pp. 113-126
    • Liu, H.1    Perlman, H.2    Pagliari, L.J.3    Pope, R.M.4
  • 107
    • 0035896575 scopus 로고    scopus 로고
    • AKT induces transcriptional activity of PU.1 through phosphorylation-mediated modifications within its transactivation domain
    • Rieske P, Pongubala JM. AKT induces transcriptional activity of PU.1 through phosphorylation-mediated modifications within its transactivation domain. J Biol Chem 2001;276:8460-8468.
    • (2001) J Biol Chem , vol.276 , pp. 8460-8468
    • Rieske, P.1    Pongubala, J.M.2
  • 108
    • 0029163387 scopus 로고
    • CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-XL
    • Boise LH, et al. CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-XL. Immunity 1995;3:87-98.
    • (1995) Immunity , vol.3 , pp. 87-98
    • Boise, L.H.1
  • 109
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • Chen C, Edelstein LC, Gelinas C. The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol Cell Biol 2000;20:2687-2695.
    • (2000) Mol Cell Biol , vol.20 , pp. 2687-2695
    • Chen, C.1    Edelstein, L.C.2    Gelinas, C.3
  • 110
    • 0034663779 scopus 로고    scopus 로고
    • The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes
    • Khoshnan A, Tindell C, Laux I, Bae D, Bennett B, Nel AE. The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes. J Immunol 2000;165:1743-1754.
    • (2000) J Immunol , vol.165 , pp. 1743-1754
    • Khoshnan, A.1    Tindell, C.2    Laux, I.3    Bae, D.4    Bennett, B.5    Nel, A.E.6
  • 111
    • 0037025948 scopus 로고    scopus 로고
    • CD28-dependent activation of protein kinase B/Akt blocks Fas-mediated apoptosis by preventing death-inducing signaling complex assembly
    • Jones RG, et al. CD28-dependent activation of protein kinase B/Akt blocks Fas-mediated apoptosis by preventing death-inducing signaling complex assembly. J Exp Med 2002;196:335-348.
    • (2002) J Exp Med , vol.196 , pp. 335-348
    • Jones, R.G.1
  • 112
    • 0039058167 scopus 로고    scopus 로고
    • Protection of CD95-mediated apoptosis by activation of phosphatidylinositide 3-kinase and protein kinase B
    • Hansler P, Papoff G, Eramo A, Reif K, Cantrell DA, Ruberti G. Protection of CD95-mediated apoptosis by activation of phosphatidylinositide 3-kinase and protein kinase B. Eur J Immunol 1998;28:57-69.
    • (1998) Eur J Immunol , vol.28 , pp. 57-69
    • Hansler, P.1    Papoff, G.2    Eramo, A.3    Reif, K.4    Cantrell, D.A.5    Ruberti, G.6
  • 114
    • 0033994661 scopus 로고    scopus 로고
    • The insulin-like growth factor-I receptor is regulated by CD28 and protects activated T cells from apoptosis
    • Walsh PT, O'Connor R. The insulin-like growth factor-I receptor is regulated by CD28 and protects activated T cells from apoptosis. Eur J Immunol 2000;30:1010-1018.
    • (2000) Eur J Immunol , vol.30 , pp. 1010-1018
    • Walsh, P.T.1    O'Connor, R.2
  • 115
    • 0033843341 scopus 로고    scopus 로고
    • Regulation of T cell development in the thymus
    • Kaye J. Regulation of T cell development in the thymus. Immunol Res 2000;21:71-81.
    • (2000) Immunol Res , vol.21 , pp. 71-81
    • Kaye, J.1
  • 116
    • 0031025652 scopus 로고    scopus 로고
    • Induction of the early growth response (Egr) family of transcription factors during thymic selection
    • Shao H, Kono DH, Chen LY, Rubm EM, Kaye J. Induction of the early growth response (Egr) family of transcription factors during thymic selection. J Exp Med 1997;185:731-744.
    • (1997) J Exp Med , vol.185 , pp. 731-744
    • Shao, H.1    Kono, D.H.2    Chen, L.Y.3    Rubm, E.M.4    Kaye, J.5
  • 117
    • 0037103324 scopus 로고    scopus 로고
    • Thymocyte development in early growth response gene 1-deficient mice
    • Bettini M, Xi H, Milbrandt J, Kersh GJ. Thymocyte development in early growth response gene 1-deficient mice. J Immunol 2002;169:1713-1720.
