메뉴 건너뛰기




Volumn 192, Issue , 2003, Pages 80-97

Lipid phosphatases in the regulation of T cell activation: Living up to their PTEN-tial

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; INOSITOL; ITK PROTEIN; LIPID PHOSPHATASE; PHOSPHATASE; PHOSPHATE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4 BISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOLIPASE C; PHOSPHOLIPID; PROTEIN; PROTEIN KINASE B; PROTEIN KINASE C ZETA; RECEPTOR; SERINE; T LYMPHOCYTE RECEPTOR; TEC PROTEIN; THREONINE; TYROSINE; UNCLASSIFIED DRUG; VAV PROTEIN;

EID: 0037564493     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2003.00013.x     Document Type: Review
Times cited : (43)

References (198)
  • 1
    • 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
  • 2
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck B, et al. Synthesis and function of 3-phosphorylated inositol lipids. Annu Rev Biochem 2002;70:535-602.
    • (2002) Annu Rev Biochem , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 3
    • 0037138365 scopus 로고    scopus 로고
    • Interaction domains: From simple binding events to complex cellular behavior
    • Pawson T, Raina M, Nash P. Interaction domains: from simple binding events to complex cellular behavior. FEBS Lett 2002;513:2-10.
    • (2002) FEBS Lett , vol.513 , pp. 2-10
    • Pawson, T.1    Raina, M.2    Nash, P.3
  • 5
    • 0032929762 scopus 로고    scopus 로고
    • Signalling through phosphoinositide 3-kinases: The lipids take centre stage
    • Leevers SJ, Vanhaesebroeck B, Waterfield MD. Signalling through phosphoinositide 3-kinases: the lipids take centre stage. Curr Opin Cell Biol 1999;11:219-225.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 219-225
    • Leevers, S.J.1    Vanhaesebroeck, B.2    Waterfield, M.D.3
  • 6
    • 0031831780 scopus 로고    scopus 로고
    • Pleckstrin homology domains: A common fold with diverse functions
    • Rebecchi MJ, Scarlata S. Pleckstrin homology domains: a common fold with diverse functions. Annu Rev Biophys Biomol Struct 1998;27:503-528.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 503-528
    • Rebecchi, M.J.1    Scarlata, S.2
  • 7
    • 0007724488 scopus 로고    scopus 로고
    • The PH superfold: A structural scaffold for multiple functions
    • Blomberg N, Baraldi E, Nilges M, Saraste M. The PH superfold: a structural scaffold for multiple functions. Trends Biochem Sci 1999;24:441-445.
    • (1999) Trends Biochem Sci , vol.24 , pp. 441-445
    • Blomberg, N.1    Baraldi, E.2    Nilges, M.3    Saraste, M.4
  • 8
    • 0033603214 scopus 로고    scopus 로고
    • Phosphoinositide binding domains: Embracing 3-phosphate
    • Fruman DA, Rameh LE, Cantley LC. Phosphoinositide binding domains: embracing 3-phosphate. Cell 1999;97:817-820.
    • (1999) Cell , vol.97 , pp. 817-820
    • Fruman, D.A.1    Rameh, L.E.2    Cantley, L.C.3
  • 9
    • 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
  • 10
    • 0035967888 scopus 로고    scopus 로고
    • Phoxy lipids: Revealing PX domains as phosphoinositide binding modules
    • Wishart MJ, Taylor GS, Dixon JE. Phoxy lipids: revealing PX domains as phosphoinositide binding modules. Cell 2001;105:817-820.
    • (2001) Cell , vol.105 , pp. 817-820
    • Wishart, M.J.1    Taylor, G.S.2    Dixon, J.E.3
  • 11
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh LE, Cantley LC. The role of phosphoinositide 3-kinase lipid products in cell function. J Biol Chem 1999;274:8347-8350.
    • (1999) J Biol Chem , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 12
    • 0344653108 scopus 로고    scopus 로고
    • Activation of phospholipase C-gamma by phosphatidylinositol 3,4,5-trisphosphate
    • Bae YS, Cantley LG, Chen CS, Kim SR, Kwon KS, Rhee SG. Activation of phospholipase C-gamma by phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 1998;273:4465-4469.
    • (1998) J Biol Chem , vol.273 , pp. 4465-4469
    • Bae, Y.S.1    Cantley, L.G.2    Chen, C.S.3    Kim, S.R.4    Kwon, K.S.5    Rhee, S.G.6
  • 13
    • 0026502874 scopus 로고
    • Regulation of D-3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigens
    • Ward SG, Ley SC, MacPhee C, Cantrell DA. Regulation of D-3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigens. 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.A.4
  • 14
    • 0026554564 scopus 로고
    • Identification of distinct populations of PI-3 kinase activity following T-cell activation
    • Thompson PA, Gutkind JS, Robbins KC, Ledbetter JA, Bolen JB. Identification of distinct populations of PI-3 kinase activity following T-cell activation. Oncogene 1992;7:719-725.
    • (1992) Oncogene , vol.7 , pp. 719-725
    • Thompson, P.A.1    Gutkind, J.S.2    Robbins, K.C.3    Ledbetter, J.A.4    Bolen, J.B.5
  • 15
    • 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
  • 16
    • 0029060259 scopus 로고
    • Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase, and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion
    • Ueda Y, et al. Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase, and wortmannin reveals heterogeneity m the regulation of T cell IL-2 secretion. Int Immunol 1995;7:957-966.
    • (1995) Int Immunol , vol.7 , pp. 957-966
    • Ueda, Y.1
  • 17
    • 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
  • 18
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts wink the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif
    • Prasad KV, et al. T-cell antigen CD28 interacts wink 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
  • 19
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling
    • Pages F, et al. Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling. Nature 1994;369:327-329.
    • (1994) Nature , vol.369 , pp. 327-329
    • Pages, F.1
  • 20
    • 0028211126 scopus 로고
    • The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 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 phosphatidylinositol 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
  • 21
    • 0028342859 scopus 로고
    • CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase
    • August A, Dupont B. CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase. Int Immunol 1994;6:769-774.
    • (1994) Int Immunol , vol.6 , pp. 769-774
    • August, A.1    Dupont, B.2
  • 22
    • 0032516873 scopus 로고    scopus 로고
    • Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction
    • Okkenhaug K, Rottapel R. Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction. J Biol Chem 1998;273:21194-21202.
    • (1998) J Biol Chem , vol.273 , pp. 21194-21202
    • Okkenhaug, K.1    Rottapel, R.2
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998;92:83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0032190774 scopus 로고    scopus 로고
    • p21 ras initiates Rac-1 but not phosphatidyl inositol 3 kinase/PKB mediated signaling pathways in T lymphocytes
    • Genot E, Reif K, Beach S, Kramer I, Cantrell D. p21 ras initiates Rac-1 but not phosphatidyl inositol 3 kinase/PKB mediated signaling pathways in T lymphocytes. Oncogene 1998;17:1731-1738.
    • (1998) Oncogene , vol.17 , pp. 1731-1738
    • Genot, E.1    Reif, K.2    Beach, S.3    Kramer, I.4    Cantrell, D.5
  • 29
    • 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
  • 30
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias KF, Cantley LC, Carpenter CL. Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 1995;270:17656-17659.
    • (1995) J Biol Chem , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 31
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng Y, Bagrodia S, Cerione RA. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J Biol Chem 1994;269:18727-18730.
    • (1994) J Biol Chem , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 32
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong LD, Traynor-Kaplan A, Bokoch GM, Schwartz MA. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994;79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 33
    • 0026316011 scopus 로고
    • Interleukin-2 receptor regulates activation of phosphatidylinositol 3-kinase
    • Remillard B, et al. Interleukin-2 receptor regulates activation of phosphatidylinositol 3-kinase. J Biol Chem 1991;266:14167-14170.
