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Volumn 3, Issue 4, 2003, Pages 317-330

PI3K in lymphocyte development, differentiation and activation

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL 3 KINASE; AGAMMAGLOBULINAEMIA TYROSINE KINASE; CD28 ANTIGEN; PROTEIN TYROSINE KINASE;

EID: 0038549067     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1056     Document Type: Review
Times cited : (668)

References (151)
  • 1
    • 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. 70, 535-602 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 3
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection more than just a road to PKB
    • Vanhaesebroeck, B. & Alessi, D. R. The PI3K-PDK1 connection more than just a road to PKB. Biochem. J. 346, 551-576 (2000).
    • (2000) Biochem. J. , vol.346 , pp. 551-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 4
    • 0037086001 scopus 로고    scopus 로고
    • 3 levels: Viability of flies lacking PTEN restored by a PH-domain mutation in Akt/PKB
    • 3 levels: viability of flies lacking PTEN restored by a PH-domain mutation in Akt/PKB. Science 295, 2088-2091 (2002).
    • (2002) Science , vol.295 , pp. 2088-2091
    • Stocker, H.1
  • 5
    • 0034092567 scopus 로고    scopus 로고
    • Tec-family kinases in lymphocyte signaling and function
    • Schaeffer, E. M. & Schwartzberg, P. L. Tec-family kinases in lymphocyte signaling and function. Curr. Opin. Immunol. 12, 282-288 (2000).
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 282-288
    • Schaeffer, E.M.1    Schwartzberg, P.L.2
  • 7
    • 0035451761 scopus 로고    scopus 로고
    • PI3-K and T-cell activation: Limitations of T-leukemic cell lines as signaling models
    • Astoul, E., Edmunds, C., Cantrell, D. A. & Ward, S. G. PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models. Trends Immunol. 22, 490-496 (2001).
    • (2001) Trends Immunol. , vol.22 , pp. 490-496
    • Astoul, E.1    Edmunds, C.2    Cantrell, D.A.3    Ward, S.G.4
  • 8
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-triphosphate in neutrophil responses
    • Arcaro, A. & Wymann, M. P. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-triphosphate in neutrophil responses. Biochem J. 296, 297-301 (1993).
    • (1993) Biochem J. , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 9
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., Matter, W. F., Hui, K. Y. & Brown, R. F. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269, 5241-5248 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 11
    • 0024315482 scopus 로고
    • Acute pathological effects on rats of orally administered wortmannin-containing preparations and purified wortmannin from Fusarium oxysporum
    • Gunther, R., Abbas, H. K. & Mirocha, C. J. Acute pathological effects on rats of orally administered wortmannin-containing preparations and purified wortmannin from Fusarium oxysporum. Food Chem. Toxicol. 27, 173-179 (1989).
    • (1989) Food Chem. Toxicol. , vol.27 , pp. 173-179
    • Gunther, R.1    Abbas, H.K.2    Mirocha, C.J.3
  • 12
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B-cell development and proliferation in absence of phosphoinositide 3-kinase p85α
    • Fruman, D. A. et al. Impaired B-cell development and proliferation in absence of phosphoinositide 3-kinase p85α. Science 283, 393-397 (1999).
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1
  • 13
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85α subunit of phosphoinositide 3-kinase
    • Suzuki, H. et al. Xid-like immunodeficiency in mice with disruption of the p85α subunit of phosphoinositide 3-kinase. Science 283, 390-392 (1999). References 12 and 13 were the first to report an Xid-like phenotype of p85α-deficient mice.
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1
  • 14
    • 0031887249 scopus 로고    scopus 로고
    • Regulation of the p85/p110 phosphatidylinositol 3′-kinase: Stabilization and inhibition of the p110α catalytic subunit by the p 85 regulatory subunit
    • Yu, J. et al. Regulation of the p85/p110 phosphatidylinositol 3′-kinase: stabilization and inhibition of the p110α catalytic subunit by the p85 regulatory subunit. Mol. Cell. Biol. 18, 1379-1387 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1379-1387
    • Yu, J.1
  • 15
    • 0033621888 scopus 로고    scopus 로고
    • Impaired kit- but not FcεRI-initiated mast-cell activation in the absence of phosphoinositide 3-kinase p85α gene products
    • Lu-Kuo, J. M., Fruman, D. A., Joyal, D. M., Cantley, L. C. & Katz, H. R. Impaired kit- but not FcεRI-initiated mast-cell activation in the absence of phosphoinositide 3-kinase p85α gene products. J. Biol. Chem. 275, 6022-6029 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 6022-6029
    • Lu-Kuo, J.M.1    Fruman, D.A.2    Joyal, D.M.3    Cantley, L.C.4    Katz, H.R.5
  • 16
    • 0032909703 scopus 로고    scopus 로고
    • Increased insulin sensitivity and hypoglycaemia in mice lacking the p85α subunit of phosphoinositide 3-kinase
    • Terauchi, Y. et al. Increased insulin sensitivity and hypoglycaemia in mice lacking the p85α subunit of phosphoinositide 3-kinase. Nature Genet 21, 230-235 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 230-235
    • Terauchi, Y.1
  • 17
    • 0033757592 scopus 로고    scopus 로고
    • Hypoglycaemia, liver necrosis and perinatal death in mice lacking all isoforms of phosphoinositide 3-kinase p85α
    • Fruman, D. A. et al. Hypoglycaemia, liver necrosis and perinatal death in mice lacking all isoforms of phosphoinositide 3-kinase p85α. Nature Genet. 26, 379-382 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 379-382
    • Fruman, D.A.1
  • 18
    • 0036143774 scopus 로고    scopus 로고
    • Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival
    • Ueki, K. et al. Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival. Mol. Cell Biol. 22, 965-977 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 965-977
    • Ueki, K.1
  • 19
    • 0037039317 scopus 로고    scopus 로고
    • Increased insulin sensitivity in mice lacking p85β subunit of phosphoinositide 3-kinase
    • Ueki, K. et al. Increased insulin sensitivity in mice lacking p85β subunit of phosphoinositide 3-kinase. Proc. Natl Acad. Sci. USA 99, 419-424 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 419-424
    • Ueki, K.1
  • 20
    • 0034676001 scopus 로고    scopus 로고
    • Role of the PI3K regulatory subunit in the control of actin organization and cell migration
    • Jimenez, C. et al. Role of the PI3K regulatory subunit in the control of actin organization and cell migration. J. Cell. Biol. 151, 249-262 (2000).