    • (2002) J Immunol , vol.169 , pp. 1713-1720
    • Bettini, M.1    Xi, H.2    Milbrandt, J.3    Kersh, G.J.4
  • 118
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997;278:687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 119
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997;91:231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1
  • 120
    • 0032787346 scopus 로고    scopus 로고
    • Signaling pathways mediating insulin-stimulated glucose transport
    • Summers SA, et al. Signaling pathways mediating insulin-stimulated glucose transport. Ann New York Acad Sci 1999;892:169-186.
    • (1999) Ann New York Acad Sci , vol.892 , pp. 169-186
    • Summers, S.A.1
  • 121
    • 0033976064 scopus 로고    scopus 로고
    • CD28 costimulation mediates T cell expansion via IL-2-independent and IL-2-dependent regulation of cell cycle progression
    • Appleman LJ, Berezovskaya A, Grass I, Boussiotis VA. CD28 costimulation mediates T cell expansion via IL-2-independent and IL-2-dependent regulation of cell cycle progression. J Immunol 2000;164:144-151.
    • (2000) J Immunol , vol.164 , pp. 144-151
    • Appleman, L.J.1    Berezovskaya, A.2    Grass, I.3    Boussiotis, V.A.4
  • 122
    • 0034670094 scopus 로고    scopus 로고
    • Signal transduction pathways that contribute to increased protein synthesis during T-cell activation
    • Miyamoto S, Kimball SR, Safer B. Signal transduction pathways that contribute to increased protein synthesis during T-cell activation. Biochim Biophys Acta 2000;1494:28-42.
    • (2000) Biochim Biophys Acta , vol.1494 , pp. 28-42
    • Miyamoto, S.1    Kimball, S.R.2    Safer, B.3
  • 123
    • 0025734876 scopus 로고
    • Inhibition of T and B lymphocyte proliferation by rapamycin
    • Kay JE, Kromwel L, Doe SE, Denyer M. Inhibition of T and B lymphocyte proliferation by rapamycin. Immunology 1991;72:544-549.
    • (1991) Immunology , vol.72 , pp. 544-549
    • Kay, J.E.1    Kromwel, L.2    Doe, S.E.3    Denyer, M.4
  • 124
    • 0025806666 scopus 로고
    • Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A
    • Sigal NH, Lin CS, Siekierka JJ. Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A. Transplant Proc 1991;23:1-5.
    • (1991) Transplant Proc , vol.23 , pp. 1-5
    • Sigal, N.H.1    Lin, C.S.2    Siekierka, J.J.3
  • 125
    • 0025977970 scopus 로고
    • The effect of the immunosuppressant FK-506 on alternate pathways of T cell activation
    • Bierer BE, Schreiber SL, Burakoff SJ. The effect of the immunosuppressant FK-506 on alternate pathways of T cell activation. Eur J Immunol 1991;21:439-445.
    • (1991) Eur J Immunol , vol.21 , pp. 439-445
    • Bierer, B.E.1    Schreiber, S.L.2    Burakoff, S.J.3
  • 126
    • 0033000334 scopus 로고    scopus 로고
    • p;70: Integrates phosphatidyhnositol 3-kinase and rapamycin- regulated signals for E2F regulation in T lymphocytes
    • Brennan P, Babbage JW, Thomas G, Cantrell D. p;70: integrates phosphatidyhnositol 3-kinase and rapamycin- regulated signals for E2F regulation in T lymphocytes. Mol Cell Biol 1999;19:4729-4738.
    • (1999) Mol Cell Biol , vol.19 , pp. 4729-4738
    • Brennan, P.1    Babbage, J.W.2    Thomas, G.3    Cantrell, D.4
  • 127
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits capdependent imtiation of translation
    • Beretta L, Gingras AC, Svitkin YV, Hall MN, Sonenberg N. Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits capdependent imtiation of translation. EMBO J 1996;15:658-664.