    • (1991) J Biol Chem , vol.266 , pp. 14167-14170
    • Remillard, B.1
  • 34
    • 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
  • 35
    • 0034282897 scopus 로고    scopus 로고
    • The docking molecule gab2 is induced by lymphocyte activation and is involved in signaling by interleukin-2 and interleukin-15 but not other common gamma chain-using cytokines
    • Gadina M, et al. The docking molecule gab2 is induced by lymphocyte activation and is involved in signaling by interleukin-2 and interleukin-15 but not other common gamma chain-using cytokines. J Biol Chem 2000;275:26959-26966.
    • (2000) J Biol Chem , vol.275 , pp. 26959-26966
    • Gadina, M.1
  • 36
    • 0033647242 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: A key biochemical signal for cell migration in response to chemokines
    • Sotsios Y, Ward SG. Phosphoinositide 3-kinase: a key biochemical signal for cell migration in response to chemokines. Immunol Rev 2000;177:217-235.
    • (2000) Immunol Rev , vol.177 , pp. 217-235
    • Sotsios, Y.1    Ward, S.G.2
  • 37
    • 0027218948 scopus 로고
    • Evidence that protein tyrosine kinase p56-Lck regulates the activity of phosphatidylinositol-3′-kinase in interleukin-2-dependent T-cells
    • Taichman R, Merida I, Torigoe T, Gaulton GN, Reed JC. Evidence that protein tyrosine kinase p56-Lck regulates the activity of phosphatidylinositol-3′-kinase in interleukin-2-dependent T-cells. J Biol Chem 1993;268:20031-20036.
    • (1993) J Biol Chem , vol.268 , pp. 20031-20036
    • Taichman, R.1    Merida, I.2    Torigoe, T.3    Gaulton, G.N.4    Reed, J.C.5
  • 38
    • 0027954564 scopus 로고
    • Activation of phosphatidylinositol-3-kinase in Jurkat T cells depends on the presence of the p56lck tyrosine kinase
    • Von Willebrand M, Baier G, Couture C, Burn P, Mustelin T. Activation of phosphatidylinositol-3-kinase in Jurkat T cells depends on the presence of the p56lck tyrosine kinase. Eur J Immunol 1994;24:234-238.
    • (1994) Eur J Immunol , vol.24 , pp. 234-238
    • Von Willebrand, M.1    Baier, G.2    Couture, C.3    Burn, P.4    Mustelin, T.5
  • 39
    • 0027925923 scopus 로고
    • Regulation of CD4-p56lck-associated phosphatidylinositol 3-kinase (PI 3-kinase) and phosphatidylinositol 4-kinase (PI 4-kinase)
    • Prasad KV, et al. Regulation of CD4-p56lck-associated phosphatidylinositol 3-kinase (PI 3-kinase) and phosphatidylinositol 4-kinase (PI 4-kinase). Philos Trans R Soc London B Biol Sci 1993;342:35-42.
    • (1993) Philos Trans R Soc London B Biol Sci , vol.342 , pp. 35-42
    • Prasad, K.V.1
  • 40
    • 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
  • 41
    • 0032561341 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulation of T cell receptor-mediated interleukin-2 gene expression in normal T cells
    • Eder AM, Dominguez L, Franke TF, Ashwell JD. Phosphoinositide 3-kinase regulation of T cell receptor-mediated interleukin-2 gene expression in normal T cells. J Biol Chem 1998;273:28025-28031.
    • (1998) J Biol Chem , vol.273 , pp. 28025-28031
    • Eder, A.M.1    Dominguez, L.2    Franke, T.F.3    Ashwell, J.D.4
  • 42
    • 0030010956 scopus 로고    scopus 로고
    • Signaling through CD28/CTLA-4 family receptors puzzling participation of phosphatidylinositol-3 kinase
    • Hutchcroft JE, Bierer BE. Signaling through CD28/CTLA-4 family receptors puzzling participation of phosphatidylinositol-3 kinase. J Immunol 1996;156:4071-4074.
    • (1996) J Immunol , vol.156 , pp. 4071-4074
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 43
    • 0029056902 scopus 로고
    • Phorbol ester treatment inhibits phosphatidylinositol 3-kinase activation by, and association with, CD28, a T-lymphocyte surface receptor
    • Hutchcroft JE, Franklin DP, Tsai B, Harrison-Findik D, Varticovski L, Bierer BE. Phorbol ester treatment inhibits phosphatidylinositol 3-kinase activation by, and association with, CD28, a T-lymphocyte surface receptor. Proc Natl Acad Sci USA 1995;92:8808-8812.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8808-8812
    • Hutchcroft, J.E.1    Franklin, D.P.2    Tsai, B.3    Harrison-Findik, D.4    Varticovski, L.5    Bierer, B.E.6
  • 44
    • 0028956419 scopus 로고
    • Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: Studies with a selective inhibitor, wortmannin
    • Lu Y, Phillips CA, Trevillyan JM. Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: studies with a selective inhibitor, wortmannin. Eur J Immunol 1995;25:533-537.
    • (1995) Eur J Immunol , vol.25 , pp. 533-537
    • Lu, Y.1    Phillips, C.A.2    Trevillyan, J.M.3
  • 45
    • 0028972549 scopus 로고
    • CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase
    • Truitt KE, Shi J, Gibson S, Segal LG, Mills GB, Imboden JB. CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase. J Immunol 1995;155:4702-4710.
    • (1995) J Immunol , vol.155 , pp. 4702-4710
    • Truitt, K.E.1    Shi, J.2    Gibson, S.3    Segal, L.G.4    Mills, G.B.5    Imboden, J.B.6
  • 46
    • 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
  • 47
    • 0035451761 scopus 로고    scopus 로고
    • PI 3-K and T-cell activation: Limitations of T-leukemic cell lines as signaling models
    • Astoul E, Edmunds C, Cantrell DA, 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    Edmunds, C.2    Cantrell, d.A.3    Ward, S.G.4
  • 48
    • 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
  • 49
    • 0034107671 scopus 로고    scopus 로고
    • Increased phosphoinositide 3-kinase activity reduces a lymphoproliferative disorder and contributes to tumor generation in vivo
    • Borlado LR, et al. Increased phosphoinositide 3-kinase activity reduces a lymphoproliferative disorder and contributes to tumor generation in vivo. FASEB J 2000;14:895-903.
    • (2000) FASEB J , vol.14 , pp. 895-903
    • Borlado, L.R.1
  • 50
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha
    • Fruman DA, et al. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha. Science 1999;283:393-397.
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1
  • 51
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase
    • Suzuki H, et al. Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase. Science 1999;283:390-392.
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1
  • 52
    • 0037039317 scopus 로고    scopus 로고
    • Increased insulin sensitivity in mice lacking p85beta subunit of phosphoinositide 3-kinase
    • Ueki K, et al. Increased insulin sensitivity in mice lacking p85beta subunit of phosphoinositide 3-kinase. Proc Natl Acad Sci USA 2002;99:419-424.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 419-424
    • Ueki, K.1
  • 53
    • 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
  • 54
    • 0036185944 scopus 로고    scopus 로고
    • Early embryonic lethality in mice deficient in the p110beta catalytic subunit of PI 3-kinase
    • Bi L, Okabe I, Bernard DJ, Nussbaum RL. Early embryonic lethality in mice deficient in the p110beta catalytic subunit of PI 3-kinase. Mamm Genome 2002;13:169-172.