    • (2000) J. Cell. Biol. , vol.151 , pp. 249-262
    • Jimenez, C.1
  • 21
    • 0037059827 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase p85 adaptor function in T cells. Co-stimulation and regulation of cytokine transcription independent of associated p110
    • Kang, H., Schneider, H. & Rudd, C. E. Phosphatidylinositol 3-kinase p85 adaptor function in T cells. Co-stimulation and regulation of cytokine transcription independent of associated p110. J. Biol. Chem. 277, 912-921 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 912-921
    • Kang, H.1    Schneider, H.2    Rudd, C.E.3
  • 22
    • 0033574429 scopus 로고    scopus 로고
    • Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110α subunit of phosphoinositide 3-kinase
    • Bi, L., Okabe, I., Bernard, D. J., Wynshaw-Boris, A. & Nussbaum, R. L. Proliferative defect and embryonic lethality in mice homozygous for a deletion in the p110α subunit of phosphoinositide 3-kinase. J. Biol. Chem. 274, 10963-10968 (1999).
    • (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
  • 23
    • 0036185944 scopus 로고    scopus 로고
    • Early embryonic lethality in mice deficient in the p110β catalytic subunit of PI3-kinase
    • Bi, L., Okabe, I., Bernard, D. J. & Nussbaum, R. L. Early embryonic lethality in mice deficient in the p110β catalytic subunit of PI3-kinase. Mamm. Genome 13, 169-172 (2002).
    • (2002) Mamm. Genome , vol.13 , pp. 169-172
    • Bi, L.1    Okabe, I.2    Bernard, D.J.3    Nussbaum, R.L.4
  • 24
    • 0037047590 scopus 로고    scopus 로고
    • Impaired B- and T-cell antigen receptor signaling in p110δ PI3-kinase mutant mice
    • Okkenhaug, K. et al. Impaired B- and T-cell antigen receptor signaling in p110δ PI3-kinase mutant mice. Science 297, 1031-1034 (2002).
    • (2002) Science , vol.297 , pp. 1031-1034
    • Okkenhaug, K.1
  • 25
    • 0037119630 scopus 로고    scopus 로고
    • A crucial role for the p110δ subunit of phosphatidylinositol 3-kinase in B-cell development and activation
    • Clayton, E. et al. A crucial role for the p110δ subunit of phosphatidylinositol 3-kinase in B-cell development and activation. J. Exp. Med. 196, 753-763 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 753-763
    • Clayton, E.1
  • 26
    • 0037695593 scopus 로고    scopus 로고
    • Essential, nonredundant role for the phosphoinositide 3-kinase p110δ in signaling by the B-cell receptor complex
    • Jou, S.-T. et al. Essential, nonredundant role for the phosphoinositide 3-kinase p110δ in signaling by the B-cell receptor complex. Mol. Cell. Biol. 22, 8580-8591 (2002). References 24-26 indicated a non-redundant role for p110δ in B-cell activation. Reference 24 also showed that p110δ is required for T-cell activation.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8580-8591
    • Jou, S.-T.1
  • 27
    • 0034635452 scopus 로고    scopus 로고
    • Central role for G protein-coupled phosphoinositide 3-kinase-γ in inflammation
    • Hirsch, E. et al. Central role for G protein-coupled phosphoinositide 3-kinase-γ in inflammation. Science 287, 1049-1053 (2000).
    • (2000) Science , vol.287 , pp. 1049-1053
    • Hirsch, E.1
  • 28
    • 0034635221 scopus 로고    scopus 로고
    • Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant-mediated signal transduction
    • Li, Z. et al. Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant-mediated signal transduction. Science 287, 1046-1049 (2000).
    • (2000) Science , vol.287 , pp. 1046-1049
    • Li, Z.1
  • 29
    • 0034635264 scopus 로고    scopus 로고
    • Function of PI3Kγ in thymocyte development. T-cell activation and neutrophil migration
    • Sasaki, T. et al. Function of PI3Kγ in thymocyte development. T-cell activation and neutrophil migration. Science 287, 1040-1046 (2000). References 27-29 showed a crucial role for p110γ in neutrophil and macrophage function. Sasaki et al. also presented evidence of reduced T-cell function in p110γ-deficient mice.
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1
  • 30
    • 0036200415 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase γ is an essential amplifier of mast-cell function
    • Laffargue, M. et al Phosphoinositide 3-kinase γ is an essential amplifier of mast-cell function. Immunity 16, 441-451 (2002).
    • (2002) Immunity , vol.16 , pp. 441-451
    • Laffargue, M.1
  • 31
    • 0035464192 scopus 로고    scopus 로고
    • Resistance to thromboembolism in PI3Kγ-deficient mice
    • Hirsch, E. et al. Resistance to thromboembolism in PI3Kγ-deficient mice. FASEB J. 15, 2019-2021 (2001).
    • (2001) FASEB J. , vol.15 , pp. 2019-2021
    • Hirsch, E.1
  • 32
    • 18644372367 scopus 로고    scopus 로고
    • Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways
    • Crackower, M. A. et al. Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways. Cell 110, 737-749 (2002).
    • (2002) Cell , vol.110 , pp. 737-749
    • Crackower, M.A.1
  • 33
    • 0036232933 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in immunity: Lessons from knockout mice
    • Sasaki, T., Suzuki, A., Sasaki, J. & Penninger, J. M. Phosphoinositide 3-kinases in immunity: lessons from knockout mice. J. Biochem. (Tokyo) 131, 495-501 (2002).
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 495-501
    • Sasaki, T.1    Suzuki, A.2    Sasaki, J.3    Penninger, J.M.4
  • 34
    • 0037326985 scopus 로고    scopus 로고
    • PI3K-signalling in B and T cells: Insights from gene-targeted mice
    • Okkenhaug, K. & Vanhaesebroeck, B. PI3K-signalling in B and T cells: insights from gene-targeted mice. Biochem. Soc. Trans. 31, 270-274 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 270-274
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 35
    • 0029064680 scopus 로고
    • Impairment of T-cell-dependent B-cell responses and B-1-cell development in CD19-deficient mice
    • Rickert, R. C., Rajewsky, K. & Roes, J. Impairment of T-cell-dependent B-cell responses and B-1-cell development in CD19-deficient mice. Nature 376, 352-355 (1995).
    • (1995) Nature , vol.376 , pp. 352-355
    • Rickert, R.C.1    Rajewsky, K.2    Roes, J.3
  • 36
    • 0033973585 scopus 로고    scopus 로고
    • Positive selection from newly formed to marginal-zone B cells depends on the rate of clonal production, CD19 and btk
    • Martin, F. & Kearney, J. F. Positive selection from newly formed to marginal-zone B cells depends on the rate of clonal production, CD19 and btk. Immunity 12, 39-49 (2000).