    • (1996) EMBO J , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 128
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • Gingras AC, Kennedy SG, O'Leary MA, Sonenberg N, Hay N. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev 1998;12:502-513.
    • (1998) Genes Dev , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 129
    • 0033604521 scopus 로고    scopus 로고
    • Ribosomal S6 kinase signaling and the control of translation
    • Dufner A, Thomas G. Ribosomal S6 kinase signaling and the control of translation. Exp Cell Res 1999;253:100-109.
    • (1999) Exp Cell Res , vol.253 , pp. 100-109
    • Dufner, A.1    Thomas, G.2
  • 130
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway
    • Manning BD, Tee AR, Logsdon MN, Blenis J, Candey LC. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway. Mol Cell 2002;10:151-162.
    • (2002) Mol Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Candey, L.C.5
  • 131
    • 0032079873 scopus 로고    scopus 로고
    • Regulation of translation initiation factors by signal transduction
    • Kleijn M, Scheper GC, Voorma HO, Thomas AA. Regulation of translation initiation factors by signal transduction. Eur J Biochem 1998;253:531-544.
    • (1998) Eur J Biochem , vol.253 , pp. 531-544
    • Kleijn, M.1    Scheper, G.C.2    Voorma, H.O.3    Thomas, A.A.4
  • 132
    • 0036136897 scopus 로고    scopus 로고
    • Role of translation initiation factor 2B in control of cell survival by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta signaling pathway
    • Pap M, Cooper GM. Role of translation initiation factor 2B in control of cell survival by the phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3beta signaling pathway. Mol Cell Biol 2002;22:578-586.
    • (2002) Mol Cell Biol , vol.22 , pp. 578-586
    • Pap, M.1    Cooper, G.M.2
  • 133
    • 17544374351 scopus 로고    scopus 로고
    • T-cell activation leads to rapid stimulation of translation initiation factor eIF2B and inactivation of glycogen synthase kinase-3
    • Welsh GI, Miyamoto S, Price NT, Safer B, Proud CG. T-cell activation leads to rapid stimulation of translation initiation factor eIF2B and inactivation of glycogen synthase kinase-3. J Biol Chem 1996;271:11410-11413.
    • (1996) J Biol Chem , vol.271 , pp. 11410-11413
    • Welsh, G.I.1    Miyamoto, S.2    Price, N.T.3    Safer, B.4    Proud, C.G.5
  • 134
    • 34248376930 scopus 로고    scopus 로고
    • The regulation of protein synthesis and translation factors by CD3 and CD28 in human primary T lymphocytes
    • Kleijn M, Proud CG. The regulation of protein synthesis and translation factors by CD3 and CD28 in human primary T lymphocytes. BMC Biochem 2002;3:11.
    • (2002) BMC Biochem , vol.3 , pp. 11
    • Kleijn, M.1    Proud, C.G.2
  • 135
    • 0035124549 scopus 로고    scopus 로고
    • T cell receptor signalling
    • Lin J, Weiss A. T cell receptor signalling. J Cell Sci 2001;114:243-244.
    • (2001) J Cell Sci , vol.114 , pp. 243-244
    • Lin, J.1    Weiss, A.2
  • 136
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • Kane LP, Lin J, Weiss A. Signal transduction by the TCR for antigen. Curr Opin Immunol 2000;12:242-249.
    • (2000) Curr Opin Immunol , vol.12 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 137
    • 0036162250 scopus 로고    scopus 로고
    • Signalling scaffolds and adaptors in T-cell immunity
    • Geng L, Rudd CE. Signalling scaffolds and adaptors in T-cell immunity. Br J Haematol 2002;116:19-27.
    • (2002) Br J Haematol , vol.116 , pp. 19-27
    • Geng, L.1    Rudd, C.E.2
  • 138
    • 0036200194 scopus 로고    scopus 로고
    • Protein kinase B (Akt) regulation and function in T lymphocytes
    • Cantrell D. Protein kinase B (Akt) regulation and function in T lymphocytes. Semin Immunol 2002;14:19-26.
    • (2002) Semin Immunol , vol.14 , pp. 19-26
    • Cantrell, D.1
  • 139
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: a play in three Akts. Genes Dev 1999;13:2905-2927.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3


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