    • (2002) Mamm Genome , vol.13 , pp. 169-172
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Nussbaum, R.L.4
  • 55
    • 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
  • 56
    • 0034635264 scopus 로고    scopus 로고
    • Function of PI3Kgaamma in thymocyte development T cell activation, and neutrophil migration
    • Sasaki T, et al. Function of PI3Kgaamma in thymocyte development T cell activation, and neutrophil migration. Science 2000;287:1040-1046.
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1
  • 57
    • 0034635452 scopus 로고    scopus 로고
    • Central role for G protein-coupled phosphoinositide 3-kinase gamma in inflammation
    • Hirsch E, et al. Central role for G protein-coupled phosphoinositide 3-kinase gamma in inflammation. Science 2000;287:1049-1053.
    • (2000) Science , vol.287 , pp. 1049-1053
    • Hirsch, E.1
  • 58
    • 0035869402 scopus 로고    scopus 로고
    • Critical requirement for the membrane-proximal cytosolic tyrosine residue for CD28-mediated costimulation in vivo
    • Harada Y, et al. Critical requirement for the membrane-proximal cytosolic tyrosine residue for CD28-mediated costimulation in vivo. J Immunol 2001;166:3797-3803.
    • (2001) J Immunol , vol.166 , pp. 3797-3803
    • Harada, Y.1
  • 59
    • 0035319244 scopus 로고    scopus 로고
    • A point mutation in CD28 distinguishes proliferative signals from survival signals
    • Okkenhaug K, et al. A point mutation in CD28 distinguishes proliferative signals from survival signals. Nat Immunol 2001; 2:325-332.
    • (2001) Nat Immunol , vol.2 , pp. 325-332
    • Okkenhaug, K.1
  • 60
    • 0033696009 scopus 로고    scopus 로고
    • Tec kinases: A family with multiple roles in immunity
    • Yang WC, Collette Y, Nunes JA, Olive D. Tec kinases: a family with multiple roles in immunity. Immunity 2000;12:373-382.
    • (2000) Immunity , vol.12 , pp. 373-382
    • Yang, W.C.1    Collette, Y.2    Nunes, J.A.3    Olive, D.4
  • 61
    • 0036676540 scopus 로고    scopus 로고
    • Beyond calcium: New signaling pathways for Tec family kinases
    • Takesono A, Finkelstein LD, Schwartzberg PL. Beyond calcium: new signaling pathways for Tec family kinases. J Cell Sci 2002; 115:3039-3048.
    • (2002) J Cell Sci , vol.115 , pp. 3039-3048
    • Takesono, A.1    Finkelstein, L.D.2    Schwartzberg, P.L.3
  • 62
    • 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
  • 63
  • 64
    • 0034687873 scopus 로고    scopus 로고
    • LAT, the linker for activation of T cells: A bridge between T cell specific and general signaling pathways
    • Wange RL. LAT, the linker for activation of T cells: a bridge between T cell specific and general signaling pathways. Sci STKE 2000;2000:RE1.
    • (2000) Sci STKE , vol.2000
    • Wange, R.L.1
  • 65
    • 0032878516 scopus 로고    scopus 로고
    • Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment
    • Shan X, Wange RL. Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment. J Biol Chem 1999;274:29323-29330.
    • (1999) J Biol Chem , vol.274 , pp. 29323-29330
    • Shan, X.1    Wange, R.L.2
  • 66
    • 0034235114 scopus 로고    scopus 로고
    • TCR/CD3-Induced activation and binding of Emt/Itk to linker of activated T cell complexes: Requirement for the Src homology 2 domain
    • Ching KA, Grasis JA, Tailor P, Kawakami Y, Kawakami T, Tsoukas CD. TCR/CD3-Induced activation and binding of Emt/Itk to linker of activated T cell complexes: requirement for the Src homology 2 domain. J Immunol 2000;165:256-262.
    • (2000) J Immunol , vol.165 , pp. 256-262
    • Ching, K.A.1    Grasis, J.A.2    Tailor, P.3    Kawakami, Y.4    Kawakami, T.5    Tsoukas, C.D.6
  • 69
    • 0035167696 scopus 로고    scopus 로고
    • Tec kinase signaling in T cells is regulated by phosphatidylinositol 3-kinase and the Tec pleckstrin homology domain
    • Yang WC, Ching KA, Tsoukas CD, Berg LJ. Tec kinase signaling in T cells is regulated by phosphatidylinositol 3-kinase and the Tec pleckstrin homology domain. J Immunol 2001;166:387-395.
    • (2001) J Immunol , vol.166 , pp. 387-395
    • Yang, W.C.1    Ching, K.A.2    Tsoukas, C.D.3    Berg, L.J.4
  • 70
    • 0035868761 scopus 로고    scopus 로고
    • A novel function for the Tec family tyrosine kinase Itk in activation of beta 1 integrins by the T-cell receptor
    • Woods ML, Kivens WJ, Adelsman MA, Qiu Y, August A, Shimizu Y. A novel function for the Tec family tyrosine kinase Itk in activation of beta 1 integrins by the T-cell receptor. EMBO J 2001; 20:1232-1244.
    • (2001) EMBO J , vol.20 , pp. 1232-1244
    • Woods, M.L.1    Kivens, W.J.2    Adelsman, M.A.3    Qiu, Y.4    August, A.5    Shimizu, Y.6
  • 71
    • 0036499182 scopus 로고    scopus 로고
    • Defective Fas ligand expression and activation-induced cell death in the absence of IL-2-inducible T cell kinase
    • Miller AT, Berg LJ. Defective Fas ligand expression and activation-induced cell death in the absence of IL-2-inducible T cell kinase. J Immunol 2002;168:2163-2172.
    • (2002) J Immunol , vol.168 , pp. 2163-2172
    • Miller, A.T.1    Berg, L.J.2
  • 72
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B, Alessi DR. The PI3K-PDK1 connection: more than just a road to PKB. Biochem J 2000;346:561-576.
    • (2000) Biochem J , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 73
    • 0036280038 scopus 로고    scopus 로고
    • Phosphoinositides and signal transduction
    • Toker A. Phosphoinositides and signal transduction. Cell Mol Life Sci 2002;59:761-779.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 761-779
    • Toker, A.1
  • 74
    • 0033545393 scopus 로고    scopus 로고
    • Intracellular signalling: PDK1 - A kinase at the hub of things
    • Belham C, Wu S, Avruch J. Intracellular signalling: PDK1 - a kinase at the hub of things. Curr Biol 1999;9:R93-R96.
    • (1999) Curr Biol , vol.9
    • Belham, C.1    Wu, S.2    Avruch, J.3
  • 75
    • 12644301164 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase
    • Alessi DR, et al. 3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. Curr Biol 1997;7:776-789.
    • (1997) Curr Biol , vol.7 , pp. 776-789
    • Alessi, D.R.1
  • 76
    • 0032482374 scopus 로고    scopus 로고
    • Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B
    • Anderson KE, Coadwell J, Stephens LR, Hawkins PT. Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B. Curr Biol 1998;8:684-691.
    • (1998) Curr Biol , vol.8 , pp. 684-691
    • Anderson, K.E.1    Coadwell, J.2    Stephens, L.R.3    Hawkins, P.T.4
  • 77
    • 0033084143 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositidedependent protein kinase-1
    • Currie RA, et al. Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositidedependent protein kinase-1. Biochem J 1999;337:575-583.
    • (1999) Biochem J , vol.337 , pp. 575-583
    • Currie, R.A.1
  • 78
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: Pivoting around PDK-1
    • Toker A, Newton AC. Cellular signaling: pivoting around PDK-1. Cell 2000;103:185-188.