    • (2000) Immunity , vol.12 , pp. 39-49
    • Martin, F.1    Kearney, J.F.2
  • 37
    • 0027169534 scopus 로고
    • CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase
    • Tuveson, D. A., Carter, R. H., Soltoff, S. P. & Fearon, D. T. CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase. Science 260, 986-989 (1993).
    • (1993) Science , vol.260 , pp. 986-989
    • Tuveson, D.A.1    Carter, R.H.2    Soltoff, S.P.3    Fearon, D.T.4
  • 38
    • 0036797376 scopus 로고    scopus 로고
    • The physiologic role of CD19 cytoplasmic tyrosines
    • Wang, Y. et al. The physiologic role of CD19 cytoplasmic tyrosines. Immunity 17, 501-514 (2002). This study indicates that phosphoinositide 3-kinase (PI3K) is the main mediator of CD19 function.
    • (2002) Immunity , vol.17 , pp. 501-514
    • Wang, Y.1
  • 39
    • 0037222784 scopus 로고    scopus 로고
    • CD19 function in early and late B-cell development. I. Maintenance of follicular and marginal zone B cells requires CD19-dependent survival signals
    • Otero, D. C., Anzelon, A. N. & Rickert, R. C. CD19 function in early and late B-cell development. I. Maintenance of follicular and marginal zone B cells requires CD19-dependent survival signals. J. Immunol. 170, 73-83 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 73-83
    • Otero, D.C.1    Anzelon, A.N.2    Rickert, R.C.3
  • 40
    • 0034995180 scopus 로고    scopus 로고
    • The follicular versus marginal-zone B-lymphocyte cell-fate decision is regulated by Aiolos, Btk and CD21
    • Cariappa, A. et al. The follicular versus marginal-zone B-lymphocyte cell-fate decision is regulated by Aiolos, Btk and CD21. Immunity 14, 603-615 (2001).
    • (2001) Immunity , vol.14 , pp. 603-615
    • Cariappa, A.1
  • 41
    • 0026587743 scopus 로고
    • CD19: Lowering the threshold for antigen-receptor stimulation of B lymphocytes
    • Carter, R. H. & Fearon, D. T. CD19: lowering the threshold for antigen-receptor stimulation of B lymphocytes. Science 256, 105-107 (1992).
    • (1992) Science , vol.256 , pp. 105-107
    • Carter, R.H.1    Fearon, D.T.2
  • 42
    • 0036604292 scopus 로고    scopus 로고
    • Complementary roles for CD19 and Bruton's tyrosine kinase in B-lymphocyte signal transduction
    • Fujimoto, M. et al. Complementary roles for CD19 and Bruton's tyrosine kinase in B-lymphocyte signal transduction. J. Immunol. 168, 5465-5476 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 5465-5476
    • Fujimoto, M.1
  • 43
    • 0035846955 scopus 로고    scopus 로고
    • Cd19-dependent activation of Akt kinase in B-lymphocytes
    • Otero, D. C., Omori, S. A. & Rickert, R. C. Cd19-dependent activation of Akt kinase in B-lymphocytes. J. Biol. Chem. 276, 1474-1478 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 1474-1478
    • Otero, D.C.1    Omori, S.A.2    Rickert, R.C.3
  • 44
    • 0037195274 scopus 로고    scopus 로고
    • A PI3-kinase signaling code for insulin-triggered insertion of glucose transporters into the plasma membrane
    • Tengholm, A. & Meyer, T. A PI3-kinase signaling code for insulin-triggered insertion of glucose transporters into the plasma membrane. Curr. Biol. 12, 1871-1876 (2002). In this paper, Tengholm et al. used evanescent field microscopy to reveal a PI3K signalling code.
    • (2002) Curr. Biol. , vol.12 , pp. 1871-1876
    • Tengholm, A.1    Meyer, T.2
  • 45
    • 0037342166 scopus 로고    scopus 로고
    • Pten inactivation Alters peripheral B-lymphocyte fate and reconstitutes CD19 function
    • Anzelon, A. N., Wu, H. & Rickert, R. C. Pten inactivation Alters peripheral B-lymphocyte fate and reconstitutes CD19 function. Nature Immunol. 4, 287-294 (2003). PTEN deficiency rescues the CD19-deficient phenotype, providing additional evidence of a crucial role for PI3K in CD19 signalling. See also note added in proof.
    • (2003) Nature Immunol. , vol.4 , pp. 287-294
    • Anzelon, A.N.1    Wu, H.2    Rickert, R.C.3
  • 46
    • 0028002840 scopus 로고
    • Both phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase products are increased by antigen-receptor signaling in B cells
    • Gold, M. R. & Aebersold, R. Both phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase products are increased by antigen-receptor signaling in B cells. J. Immunol. 152, 42-50 (1994).
    • (1994) J. Immunol. , vol.152 , pp. 42-50
    • Gold, M.R.1    Aebersold, R.2
  • 47
    • 0033612540 scopus 로고    scopus 로고
    • The dynamics of protein kinase B regulation during B-cell antigen receptor engagement
    • Astoul, E., Watton, S. & Cantrell, D. The dynamics of protein kinase B regulation during B-cell antigen receptor engagement. J. Cell Biol. 145, 1511-1520 (1999). In references 47 and 77, green fluorescent protein (GFP)-PH domains were used to visualize PI3K signalling in B-cell lines. See also references 103 and 104 for similar work in transgenic T cells.
    • (1999) J. Cell. Biol. , vol.145 , pp. 1511-1520
    • Astoul, E.1    Watton, S.2    Cantrell, D.3
  • 48
    • 0034507903 scopus 로고    scopus 로고
    • BCAP the tyrosine kinase substrate that connects B-cell receptor to phosphoinositide 3-kinase activation
    • Okada, T., Maeda, A., Iwamatsu, A., Gotoh, K. & Kurosaki, T. BCAP: the tyrosine kinase substrate that connects B-cell receptor to phosphoinositide 3-kinase activation. Immunity 13, 817-827 (2000).
    • (2000) Immunity , vol.13 , pp. 817-827
    • Okada, T.1    Maeda, A.2    Iwamatsu, A.3    Gotoh, K.4    Kurosaki, T.5
  • 49
    • 0037079737 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of B-cell adaptor for phosphoinositide 3-kinase is required for Akt activation in response to CD19 engagement
    • Inabe, K. & Kurosaki, T. Tyrosine phosphorylation of B-cell adaptor for phosphoinositide 3-kinase is required for Akt activation in response to CD19 engagement. Blood 99, 584-589 (2002).
    • (2002) Blood , vol.99 , pp. 584-589
    • Inabe, K.1    Kurosaki, T.2
  • 50
    • 0037018096 scopus 로고    scopus 로고
    • Essential immunoregulatory role for BCAP in B-cell development and function
    • Yamazaki, T. et al. Essential immunoregulatory role for BCAP in B-cell development and function. J. Exp. Med. 195, 535-545 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 535-545
    • Yamazaki, T.1
  • 51
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI3-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 279, 558-560 (1998).
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1
  • 52
    • 0037148505 scopus 로고    scopus 로고
    • Vav3 modulates B-cell receptor responses by regulating phosphoinositide 3-kinase activation
    • Inabe, K. et al. Vav3 modulates B-cell receptor responses by regulating phosphoinositide 3-kinase activation. J. Exp. Med. 195, 189-200 (2002). This paper indicates that VAV acts upstream, rather than downstream, of the PI3K signalling pathway.
    • (2002) J. Exp. Med. , vol.195 , pp. 189-200
    • Inabe, K.1
  • 53
    • 0037341617 scopus 로고    scopus 로고
    • PI3K and Btk differentially regulate B-cell antigen receptor-mediated signal transduction
    • Suzuki, H. et al. PI3K and Btk differentially regulate B-cell antigen receptor-mediated signal transduction. Nature Immunol. 4, 280-286 (2003). The authors of this paper propose that BTK acts in a pathway parallel to PI3K, rather than downstream of PI3K as was previously assumed. This is a provocative, but highly controversial, issue.
    • (2003) Nature Immunol. , vol.4 , pp. 280-286
    • Suzuki, H.1
  • 55
    • 0032147181 scopus 로고    scopus 로고
    • Btk function in B-cell development and response
    • Satterthwaite, A. B., Li, Z. & Witte, O. N. Btk function in B-cell development and response. Semin. Immunol. 10, 309-316 (1998).
    • (1998) Semin. Immunol. , vol.10 , pp. 309-316
    • Satterthwaite, A.B.1    Li, Z.2    Witte, O.N.3
  • 56
    • 0033812082 scopus 로고    scopus 로고
    • Regulation of B-cell activation and differentiation by the phosphatidylinositol 3-kinase and phospholipase Cγ pathway
    • Marshall, A. J., Niiro, H., Yun, T. J. & Clark, E. A. Regulation of B-cell activation and differentiation by the phosphatidylinositol 3-kinase and phospholipase Cγ pathway. Immunol. Rev. 176, 30-46 (2000).
    • (2000) Immunol. Rev. , vol.176 , pp. 30-46
    • Marshall, A.J.1    Niiro, H.2    Yun, T.J.3    Clark, E.A.4
  • 57
    • 0032503687 scopus 로고    scopus 로고
    • 3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • 3: a regulatory nexus between tyrosine kinases and sustained calcium signals. Cell 94, 5-8 (1998).
    • (1998) Cell , vol.94 , pp. 5-8
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 58
    • 0030038840 scopus 로고    scopus 로고
    • Activation of BTK by a phosphorylation mechanism initiated by SRC-family kinases
    • Rawlings, D. J. et al. Activation of BTK by a phosphorylation mechanism initiated by SRC-family kinases. Science 271, 822-825 (1996).
    • (1996) Science , vol.271 , pp. 822-825
    • Rawlings, D.J.1
  • 59
    • 0030152357 scopus 로고    scopus 로고
    • Regulation of Btk function by a major autophosphorylation site within the SH3 domain
    • Park, H., et al. Regulation of Btk function by a major autophosphorylation site within the SH3 domain. Immunity 4, 515-525 (1996).
    • (1996) Immunity , vol.4 , pp. 515-525
    • Park, H.1
  • 60
    • 0033515021 scopus 로고    scopus 로고
    • In situ detection of activated Bruton's tyrosine kinase in the Ig signaling complex by phosphopeptide-specific monoclonal antibodies
    • Nisitani, S., Kato, R. M., Rawlings, D. J., Witte, O. N. & Wahl, M. I. In situ detection of activated Bruton's tyrosine kinase in the Ig signaling complex by phosphopeptide-specific monoclonal antibodies. Proc. Natl Acad. Sci. USA 96, 2221-2226 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2221-2226
    • Nisitani, S.1    Kato, R.M.2    Rawlings, D.J.3    Witte, O.N.4    Wahl, M.I.5
  • 61
    • 0037039320 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase and Bruton's tyrosine kinase regulate overlapping sets of genes in B lymphocytes
    • Fruman, D. A. et al. Phosphoinositide 3-kinase and Bruton's tyrosine kinase regulate overlapping sets of genes in B lymphocytes. Proc. Natl Acad. Sci. USA 99, 359-364 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 359-364
    • Fruman, D.A.1
  • 62
    • 0034678458 scopus 로고    scopus 로고
    • A novel B lymphocyte-associated adaptor protein, Bam32, regulates antigen receptor signaling downstream of phosphatidylinositol 3-kinase
    • Marshall, A. J. et al. A novel B lymphocyte-associated adaptor protein, Bam32, regulates antigen receptor signaling downstream of phosphatidylinositol 3-kinase. J. Exp. Med. 191, 1319-1332 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1319-1332
    • Marshall, A.J.1
  • 63
    • 0037033384 scopus 로고    scopus 로고
    • The B-lymphocyte adaptor molecule of 32 kD (Bam32) regulates B-cell antigen receptor signaling and cell survival
    • 3-binding protein (BAM32) that seems to regulate PLCγ.
    • (2002) J. Exp. Med. , vol.195 , pp. 143-149
    • Niiro, H.1    Maeda, A.2    Kurosaki, T.3    Clark, E.A.4
  • 64
    • 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, M. R. 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. 176, 47-68 (2000).