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 79
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • Alessi DR, et al. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J 1996;15:6541-6551.
    • (1996) EMBO J , vol.15 , pp. 6541-6551
    • Alessi, D.R.1
  • 80
    • 0033594480 scopus 로고    scopus 로고
    • PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
    • Balendran A, et al. PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr Biol 1999;9:393-404.
    • (1999) Curr Biol , vol.9 , pp. 393-404
    • Balendran, A.1
  • 81
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker A, Newton AC. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J Biol Chem 2000;275:8271-8274.
    • (2000) J Biol Chem , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 82
    • 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
  • 83
    • 0036181470 scopus 로고    scopus 로고
    • Cytokine-mediated inhibition of apoptosis in non-transformed T cells and neutrophils can be dissociated from protein kinase B activation
    • Scheel-Toellner D, et al. Cytokine-mediated inhibition of apoptosis in non-transformed T cells and neutrophils can be dissociated from protein kinase B activation. Eur J Immunol 2002;32:486-493.
    • (2002) Eur J Immunol , vol.32 , pp. 486-493
    • Scheel-Toellner, D.1
  • 84
    • 0034820828 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinases in tumor progression
    • Roymans D, Slegers H. Phosphatidylinositol 3-kinases in tumor progression. Eur J Biochem 2001;268:487-498.
    • (2001) Eur J Biochem , vol.268 , pp. 487-498
    • Roymans, D.1    Slegers, H.2
  • 85
    • 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
  • 86
    • 0037087472 scopus 로고    scopus 로고
    • CD28 costimulation mediates down-regulation of p27kip1 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 p27kip1 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
  • 87
    • 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
  • 88
    • 0030662419 scopus 로고    scopus 로고
    • Activation of the PI3K effector protein kinase B following ligation of CD28 or Fas
    • Parry R, Smith G, Reif K, Sansom DM, Ward S. Activation of the PI3K effector protein kinase B following ligation of CD28 or Fas. Biochem Soc Trans 1997;25:S589.
    • (1997) Biochem Soc Trans , vol.25
    • Parry, R.1    Smith, G.2    Reif, K.3    Sansom, D.M.4    Ward, S.5
  • 89
    • 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
  • 90
    • 0030908525 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase links the interleukin-2 receptor to protein kinase B and p70, S6 kinase
    • Reif K, Burgering BM, Cantrell DA. Phosphatidylinositol 3-kinase links the interleukin-2 receptor to protein kinase B and p70, S6 kinase. J Biol Chem 1997;272:14426-14433.
    • (1997) J Biol Chem , vol.272 , pp. 14426-14433
    • Reif, K.1    Burgering, B.M.2    Cantrell, D.A.3
  • 91
    • 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
  • 93
    • 0036316344 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappa B-dependent transcription
    • Kane LP, Mollenauer MN, Xu Z, Turck CW, Weiss A. Akt-dependent phosphorylation specifically regulates Cot induction of NF-kappa B-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, C.W.4    Weiss, A.5
  • 94
    • 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
  • 95
    • 0033038491 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit
    • Sizemore N, Leung S, Stark GR. Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit. Mol Cell Biol 1999;19:4798-4805.
    • (1999) Mol Cell Biol , vol.19 , pp. 4798-4805
    • Sizemore, N.1    Leung, S.2    Stark, G.R.3
  • 96
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-kappaB
    • Madrid LV, Wang CY, Guttridge DC, Schottelius AJ, Baldwin ASJ, Mayo MW. Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-kappaB. Mol Cell Biol 2000;20:1626-1638.
    • (2000) Mol Cell Biol , vol.20 , pp. 1626-1638
    • Madrid, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin, A.S.J.5    Mayo, M.W.6
  • 97
    • 0036278214 scopus 로고    scopus 로고
    • Protein kinase C and AKT/protein kinase B in CD4+ T-lymphocytes: New partners in TCR/CD28 signal integration
    • Bauer B, Baier G. Protein kinase C and AKT/protein kinase B in CD4+ T-lymphocytes: new partners in TCR/CD28 signal integration. Mol Immunol 2002;38:1087-1099.
    • (2002) Mol Immunol , vol.38 , pp. 1087-1099
    • Bauer, B.1    Baier, G.2
  • 98
    • 0035399612 scopus 로고    scopus 로고
    • Expression of active protein kinase B in T cells perturbs both T and B cell homeostasis and promotes inflammation
    • Parsons MJ, Jones RG, Tsao MS, Odermatt B, Ohashi PS, Woodgett JR. Expression of active protein kinase B in T cells perturbs both T and B cell homeostasis and promotes inflammation. J Immunol 2001;167:42-48.
    • (2001) J Immunol , vol.167 , pp. 42-48
    • Parsons, M.J.1    Jones, R.G.2    Tsao, M.S.3    Odermatt, B.4    Ohashi, P.S.5    Woodgett, J.R.6
  • 99
    • 0035980060 scopus 로고    scopus 로고
    • Akt inhibits the orphan nuclear receptor Nur77 and T-cell apoptosis
    • Masuyama N, Oishi K, Mori Y, Ueno T, Takahama Y, Gotoh Y. Akt inhibits the orphan nuclear receptor Nur77 and T-cell apoptosis. J Biol Chem 2001;276:32799-32805.
    • (2001) J Biol Chem , vol.276 , pp. 32799-32805
    • Masuyama, N.1    Oishi, K.2    Mori, Y.3    Ueno, T.4    Takahama, Y.5    Gotoh, Y.6
  • 100
    • 0035957428 scopus 로고    scopus 로고
    • Akt phosphorylates and regulates the orphan nuclear receptor Nur77
    • Pekarsky Y, et al. Akt phosphorylates and regulates the orphan nuclear receptor Nur77. Proc Natl Acad Sci USA 2001;98:3690-3694.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3690-3694
    • Pekarsky, Y.1
  • 101
    • 0035831556 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells
    • Panka DJ, Mano T, Suhara T, Walsh K, Mier JW. Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells. J Biol Chem 2001;276:6893-6896.
    • (2001) J Biol Chem , vol.276 , pp. 6893-6896
    • Panka, D.J.1    Mano, T.2    Suhara, T.3    Walsh, K.4    Mier, J.W.5
  • 102
    • 0034954418 scopus 로고    scopus 로고
    • Disruption of Akt kinase activation is important for immunosuppression reduced by measles virus
    • Avota E, et al. Disruption of Akt kinase activation is important for immunosuppression reduced by measles virus. Nat Med 2001;7:725-731.
    • (2001) Nat Med , vol.7 , pp. 725-731
    • Avota, E.1
  • 103
    • 0034025493 scopus 로고    scopus 로고
    • Eyes wide shut: Protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters
    • Kazanietz MG. Eyes wide shut: protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters. Mol Carcinog 2000;28:5-11.
    • (2000) Mol Carcinog , vol.28 , pp. 5-11
    • Kazanietz, M.G.1
  • 104
    • 0034529764 scopus 로고    scopus 로고
    • T cell expressed PKCtheta demonstrates cell-type selective function
    • Bauer B, et al. T cell expressed PKCtheta demonstrates cell-type selective function. Eur J Immunol 2000;30:3645-3654.
    • (2000) Eur J Immunol , vol.30 , pp. 3645-3654
    • Bauer, B.1
  • 105
    • 0034724201 scopus 로고    scopus 로고
    • NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta
    • Coudronniere N, Villalba M, Englund N, Altman A. NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta. Proc Natl Acad Sci USA 2000;97:3394-3399.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3394-3399
    • Coudronniere, N.1    Villalba, M.2    Englund, N.3    Altman, A.4
  • 106
    • 0034031401 scopus 로고    scopus 로고
    • Protein kinase C-theta participates in NF-kappaB activation induced by CD3-CD28 costimulation through selective activation of IkappaB kinase beta
    • Lin X, O'Mahony A, Mu Y, Geleziunas R, Greene WC. Protein kinase C-theta participates in NF-kappaB activation induced by CD3-CD28 costimulation through selective activation of IkappaB kinase beta. Mol Cell Biol 2000;20:2933-2940.