    • (2000) Immunol. Rev. , vol.176 , pp. 47-68
    • Gold, M.R.1
  • 65
    • 0036631548 scopus 로고    scopus 로고
    • VAV proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner, M. & Billadeau, D. D. VAV proteins as signal integrators for multi-subunit immune-recognition receptors. Nature Rev. Immunol. 2, 476-486 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 66
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Isakoff, S. J. et al. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17, 5374-5387 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5374-5387
    • Isakoff, S.J.1
  • 67
    • 0037131365 scopus 로고    scopus 로고
    • Critical role of the pleckstrin homology and cysteine-rich domains in Vav signaling and transforming activity
    • Palmby, T. R., Abe, K. & Der, C. J. Critical role of the pleckstrin homology and cysteine-rich domains in Vav signaling and transforming activity. J. Biol. Chem. 277, 39350-39359 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39350-39359
    • Palmby, T.R.1    Abe, K.2    Der, C.J.3
  • 68
    • 0037986310 scopus 로고    scopus 로고
    • Loss of PtdIns-3-P binding by the C-terminal Tiam-1 pleckstrin homology (PH) domain prevents in vivo Rac1 activation without affecting membrane targeting
    • 13 January (DOI: 10.1074/jbc M 211901200)
    • Baumeister, M. A. et al. Loss of PtdIns-3-P binding by the C-terminal Tiam-1 pleckstrin homology (PH) domain prevents in vivo Rac1 activation without affecting membrane targeting. J. Biol. Chem. 13 January 2003 (DOI: 10.1074/jbc M211901200).
    • (2003) J. Biol. Chem.
    • Baumeister, M.A.1
  • 69
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. & Ferguson, K. M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains Biochem. J. 350, 1-18 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 71
    • 0033531796 scopus 로고    scopus 로고
    • FcγRIIb modulation of surface immunoglobulin-induced Akt activation in murine B cells
    • Jacob, A., Cooney, D. Tridandapani, S., Kelley, T. & Coggeshall, K. M. FcγRIIb modulation of surface immunoglobulin-induced Akt activation in murine B cells J. Biol. Chem. 274, 13704-13710 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13704-13710
    • Jacob, A.1    Cooney, D.2    Tridandapani, S.3    Kelley, T.4    Coggeshall, K.M.5
  • 72
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland, S., Pearse, R. N., Kurosaki, T. & Ravetch, J. V. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8, 509-516 (1998).
    • (1998) Immunity , vol.8 , pp. 509-516
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 73
    • 0032055484 scopus 로고    scopus 로고
    • 3)/ Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals
    • 3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 17, 1961-1972 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1961-1972
    • Scharenberg, A.M.1
  • 74
    • 0032487425 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatase SHIP is a crucial negative regulator of B-cell antigen receptor signaling
    • Liu, Q. et al. The inositol polyphosphate 5-phosphatase SHIP is a crucial negative regulator of B-cell antigen receptor signaling. J. Exp. Med. 188, 1333-1342 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 1333-1342
    • Liu, Q.1
  • 75
    • 2642684541 scopus 로고    scopus 로고
    • Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span
    • Helgason, C. D. et al. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span. Genes Dev. 12, 1610-1620 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1610-1620
    • Helgason, C.D.1
  • 76
    • 0034194516 scopus 로고    scopus 로고
    • Differential regulation of B-cell development, activation, and death by the SRC homology 2 domain-containing 5′ inositol phosphatase (SHIP)
    • Brauweiler, A. et al. Differential regulation of B-cell development, activation, and death by the SRC homology 2 domain-containing 5′ inositol phosphatase (SHIP). J. Exp. Med. 191, 1545-1554 (2000). References 74-76 describe the autoimmune phenotype of SHIP-deficient mice, which is due, in part, to hyperactive B cells.
    • (2000) J. Exp. Med. , vol.191 , pp. 1545-1554
    • Brauweiler, A.1
  • 77
    • 0036310638 scopus 로고    scopus 로고
    • TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: Sustained plasma-membrane recruitment triggered by the B-cell antigen receptor
    • Marshall, A. J., Krahn, A. K., Ma, K., Duronio, V. & Hou, S. TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma-membrane recruitment triggered by the B-cell antigen receptor. Mol. Cell Biol. 22, 5479-5491 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5479-5491
    • Marshall, A.J.1    Krahn, A.K.2    Ma, K.3    Duronio, V.4    Hou, S.5
  • 78
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler, S. et al. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351, 19-31 (2000).
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1
  • 79
    • 0037191792 scopus 로고    scopus 로고
    • Self-recognition promotes the foreign antigen sensitivity of naive T lymphocytes
    • Stefanova, I., Dorfman, J. R. & Germain, R. N. Self-recognition promotes the foreign antigen sensitivity of naive T lymphocytes. Nature 420, 429-434 (2002).
    • (2002) Nature , vol.420 , pp. 429-434
    • Stefanova, I.1    Dorfman, J.R.2    Germain, R.N.3
  • 80
    • 0036885067 scopus 로고    scopus 로고
    • Decision making in the immune system: The lineage decisions of helper T cells
    • Murphy, K. M. & Reiner S. L. Decision making in the immune system: the lineage decisions of helper T cells. Nature Rev. Immunol. 2, 933-944 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 933-944
    • Murphy, K.M.1    Reiner, S.L.2
  • 82
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N. & Kupfer, A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82-86 (1998).
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 84
    • 0033712984 scopus 로고    scopus 로고
    • Xid-like phenotypes: A B-cell signalosome takes shape
    • Fruman, D. A. Satterthwaite, A. B. & Witte, O. N. Xid-like phenotypes: a B-cell signalosome takes shape. Immunity 13, 1-3 (2000).
    • (2000) Immunity , vol.13 , pp. 1-3
    • Fruman, D.A.1    Satterthwaite, A.B.2    Witte, O.N.3
  • 85
    • 0035554676 scopus 로고    scopus 로고
    • Regulatory T cells in the control of immune pathology
    • Maloy, K. J. & Powrie, F. Regulatory T cells in the control of immune pathology. Nature Immunol. 2, 816-822 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 816-822
    • Maloy, K.J.1    Powrie, F.2
  • 87
    • 0033213484 scopus 로고    scopus 로고
    • + T cells
    • + T cells. Immunity 11, 399-409 (1999).
    • (1999) Immunity , vol.11 , pp. 399-409
    • Fowell, D.J.1
  • 88
    • 0035194916 scopus 로고    scopus 로고
    • Mutation of Tec-family kinases alters T-helper cell differentiation
    • Schaeffer, E. M. et al. Mutation of Tec-family kinases alters T-helper cell differentiation. Nature Immunol. 2, 1183-1188 (2001). References 86-88 link PI3K to T-cell differentiation by showing involvement of the PI3K effectors AKT/PKB and ITK.
    • (2001) Nature Immunol. , vol.2 , pp. 1183-1188
    • Schaeffer, E.M.1
  • 89
    • 0027429761 scopus 로고
    • Ligation of CD28 receptor by B7 induces formation of D-3 phosphoinositides in T lymphocytes independently of T-cell receptor/CD3 activation
    • Ward, S. G., Westwick, J., Hall, N. D. & Sansom, D. M. Ligation of CD28 receptor by B7 induces formation of D-3 phosphoinositides in T lymphocytes independently of T-cell receptor/CD3 activation. Eur. J. Immunol. 23, 2572-2577 (1993).
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2572-2577
    • Ward, S.G.1    Westwick, J.2    Hall, N.D.3    Sansom, D.M.4
  • 90
    • 0036853106 scopus 로고    scopus 로고
    • Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse
    • Costello, P. S., Gallagher, M. & Cantrell, D. A. Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse. Nature Immunol. 3, 1082-1089 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 1082-1089
    • Costello, P.S.1    Gallagher, M.2    Cantrell, D.A.3
  • 91
    • 0036852243 scopus 로고    scopus 로고
    • Imaging antigen-induced PI3K activation in T cells
    • Harriague, J. & Bismuth, G. Imaging antigen-induced PI3K activation in T cells. Nature Immunol, 3, 1090-1096 (2002). In references 90 and 91, GFP-PH chimaeric proteins were used to visualize PI3K signalling in T cells, yielding some surprising results.
    • (2002) Nature Immunol. , vol.3 , pp. 1090-1096
    • Harriague, J.1    Bismuth, G.2
  • 92
    • 0035367805 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in T-lymphocyte activation
    • Ward, S. G. & Cantrell, D. A. Phosphoinositide 3-kinases in T-lymphocyte activation. Curr. Opin. Immunol. 13, 332-338 (2001).
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 332-338
    • Ward, S.G.1    Cantrell, D.A.2
  • 93
    • 0032479864 scopus 로고    scopus 로고
    • T-cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-ζ 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-ζ complex, recruits intracellular signaling proteins to the plasma membrane. J. Exp. Med. 188, 561-575 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 561-575
    • Bruyns, E.1
  • 94
    • 0032498231 scopus 로고    scopus 로고
    • LAT the ZAP-70 tyrosine kinase substrate that links T-cell receptor to cellular activation
    • Zhang, W., Sloan, L. J., Kitchen, J., Trible, R. P. & Samelson, L. E. LAT: the ZAP-70 tyrosine kinase substrate that links T-cell receptor to cellular activation. Cell 92, 83-92 (1998).
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan, L.J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 95
    • 0037029653 scopus 로고    scopus 로고
    • Vav1 transduces T-cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and -independent pathways
    • Reynolds, L. F. et al. Vav1 transduces T-cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and -independent pathways. J. Exp. Med. 195, 1103-1114 (2002). Reference 95 places VAV1 between T-cell receptor and PI3K signalling. Previous studies had placed VAV downstream, rather than upstream, of PI3K.
    • (2002) J. Exp. Med. , vol.195 , pp. 1103-1114
    • Reynolds, L.F.1
  • 96
    • 0030848134 scopus 로고    scopus 로고
    • Evidence for phosphatidylinositol 3-kinase-dependent T-cell antigen receptor (TCR) signal transduction
    • Exley, M. & Varticovski, L. Evidence for phosphatidylinositol 3-kinase-dependent T-cell antigen receptor (TCR) signal transduction. Mol. Immunol. 34, 221-226 (1997).
    • (1997) Mol. Immunol. , vol.34 , pp. 221-226
    • Exley, M.1    Varticovski, L.2
  • 97
    • 0032561341 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulation of T-cell receptor-mediated interleukin-2 gene expression in normal T cells
    • Eder, A. M., Dominguez, L., Franke, T. F. & Ashwell, J. D. Phosphoinositide 3-kinase regulation of T-cell receptor-mediated interleukin-2 gene expression in normal T cells. J. Biol. Chem. 273, 28025-28031 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28025-28031
    • Eder, A.M.1    Dominguez, L.2    Franke, T.F.3    Ashwell, J.D.4
  • 98
    • 0032543221 scopus 로고    scopus 로고
    • T-cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells
    • Liu, K. Q., Bunnell, S. C., Gurniak, C. B. & Berg, L. J. T-cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells. J. Exp. Med. 187, 1721-1727 (1998).
    • (1998) J. Exp. Med. , vol.187 , pp. 1721-1727
    • Liu, K.Q.1    Bunnell, S.C.2    Gurniak, C.B.3    Berg, L.J.4
  • 99
    • 0030852623 scopus 로고    scopus 로고
    • Itk negatively regulates induction of T-cell proliferation by CD28 costimulation
    • Liao, X. C. et al. Itk negatively regulates induction of T-cell proliferation by CD28 costimulation. J. Exp. Med. 186, 221-228 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 221-228
    • Liao, X.C.1
  • 100
    • 2542461503 scopus 로고    scopus 로고
    • Requirements for activation and RAFT localization of the T-lymphocyte kinase RIk/Txk
    • Chamorro, M. et al. Requirements for activation and RAFT localization of the T-lymphocyte kinase RIk/Txk. BMC Immunol. 2, 3 (2001).
    • (2001) BMC Immunol. , vol.2 , pp. 3
    • Chamorro, M.1
  • 101
    • 0033597440 scopus 로고    scopus 로고
    • Requirement for Tec kinases RIk and Itk in T-cell receptor signaling and immunity
    • Schaeffer, E. M. et al. Requirement for Tec kinases RIk and Itk in T-cell receptor signaling and immunity. Science 264, 638-641 (1999).
    • (1999) Science , vol.264 , pp. 638-641
    • Schaeffer, E.M.1
  • 103
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola, A., Schroeder, S., Sakakibara, Y. & Lanzavecchia, A T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 283, 680-682 (1999).
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 104
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T-cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. & Seed, B. Membrane compartmentation is required for efficient T-cell activation. Immunity 8, 723-732 (1998).
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 105
    • 0029965232 scopus 로고    scopus 로고
    • PI3-kinase: A pivotal pathway in T-cell activation?
    • Ward, S. G., June, C. H. & Olive, D. PI 3-kinase: a pivotal pathway in T-cell activation? Immunol. Today 17, 187-197 (1996).
    • (1996) Immunol. Today , vol.17 , pp. 187-197
    • Ward, S.G.1    June, C.H.2    Olive, D.3
  • 106
    • 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 369, 327-329 (1994).
    • (1994) Nature , vol.369 , pp. 327-329
    • Pages, F.1
  • 107
    • 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. Nature Immunol. 2, 325-332 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 325-332
    • Okkenhaug, K.1
  • 108
    • 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. 166, 3797-3803 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 3797-3803
    • Harada, Y.1
  • 109
    • 0035340150 scopus 로고    scopus 로고
    • L
    • L. J. Immunol. 166, 5331-5335 (2001). References 107-109 provide evidence of a crucial role for PI3K in transmitting survival signals, but not necessarily signals for the production of IL-2 or proliferation.