    • (2000) Mol Cell Biol , vol.20 , pp. 2933-2940
    • Lin, X.1    O'Mahony, A.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 107
    • 18844473151 scopus 로고    scopus 로고
    • PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes
    • Sun Z, et al. PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes. Nature 2000;404:402-407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1
  • 108
    • 0035943657 scopus 로고    scopus 로고
    • Complex formation and cooperation of protein kinase C theta and Akt1/protein kinase B alpha in the NF-kappa B transactivation cascade in Jurkat T cells
    • Bauer B, et al. Complex formation and cooperation of protein kinase C theta and Akt1/protein kinase B alpha in the NF-kappa B transactivation cascade in Jurkat T cells. J Biol Chem 2001;276:31627-31634.
    • (2001) J Biol Chem , vol.276 , pp. 31627-31634
    • Bauer, B.1
  • 109
    • 0031012266 scopus 로고    scopus 로고
    • Selective modulation of protein kinase C-theta during T-cell activation
    • Monks CR, Kupfer H, Tamir I, Barlow A, Kupfer A. Selective modulation of protein kinase C-theta during T-cell activation. Nature 1997;385:83-86.
    • (1997) Nature , vol.385 , pp. 83-86
    • Monks, C.R.1    Kupfer, H.2    Tamir, I.3    Barlow, A.4    Kupfer, A.5
  • 110
    • 0037092038 scopus 로고    scopus 로고
    • Translocation of PKC [theta] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C
    • Villalba M, et al. Translocation of PKC [theta] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C. J Cell Biol 2002;157:253-263.
    • (2002) J Cell Biol , vol.157 , pp. 253-263
    • Villalba, M.1
  • 111
    • 0028911139 scopus 로고
    • Analysis of the role of protein kinase C-alpha, -epsilon, and -zeta in T cell activation
    • Genot EM, Parker PJ, Cantrell DA. Analysis of the role of protein kinase C-alpha, -epsilon, and -zeta in T cell activation. J Biol Chem 1995;270:9833-9839.
    • (1995) J Biol Chem , vol.270 , pp. 9833-9839
    • Genot, E.M.1    Parker, P.J.2    Cantrell, D.A.3
  • 112
    • 0036190970 scopus 로고
    • Role of glycogen synthase kinase-3 in cancer: Regulation by Wnts and other signaling pathways
    • Manoukian AS, Woodgett JR. Role of glycogen synthase kinase-3 in cancer: regulation by Wnts and other signaling pathways. Adv Cancer Res 1902;84:203-229.
    • (1902) Adv Cancer Res , vol.84 , pp. 203-229
    • Manoukian, A.S.1    Woodgett, J.R.2
  • 114
    • 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
  • 115
    • 0033026520 scopus 로고    scopus 로고
    • Tcf-1-mediated transcription in T lymphocytes, differential role for glycogen synthase kinase-3 in fibroblasts and T cells
    • Staal FJ, Burgering BM, van de Wetering M, Clevers HC. Tcf-1-mediated transcription in T lymphocytes, differential role for glycogen synthase kinase-3 in fibroblasts and T cells. Int Immunol 1999;11:317-323.
    • (1999) Int Immunol , vol.11 , pp. 317-323
    • Staal, F.J.1    Burgering, B.M.2    Van De Wetering, M.3    Clevers, H.C.4
  • 116
    • 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 Natl Acad Sci USA 2002;99:11796-11801.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11796-11801
    • Diehn, M.1
  • 117
    • 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
  • 118
    • 0036007421 scopus 로고    scopus 로고
    • Regulation of cell size in growth, development and human disease: PI3K, PKB and S6K
    • Kozma SC, Thomas G. Regulation of cell size in growth, development and human disease: PI3K, PKB and S6K. BioEssays 2002;24:65-71.
    • (2002) BioEssays , vol.24 , pp. 65-71
    • Kozma, S.C.1    Thomas, G.2
  • 120
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras AC, Raught B, Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 1999;68:913-963.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 121
    • 0033000334 scopus 로고    scopus 로고
    • p 70 (s6k) integrates phosphatidylinositol 3-kinase and rapamycin-regulated signals for E2F regulation in T lymphocytes
    • Brennan P, Babbage JW, Thomas G, Cantrell D. p 70 (s6k) integrates phosphatidylinositol 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
  • 122
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn GJ, Williams J, Sabers C, Wiederrecht G, Lawrence JCJ, Abraham RT. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J 1996;15:5256-5267.
    • (1996) EMBO J , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence, J.C.J.5    Abraham, R.T.6
  • 123
    • 0034234924 scopus 로고    scopus 로고
    • A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells
    • Sekulic A, et al. A direct linkage between the phosphoinositide 3-kinase-AKT signaling pathway and the mammalian target of rapamycin in mitogen-stimulated and transformed cells. Cancer Res 2000;60:3504-3513.
    • (2000) Cancer Res , vol.60 , pp. 3504-3513
    • Sekulic, A.1
  • 124
    • 0037059760 scopus 로고    scopus 로고
    • A new role for the p85-phosphatidylinositol 3-kinase regulatory subunit linking FRAP to p70 S6 kinase activation
    • Gonzalez-Garcia A, et al. A new role for the p85-phosphatidylinositol 3-kinase regulatory subunit linking FRAP to p70 S6 kinase activation. J Biol Chem 2002;277:1500-1508.
    • (2002) J Biol Chem , vol.277 , pp. 1500-1508
    • Gonzalez-Garcia, A.1
  • 125
    • 0030921302 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in NFAT activation in T cells
    • Jascur T, Gilman J, Mustelin T. Involvement of phosphatidylinositol 3-kinase in NFAT activation in T cells. J Biol Chem 1997;272:14483-14488.
    • (1997) J Biol Chem , vol.272 , pp. 14483-14488
    • Jascur, T.1    Gilman, J.2    Mustelin, T.3
  • 126
    • 0033597440 scopus 로고    scopus 로고
    • Requirement for Tec kinases Rlk and Itk in T cell receptor signaling and immunity
    • Schaeffer EM, et al. Requirement for Tec kinases Rlk and Itk in T cell receptor signaling and immunity. Science 1999;284:638-641.
    • (1999) Science , vol.284 , pp. 638-641
    • Schaeffer, E.M.1
  • 127
    • 0034046180 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton
    • Acuto O, Cantrell D. T cell activation and the cytoskeleton. Annu Rev Immunol 2000;18:165-184.
    • (2000) Annu Rev Immunol , vol.18 , pp. 165-184
    • Acuto, O.1    Cantrell, D.2
  • 128
    • 0036631548 scopus 로고    scopus 로고
    • VAV proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner M, Billadeau DD. VAV proteins as signal integrators for multi-subunit immune-recognition receptors. Nat Rev Immunol 2002;2:476-486.
    • (2002) Nat Rev Immunol , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 129
    • 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
  • 130
    • 0031830195 scopus 로고    scopus 로고
    • Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase gamma, a Rac guanosine exchange factor, and Rac
    • Ma AD, Metjian A, Bagrodia S, Taylor S, Abrams CS. Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase gamma, a Rac guanosine exchange factor, and Rac. Mol Cell Biol 1998;18:4744-4751.