    • (2001) J. Immunol. , vol.166 , pp. 5331-5335
    • Burr, J.S.1
  • 110
    • 0034658320 scopus 로고    scopus 로고
    • L levels in vivo
    • L levels in vivo. J. Exp. Med. 191, 1721-1734 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1721-1734
    • Jones, R.G.1
  • 112
    • 0034686446 scopus 로고    scopus 로고
    • L restores cell survival, but not proliferation off effector differentiation, in CD28-deficient T lymphocytes
    • L restores cell survival, but not proliferation off effector differentiation, in CD28-deficient T lymphocytes. J. Exp. Med. 191, 2031-2038 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 2031-2038
    • Dahl, A.M.1
  • 113
    • 0031962106 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling
    • Kim, H. H., Tharayil, M. & Rudd, C. E. Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling. J. Biol. Chem. 273, 296-301 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 296-301
    • Kim, H.H.1    Tharayil, M.2    Rudd, C.E.3
  • 114
    • 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. 273, 21194-21202 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 21194-21202
    • Okkenhaug, K.1    Rottapel, R.2
  • 115
    • 0033517125 scopus 로고    scopus 로고
    • Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T-cell costimulation
    • Holdorf, A. D. et al. Proline residues in CD28 and the Src homology (SH) 3 domain of Lck are required for T-cell costimulation. J. Exp. Med. 190, 375-384 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 375-384
    • Holdorf, A.D.1
  • 116
    • 0031255110 scopus 로고    scopus 로고
    • The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T-cell costimulatory receptor CD28
    • Marengere, L. E. et al. The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T-cell costimulatory receptor CD28. J. Immunol. 159, 3220-3229 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 3220-3229
    • Marengere, L.E.1
  • 117
    • 0029931976 scopus 로고    scopus 로고
    • Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association
    • Pages, F. et al. Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association. J. Biol. Chem. 271, 9403-9409 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9403-9409
    • Pages, F.1
  • 118
    • 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, K. V. S. 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 91, 2834-2838 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2834-2838
    • Prasad, K.V.S.1
  • 119
    • 0028118512 scopus 로고
    • Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells
    • Truitt, K. E., Hicks, C. M. & Imboden, J. B. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells. J. Exp. Med. 179, 1071-1076 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 1071-1076
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 120
    • 0028802706 scopus 로고
    • Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation
    • Cai, Y. C. et al. Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation. Immunity 3, 417-426 (1995).
    • (1995) Immunity , vol.3 , pp. 417-426
    • Cai, Y.C.1
  • 121
    • 0036195934 scopus 로고    scopus 로고
    • Regulation of Lck activity by CD4 and CD28 in the immunological synapse
    • Holdorf, A. D. Lee, K. H., Burack, W. R., Allen, P. M. & Shaw, A. S. Regulation of Lck activity by CD4 and CD28 in the immunological synapse. Nature Immunol. 3, 259-264 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 259-264
    • Holdorf, A.D.1    Lee, K.H.2    Burack, W.R.3    Allen, P.M.4    Shaw, A.S.5
  • 122
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi, I. et al. Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653 (1997).
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1
  • 123
    • 0031029781 scopus 로고    scopus 로고
    • Regulatory intramolecular association in a tyrosine kinase of the Tec family
    • Andreotti, A. H., Bunnell, S. C., Feng, S., Berg, L. J. & Schreiber, S. L. Regulatory intramolecular association in a tyrosine kinase of the Tec family. Nature 385, 93-97 (1997).
    • (1997) Nature , vol.385 , pp. 93-97
    • Andreotti, A.H.1    Bunnell, S.C.2    Feng, S.3    Berg, L.J.4    Schreiber, S.L.5
  • 124
    • 0035660611 scopus 로고    scopus 로고
    • Requirement for CD28 co-stimulation is lower in SHP-1-deficient T cells
    • Sathish, J. G. et al. Requirement for CD28 co-stimulation is lower in SHP-1-deficient T cells. Eur. J. Immunol. 31, 3649-3658 (2001).
    • (2001) Eur. J. Immunol. , vol.31 , pp. 3649-3658
    • Sathish, J.G.1
  • 125
    • 0036069699 scopus 로고    scopus 로고
    • The CD28 signaling pathway regulates glucose metabolism
    • Frauwirth, K. A. et al. The CD28 signaling pathway regulates glucose metabolism. Immunity 16, 769-777 (2002).
    • (2002) Immunity , vol.16 , pp. 769-777
    • Frauwirth, K.A.1
  • 126
    • 0032904432 scopus 로고    scopus 로고
    • EPTEN a tumour suppressor that functions as a phospholipid phosphatase
    • Maehama, T. & Dixon, J. E. EPTEN: a tumour suppressor that functions as a phospholipid phosphatase. Trends Cell Biol. 9, 125-128 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 125-128
    • Maehama, T.1    Dixon, J.E.2
  • 127
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley, L. C. & Neel, B. G. New insights into tumor suppression PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/ AKT pathway. Proc. Natl Acad. Sci. USA 96, 4240-4245 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 129
    • 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 14, 523-534 (2001). References 128 and 129 show that unrestrained PI3K signalling as a consequence of reduced or absent PTEN expression by T cells leads to autoimmune disease and leukaemia.
    • (2001) Immunity , vol.14 , pp. 523-534
    • Suzuki, A.1
  • 130
    • 0034107671 scopus 로고    scopus 로고
    • Increased phosphoinositide 3-kinase activity induces a lymphoproliferative disorder and contributes to tumor generation in vivo
    • Borlado, L. R. et al. Increased phosphoinositide 3-kinase activity induces a lymphoproliferative disorder and contributes to tumor generation in vivo. FASEB J. 14, 895-903 (2000).
    • (2000) FASEB J. , vol.14 , pp. 895-903
    • Borlado, L.R.1
  • 131
    • 85047682727 scopus 로고    scopus 로고
    • FcγRIIB-mediated inhibition of T-cell receptor signal transduction involves the phosphorylation of SH2-containing inositol 5-phosphatase (SHIP), dephosphorylation of the linker of activated T-cells (LAT) and inhibition of calcium mobilization
    • Jensen, W. A. Marschner, S., Ott, V. L. & Cambier, J. C. FcγRIIB-mediated inhibition of T-cell receptor signal transduction involves the phosphorylation of SH2-containing inositol 5-phosphatase (SHIP), dephosphorylation of the linker of activated T-cells (LAT) and inhibition of calcium mobilization. Biochem. Soc Trans. 29, 840-846 (2001).
    • (2001) Biochem. Soc Trans. , vol.29 , pp. 840-846
    • Jensen, W.A.1    Marschner, S.2    Ott, V.L.3    Cambier, J.C.4
  • 132
    • 0037111475 scopus 로고    scopus 로고
    • Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors
    • Freeburn, R. W. et al. Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors. J. Immunol. 169, 5441-5450 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 5441-5450
    • Freeburn, R.W.1
  • 133
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman, M., Downes, C. P., Keeler, M., Keller, T. & Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332, 644-646 (1988).
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 134
    • 0033856462 scopus 로고    scopus 로고
    • PI3-kinase inhibition: A target for drug development?
    • Stein, R. C. & Waterfield, M. D. PI3-kinase inhibition: a target for drug development? Mol. Med. Today 6, 347-357 (2000).
    • (2000) Mol. Med. Today , vol.6 , pp. 347-357
    • Stein, R.C.1    Waterfield, M.D.2
  • 135
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase δ in neutrophil directional movement
    • Sadhu, C., Masinovsky, B., Dick, K., Sowell, C. G. & Staunton, D. E. Essential role of phosphoinositide 3-kinase δ in neutrophil directional movement. J. Immunol. 170, 2647-2654 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 2647-2654
    • Sadhu, C.1    Masinovsky, B.2    Dick, K.3    Sowell, C.G.4    Staunton, D.E.5
  • 136
    • 0037381002 scopus 로고    scopus 로고
    • Regulation of breast cancer cell chemotaxis by the phosphoinositide 3-kinase p1105
    • in the press
    • Sawyer, C. et al. Regulation of breast cancer cell chemotaxis by the phosphoinositide 3-kinase p1105. Cancer Res. (in the press).
    • Cancer Res.
    • Sawyer, C.1
  • 137
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., Cantley, L. C. & Carpenter, C. L. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270, 17656-17659 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 138
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng, Y., Bagrodia, S. & Cerione, R. A. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269, 18727-18730 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 139
    • 0028074316 scopus 로고
    • Phosphatidylinositol-3-OH kinase as a direct target of Ras
    • Rodriguez-Viciana, P. et al. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature 370, 527-532 (1994).
    • (1994) Nature , vol.370 , pp. 527-532
    • Rodriguez-Viciana, P.1
  • 140
    • 0030887632 scopus 로고    scopus 로고
    • The Gβγ sensitivity of a PI3K is dependent upon a tightly associated adaptor, p 101
    • Stephens, L. R. et al. The Gβγ sensitivity of a PI3K is dependent upon a tightly associated adaptor, p101. Cell 89, 105-114 (1997).
    • (1997) Cell , vol.89 , pp. 105-114
    • Stephens, L.R.1
  • 142
    • 0028036698 scopus 로고
    • Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1 and interleukin-4 stimulation
    • Myers, M. G. Jr et al. Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1 and interleukin-4 stimulation. J. Biol. Chem. 269, 28783-28789 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 28783-28789
    • Myers M.G., Jr.1
  • 143
    • 0034986036 scopus 로고    scopus 로고
    • Antigen-receptor cross-linking and lipopolysaccharide trigger distinct phosphainositide 3-kinase-dependent pathways to NF-κB activation in primary B cells
    • Bone, H. & Williams, N. A. Antigen-receptor cross-linking and lipopolysaccharide trigger distinct phosphainositide 3-kinase-dependent pathways to NF-κB activation in primary B cells. Int. Immunol. 13, 807-816 (2001).
    • (2001) Int. Immunol. , vol.13 , pp. 807-816
    • Bone, H.1    Williams, N.A.2
  • 144
    • 0034577944 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated NF-κB activation requires a Rac1-dependent pathway
    • Arbibe, L. et al. Toll-like receptor 2-mediated NF-κB activation requires a Rac1-dependent pathway. Nature Immunol. 1, 533-540 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 533-540
    • Arbibe, L.1
  • 145
    • 0034292331 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and NF-κB/Rel are at the divergence of CD40-mediated proliferation and survival pathways
    • Andjelic, S. et al. Phosphatidylinositol 3-kinase and NF-κB/ Rel are at the divergence of CD40-mediated proliferation and survival pathways. J. Immunol. 165, 3860-3867 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 3860-3867
    • Andjelic, S.1
  • 146
    • 0035839450 scopus 로고    scopus 로고
    • A positive regulatory role for Cbl-family proteins in tumor necrosis factor-related activation-induced cytokine (trance) and CD40L-mediated Akt activation
    • Arron, J. R. et al. A positive regulatory role for Cbl-family proteins in tumor necrosis factor-related activation-induced cytokine (trance) and CD40L-mediated Akt activation. J. Biol. Chem. 276, 30011-30017 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 30011-30017
    • Arron, J.R.1
  • 147
    • 0036584284 scopus 로고    scopus 로고
    • Regulation of B-cell signal transduction by adaptor proteins
    • Kurosaki, T. Regulation of B-cell signal transduction by adaptor proteins. Nature Rev. Immunol. 2, 354-363 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 354-363
    • Kurosaki, T.1
  • 148
    • 0033912699 scopus 로고    scopus 로고
    • The T-cell receptor regulates Akt (protein kinase B) via a pathway involving Rac 1 and phosphatidylinositide 3-kinase
    • Genot, E. M. et al. The T-cell receptor regulates Akt (protein kinase B) via a pathway involving Rac 1 and phosphatidylinositide 3-kinase Mol. Cell Biol. 20, 5469-5478 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5469-5478
    • Genot, E.M.1
  • 149
    • 0036679733 scopus 로고    scopus 로고
    • It's all Rel-ative: NF-κB and CD28 costimulation of T-cell activation
    • Kane, L. P., Lin, J. & Weiss. A It's all Rel-ative: NF-κB and CD28 costimulation of T-cell activation. Trends Immunol. 23, 413-420 (2002).
    • (2002) Trends Immunol. , vol.23 , pp. 413-420
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 151
    • 0037416216 scopus 로고    scopus 로고
    • Critical roles of Pten in B-cell homeostasis and immunoglobulin class switch recombination
    • Suzuki, A. et al. Critical roles of Pten in B-cell homeostasis and immunoglobulin class switch recombination. J. Exp. Med. 197, 657-667 (2003).
    • (2003) J. Exp. Med. , vol.197 , pp. 657-667
    • Suzuki, A.1


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