    • (1998) Mol Cell Biol , vol.18 , pp. 4744-4751
    • Ma, A.D.1    Metjian, A.2    Bagrodia, S.3    Taylor, S.4    Abrams, C.S.5
  • 131
    • 0034685772 scopus 로고    scopus 로고
    • Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding
    • Das B, et al. Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding. J Biol Chem 2000;275:15074-15081.
    • (2000) J Biol Chem , vol.275 , pp. 15074-15081
    • Das, B.1
  • 132
    • 0031936619 scopus 로고    scopus 로고
    • Signaling through CD5 activates a pathway involving phosphatidylinositol 3-kinase, Vav, and Rac1 in human mature T lymphocytes
    • Gringhuis SI, de Leij LF, Coffer PJ, Vellenga E. Signaling through CD5 activates a pathway involving phosphatidylinositol 3-kinase, Vav, and Rac1 in human mature T lymphocytes. Mol Cell Biol 1998;18:1725-1735.
    • (1998) Mol Cell Biol , vol.18 , pp. 1725-1735
    • Gringhuis, S.I.1    De Leij, L.F.2    Coffer, P.J.3    Vellenga, E.4
  • 133
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han J, et al. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 1998;279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1
  • 134
    • 0034598312 scopus 로고    scopus 로고
    • The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH(2)-terminal kinase 1
    • Arudchandran R, et al. The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH(2)-terminal kinase 1. J Exp Med 2000;191:47-60.
    • (2000) J Exp Med , vol.191 , pp. 47-60
    • Arudchandran, R.1
  • 135
    • 0034446569 scopus 로고    scopus 로고
    • Mutant T cell lines as model systems for the dissection of T cell antigen receptor signaling pathways
    • Abraham RT. Mutant T cell lines as model systems for the dissection of T cell antigen receptor signaling pathways. Immunol Res 2000;22:95-117.
    • (2000) Immunol Res , vol.22 , pp. 95-117
    • Abraham, R.T.1
  • 136
    • 0037029653 scopus 로고    scopus 로고
    • Vav1 transduces T cell receptor signals to the activation of phospholipase C-gammal via phosphoinositide 3-kinase-dependent and -independent pathways
    • Reynolds LF, et al. Vav1 transduces T cell receptor signals to the activation of phospholipase C-gammal via phosphoinositide 3-kinase-dependent and -independent pathways. J Exp Med 2002;195:1103-1114.
    • (2002) J Exp Med , vol.195 , pp. 1103-1114
    • Reynolds, L.F.1
  • 137
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase C gamma by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca M, Logan SK, Lehto VP, Baccante G, Lemmon MA, Schlessinger J. Activation of phospholipase C gamma by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J 1998;17:414-422.
    • (1998) EMBO J , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 139
    • 0035805484 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase facilitates antigen-stimulated Ca(2+) influx in RBL-2H3 mast cells via a phosphatidylinositol 3,4, 5-trisphosphate-sensitive Ca(2+) entry mechanism
    • Ching TT, Hsu AL, Johnson AJ, Chen CS. Phosphoinositide 3-kinase facilitates antigen-stimulated Ca(2+) influx in RBL-2H3 mast cells via a phosphatidylinositol 3,4, 5-trisphosphate-sensitive Ca(2+) entry mechanism. J Biol Chem 2001;276:14814-14820.
    • (2001) J Biol Chem , vol.276 , pp. 14814-14820
    • Ching, T.T.1    Hsu, A.L.2    Johnson, A.J.3    Chen, C.S.4
  • 140
    • 0033600848 scopus 로고    scopus 로고
    • SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity
    • Cuevas B, et al. SHP-1 regulates Lck-induced phosphatidylinositol 3-kinase phosphorylation and activity. J Biol Chem 1999;274:27583-27589.
    • (1999) J Biol Chem , vol.274 , pp. 27583-27589
    • Cuevas, B.1
  • 141
    • 0035895959 scopus 로고    scopus 로고
    • Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells
    • Fang D, Wang HY, Fang N, Altman Y, Elly C, Liu YC. Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. J Biol Chem 2001;276:4872-4878.
    • (2001) J Biol Chem , vol.276 , pp. 4872-4878
    • Fang, D.1    Wang, H.Y.2    Fang, N.3    Altman, Y.4    Elly, C.5    Liu, Y.C.6
  • 142
    • 0035555195 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells
    • Fang D, Liu YC. Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells. Nat Immunol 2001;2:870-875.
    • (2001) Nat Immunol , vol.2 , pp. 870-875
    • Fang, D.1    Liu, Y.C.2
  • 144
    • 0036201223 scopus 로고    scopus 로고
    • Signaling pathways of D3-phosphoinositide-binding kinases in T cells and their regulation by PTEN
    • Seminario MC, Wange RL. Signaling pathways of D3-phosphoinositide-binding kinases in T cells and their regulation by PTEN. Semin Immunol 2002;14:27-36.
    • (2002) Semin Immunol , vol.14 , pp. 27-36
    • Seminario, M.C.1    Wange, R.L.2
  • 145
    • 0036181869 scopus 로고    scopus 로고
    • PTEN the down side of PI 3-kinase signalling
    • Leslie NR, Downes CP. PTEN: the down side of PI 3-kinase signalling. Cell Signal 2002;14:285-295.
    • (2002) Cell Signal , vol.14 , pp. 285-295
    • Leslie, N.R.1    Downes, C.P.2
  • 146
    • 0034610982 scopus 로고    scopus 로고
    • A dual role for Src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity: Aberrant development and enhanced function of b lymphocytes in SHIP -/- mice
    • Helgason CD, et al. A dual role for Src homology 2 domain-containing inositol-5-phosphatase (SHIP) in immunity: aberrant development and enhanced function of b lymphocytes in SHIP -/- mice. J Exp Med 2000;191:781-794.
    • (2000) J Exp Med , vol.191 , pp. 781-794
    • Helgason, C.D.1
  • 147
    • 0032702790 scopus 로고    scopus 로고
    • CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP
    • Edmunds C, Parry RV, Burgess SJ, Reaves B, Ward SG. CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP. Eur J Immunol 1999;29:3507-3515.
    • (1999) Eur J Immunol , vol.29 , pp. 3507-3515
    • Edmunds, C.1    Parry, R.V.2    Burgess, S.J.3    Reaves, B.4    Ward, S.G.5
  • 148
    • 0036206130 scopus 로고    scopus 로고
    • Protean PTEN: Form and function
    • Waite KA, Eng C. Protean PTEN: form and function. Am J Hum Genet 2002;70:829-844.
    • (2002) Am J Hum Genet , vol.70 , pp. 829-844
    • Waite, K.A.1    Eng, C.2
  • 149
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li J, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 1997;275:1943-1947.
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1
  • 150
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T, Dixon JE. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 1998;273:13375-13378.
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 151
    • 0032506011 scopus 로고    scopus 로고
    • The lipid phosphatase activity of PTEN is critical for its tumor suppressor function
    • Myers MP, et al. The lipid phosphatase activity of PTEN is critical for its tumor suppressor function. Proc Natl Acad Sci USA 1998;95:13513-13518.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13513-13518
    • Myers, M.P.1
  • 152
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee JO, et al. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 1999;99:323-334.
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1
  • 153
    • 0033606767 scopus 로고    scopus 로고
    • Shc and FAK differentially regulate cell motility and directionality modulated by PTEN
    • Gu J, et al. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J Cell Biol 1999;146:389-403.
    • (1999) J Cell Biol , vol.146 , pp. 389-403
    • Gu, J.1
  • 154
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM. Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science 1998;280:1614-1617.
    • (1998) Science , vol.280 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.4    Parsons, R.5    Yamada, K.M.6
  • 155
    • 0033575287 scopus 로고    scopus 로고
    • PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway
    • Tamura M, Gu J, Danen EH, Takino T, Miyamoto S, Yamada KM. PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. J Biol Chem 1999;274:20693-20703.
    • (1999) J Biol Chem , vol.274 , pp. 20693-20703
    • Tamura, M.1    Gu, J.2    Danen, E.H.3    Takino, T.4    Miyamoto, S.5    Yamada, K.M.6
  • 157
  • 160
    • 0033946740 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail regulates protein stability and function
    • Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. Phosphorylation of the PTEN tail regulates protein stability and function. Mol Cell Biol 2000;20:5010-5018.
    • (2000) Mol Cell Biol , vol.20 , pp. 5010-5018
    • Vazquez, F.1    Ramaswamy, S.2    Nakamura, N.3    Sellers, W.R.4
  • 161
    • 0035394373 scopus 로고    scopus 로고
    • Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383
    • Tolkacheva T, Boddapati M, Sanfiz A, Tsuchida K, Kimmelman AC, Chan AM. Regulation of PTEN binding to MAGI-2 by two putative phosphorylation sites at threonine 382 and 383. Cancer Res 2001;61:4985-4989.
    • (2001) Cancer Res , vol.61 , pp. 4985-4989
    • Tolkacheva, T.1    Boddapati, M.2    Sanfiz, A.3    Tsuchida, K.4    Kimmelman, A.C.5    Chan, A.M.6
  • 162
    • 0036644058 scopus 로고    scopus 로고
    • Negative feedback regulation of the tumor suppressor PTEN by phosphoinositide-induced serine phosphorylation
    • Birle D, et al. Negative feedback regulation of the tumor suppressor PTEN by phosphoinositide-induced serine phosphorylation. J Immunol 2002;169:286-291.
    • (2002) J Immunol , vol.169 , pp. 286-291
    • Birle, D.1
  • 163
    • 0035966127 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex
    • Vazquez F, Grossman SR, Takahashi Y, Rokas MV, Nakamura N, Sellers WR. Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem 2001;276:48627-48630.
    • (2001) J Biol Chem , vol.276 , pp. 48627-48630
    • Vazquez, F.1    Grossman, S.R.2    Takahashi, Y.3    Rokas, M.V.4    Nakamura, N.5    Sellers, W.R.6
  • 164
    • 0035847102 scopus 로고    scopus 로고
    • The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation
    • Torres J, Pulido R. The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J Biol Chem 2001;276:993-998.
    • (2001) J Biol Chem , vol.276 , pp. 993-998
    • Torres, J.1    Pulido, R.2
  • 165
    • 0034647496 scopus 로고    scopus 로고
    • Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase
    • Wu Y, et al. Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J Biol Chem 2000;275:21477-21485.
    • (2000) J Biol Chem , vol.275 , pp. 21477-21485
    • Wu, Y.1
  • 166
    • 0034636038 scopus 로고    scopus 로고
    • Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2
    • Wu X, et al. Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2. Proc Natl Acad Sci USA 2000;97:4233-4238.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4233-4238
    • Wu, X.1
  • 168
    • 0036193746 scopus 로고    scopus 로고
    • Oxidants painting the cysteine chapel: Redox regulation of PTPs
    • Xu D, Rovira II, Finkel T. Oxidants painting the cysteine chapel: redox regulation of PTPs. Dev Cell 2002;2:251-252.
    • (2002) Dev Cell , vol.2 , pp. 251-252
    • Xu, D.1    Rovira, I.I.2    Finkel, T.3
  • 169
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee SG. Redox signaling: hydrogen peroxide as intracellular messenger. Exp Mol Med 1999;31:53-59.
    • (1999) Exp Mol Med , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 170
    • 0033563157 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of MMAC1/PTEN to ghoblastoma cells inhibits S phase entry by the recruitment of p27Kip1 into cyclin E/CDK2 complexes
    • Cheney IW, Neuteboom ST, Vaillancourt MT, Ramachandra M, Bookstein R. Adenovirus-mediated gene transfer of MMAC1/PTEN to ghoblastoma cells inhibits S phase entry by the recruitment of p27Kip1 into cyclin E/CDK2 complexes. Cancer Res 1999;59:2318-2323.
    • (1999) Cancer Res , vol.59 , pp. 2318-2323
    • Cheney, I.W.1    Neuteboom, S.T.2    Vaillancourt, M.T.3    Ramachandra, M.4    Bookstein, R.5
  • 171
    • 0033621797 scopus 로고    scopus 로고
    • Transcriptional activation of p21WAF1 by PTEN/MMAC1 tumor suppressor
    • Wu RC, Li X, Schonthal AH. Transcriptional activation of p21WAF1 by PTEN/MMAC1 tumor suppressor. Mol Cell Biochem 2000;203:59-71.
    • (2000) Mol Cell Biochem , vol.203 , pp. 59-71
    • Wu, R.C.1    Li, X.2    Schonthal, A.H.3
  • 172
    • 0033514509 scopus 로고    scopus 로고
    • Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway
    • Ramaswamy S, et al. Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway. Proc Natl Acad Sci USA 1999;96:2110-2115.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2110-2115
    • Ramaswamy, S.1
  • 173
    • 0036232754 scopus 로고    scopus 로고
    • The phosphatidylinositol phosphatase PTEN is under control of costimulation and regulates proliferation in human T cells
    • Schmidt-Weber CB, Wohlfahrt JG, Akdis CA, Blaser K. The phosphatidylinositol phosphatase PTEN is under control of costimulation and regulates proliferation in human T cells. Eur J Immunol 2002;32:1196-1204.
    • (2002) Eur J Immunol , vol.32 , pp. 1196-1204
    • Schmidt-Weber, C.B.1    Wohlfahrt, J.G.2    Akdis, C.A.3    Blaser, K.4
  • 174
    • 13144249184 scopus 로고    scopus 로고
    • High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice
    • Suzuki A, et al. High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice. Curr Biol 1998;8:1169-1178.
    • (1998) Curr Biol , vol.8 , pp. 1169-1178
    • Suzuki, A.1
  • 175
  • 176
    • 0034213075 scopus 로고    scopus 로고
    • The conserved phosphoinositide 3-kinase pathway determines heart size in mice
    • Shioi T, et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J 2000;19:2537-2548.
    • (2000) EMBO J , vol.19 , pp. 2537-2548
    • Shioi, T.1
  • 177
    • 18644372367 scopus 로고    scopus 로고
    • Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways
    • Crackower M, et al. Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways. Cell 2002;110:737.
    • (2002) Cell , vol.110 , pp. 737
    • Crackower, M.1
  • 178
    • 0037125980 scopus 로고    scopus 로고
    • Akt induces enhanced myocardial contractility and cell size in vivo in transgenic mice
    • Condorelli G, et al. Akt induces enhanced myocardial contractility and cell size in vivo in transgenic mice. Proc Natl Acad Sci USA 2002;99:12333-12338.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12333-12338
    • Condorelli, G.1
  • 179
    • 0035734381 scopus 로고    scopus 로고
    • Pten regulates neuronal soma size: A mouse model of Lhermitte-Duclos disease
    • Kwon CH, et al. Pten regulates neuronal soma size: a mouse model of Lhermitte-Duclos disease. Nat Genet 2001;29:404-411.
    • (2001) Nat Genet , vol.29 , pp. 404-411
    • Kwon, C.H.1
  • 180
    • 0035733762 scopus 로고    scopus 로고
    • Deletion of Pten in mouse brain causes seizures, ataxia and defects in soma size resembling Lhermitte-Duclos disease
    • Backman SA, et al. Deletion of Pten in mouse brain causes seizures, ataxia and defects in soma size resembling Lhermitte-Duclos disease. Nat Genet 2001;29:396-403.
    • (2001) Nat Genet , vol.29 , pp. 396-403
    • Backman, S.A.1
  • 181
    • 0035824396 scopus 로고    scopus 로고
    • Negative regulation of neural stem/progenitor cell proliferation by the Pten tumor suppressor gene in vivo
    • Groszer M, et al. Negative regulation of neural stem/progenitor cell proliferation by the Pten tumor suppressor gene in vivo. Science 2001;294:2186-2189.
    • (2001) Science , vol.294 , pp. 2186-2189
    • Groszer, M.1
  • 182
    • 0034921007 scopus 로고    scopus 로고
    • Tumor suppressor PTEN: Modulator of cell signaling, growth, migration and apoptosis
    • Yamada KM, Araki M. Tumor suppressor PTEN: modulator of cell signaling, growth, migration and apoptosis. J Cell Sci 2001;114:2375-2382.
    • (2001) J Cell Sci , vol.114 , pp. 2375-2382
    • Yamada, K.M.1    Araki, M.2
  • 183
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • Di Cristofano A, Pandolfi PP. The multiple roles of PTEN in tumor suppression. Cell 2000;100:387-390.
    • (2000) Cell , vol.100 , pp. 387-390
    • Di Cristofano, A.1    Pandolfi, P.P.2
  • 184
    • 0343183328 scopus 로고    scopus 로고
    • Genetic deletion of the Pten rumor suppressor gene promotes cell motility by activation of Rac1 and Cdc42 GTPases
    • Liliental J, et al. Genetic deletion of the Pten rumor suppressor gene promotes cell motility by activation of Rac1 and Cdc42 GTPases. Curr Biol 2000;10:401-404.
    • (2000) Curr Biol , vol.10 , pp. 401-404
    • Liliental, J.1
  • 185
    • 0033229893 scopus 로고    scopus 로고
    • The PTEN lipid phosphatase domain is not required to inhibit invasion of glioma cells
    • Maier D, et al. The PTEN lipid phosphatase domain is not required to inhibit invasion of glioma cells. Cancer Res 1999;59:5479-5482.
    • (1999) Cancer Res , vol.59 , pp. 5479-5482
    • Maier, D.1
  • 186
    • 0034919058 scopus 로고    scopus 로고
    • Itk/Emt: A link between T cell antigen receptor-mediated Ca2+ events and cytoskeletal reorganization
    • Tsoukas CD, Grasis JA, Ching KA, Kawakami Y, Kawakami T. Itk/Emt: a link between T cell antigen receptor-mediated Ca2+ events and cytoskeletal reorganization. Trends Immunol 2001;22:17-20.
    • (2001) Trends Immunol , vol.22 , pp. 17-20
    • Tsoukas, C.D.1    Grasis, J.A.2    Ching, K.A.3    Kawakami, Y.4    Kawakami, T.5
  • 187
    • 0037071837 scopus 로고    scopus 로고
    • The attraction of lipids
    • Tromans A. The attraction of lipids. Nature 2002;417:702.
    • (2002) Nature , vol.417 , pp. 702
    • Tromans, A.1
  • 188
    • 0037205266 scopus 로고    scopus 로고
    • PI 3-kinases and PTEN: How opposites chemoattract
    • Comer FI, Parent CA. PI 3-kinases and PTEN: how opposites chemoattract. Cell 2002;109:541-544.
    • (2002) Cell , vol.109 , pp. 541-544
    • Comer, F.I.1    Parent, C.A.2
  • 189
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto S, Meili R, Lee S, Parry L, Firtel RA. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 2002;109:611-623.
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 190
    • 0037205230 scopus 로고    scopus 로고
    • Tumor suppressor PTEN mediates sensing of chemoattractant gradients
    • Iijima M, Devreotes P. Tumor suppressor PTEN mediates sensing of chemoattractant gradients. Cell 2002;109:599-610.
    • (2002) Cell , vol.109 , pp. 599-610
    • Iijima, M.1    Devreotes, P.2
  • 191
    • 0036644183 scopus 로고    scopus 로고
    • Disruption of a single Pten allele augments the chemotactic response of B lymphocytes to stromal cell-derived factor-1
    • Fox JA, Ung K, Tanlimco SG, Jirik FR. Disruption of a single Pten allele augments the chemotactic response of B lymphocytes to stromal cell-derived factor-1. J Immunol 2002;169:49-54.
    • (2002) J Immunol , vol.169 , pp. 49-54
    • Fox, J.A.1    Ung, K.2    Tanlimco, S.G.3    Jirik, F.R.4
  • 192
    • 0034995242 scopus 로고    scopus 로고
    • T cell-specific loss of Pten leads to defects in central and peripheral tolerance
    • Suzuki A, et al. T cell-specific loss of Pten leads to defects in central and peripheral tolerance. Immunity 2001;14:523-534.
    • (2001) Immunity , vol.14 , pp. 523-534
    • Suzuki, A.1
  • 193
    • 0032740314 scopus 로고    scopus 로고
    • Commitment to the CD4 lineage mediated by extracellular signal-related kinase mitogen-activated protein kinase and lck signaling
    • Sharp LL, Hedrick SM. Commitment to the CD4 lineage mediated by extracellular signal-related kinase mitogen-activated protein kinase and lck signaling. J Immunol 1999;163:6598-6605.
    • (1999) J Immunol , vol.163 , pp. 6598-6605
    • Sharp, L.L.1    Hedrick, S.M.2
  • 196
    • 0343621512 scopus 로고    scopus 로고
    • The tumor suppressor PTEN regulates T cell surviral and antigen receptor signaling by acting as a phosphatidylinositol 3-phosphatase
    • Wang X, Gjorloff-Wingren A, Saxena M, Pathan N, Reed JC, Mustelin T. The tumor suppressor PTEN regulates T cell surviral and antigen receptor signaling by acting as a phosphatidylinositol 3-phosphatase. J Immunol 2000;164:1934-1939.
    • (2000) J Immunol , vol.164 , pp. 1934-1939
    • Wang, X.1    Gjorloff-Wingren, A.2    Saxena, M.3    Pathan, N.4    Reed, J.C.5    Mustelin, T.6
  • 197
    • 0017702412 scopus 로고
    • Characterization of EBV-genome negative 'null' and 'T' cell lines derived from children with acute lymphoblastic leukemia and leukemic transformed non-Hodgkin lymphoma
    • Schneider U, Schwenk HU, Bornkamm G. Characterization of EBV-genome negative 'null' and 'T' cell lines derived from children with acute lymphoblastic leukemia and leukemic transformed non-Hodgkin lymphoma. Int J Cancer 1977;19:621-626.
    • (1977) Int J Cancer , vol.19 , pp. 621-626
    • Schneider, U.1    Schwenk, H.U.2    Bornkamm, G.3
  • 198
    • 0035991823 scopus 로고    scopus 로고
    • The inducible expression of the tumor suppressor gene PTEN promotes apoptosis and decreases cell size by inhibiting the PI3K/Akt pathway in Jurkat T cells
    • Xu Z, Stokoe D, Kane LP, Weiss A. The inducible expression of the tumor suppressor gene PTEN promotes apoptosis and decreases cell size by inhibiting the PI3K/Akt pathway in Jurkat T cells. Cell Growth Differ 2002;13:285-296.
    • (2002) Cell Growth Differ , vol.13 , pp. 285-296
    • Xu, Z.1    Stokoe, D.2    Kane, L.P.3    Weiss, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.