CD28-Mediated Costimulation in the Absence of Phosphatidylinositol 3-Kinase Association and Activation

REFERENCES

• Allison, J. P. 1994. CD28-B7 interactions in T-cell activation. Curr. Opin. Immunol. 6:414–419.
   PubMed Web of Science ®Google Scholar
• Aruffo, A., and B. Seed. 1987. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc. Natl. Acad. Sci. USA 84: 8573–8577.
   PubMed Web of Science ®Google Scholar
• Azuma, M., D. Ito, H. Yagita, K. Okumura, J. H. Phillips, L. L. Lanier, and C. Somoza. 1993. B70 antigen is a second ligand for CTLA-4 and CD28. Nature (London) 366:76–79.
   PubMed Web of Science ®Google Scholar
• Cantley, L. C., K. R. Auger, C. Carpenter, B. Duckworth, A. Graziani, R. Kapeller, and S. Soltoff. 1991. Oncogenes and signal transduction. Cell 64:281–302. (Erratum, 65:914 ff.)
   PubMed Web of Science ®Google Scholar
• Carraway, K. L., and L. C. Cantley. 1994. A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 78: 5–8.
   PubMed Web of Science ®Google Scholar
• Carter, R. H., and D. T. Fearon. 1992. CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. Science 256:105–107.
   PubMed Web of Science ®Google Scholar
• Chen, L., S. Ashe, W. A. Brady, I. Hellstrom, K. E. Hellstrom, J. A. Ledbetter, P. McGowan, and P. S. Linsley. 1992. Costimulation of antitumor immunity by the B7 counterreceptor for the T lymphocyte molecules CD28 and CTLA-4. Cell 71:1093–1102.
   PubMed Web of Science ®Google Scholar
• Clipstone, N. A., and G. R. Crabtree. 1992. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature (London) 357:695–697.
   PubMed Web of Science ®Google Scholar
• Durand, D. B., M. R. Bush, J. G. Morgan, A. Weiss, and G. R. Crabtree. 1987. A 275 basepair fragment at the 59 end of the interleukin 2 gene enhances expression from a heterologous promoter in response to signals from the T cell antigen receptor. J. Exp. Med. 165:395–407.
   PubMed Web of Science ®Google Scholar
• Fantl, W. J., J. A. Escobedo, G. A. Martin, C. W. Turck, M. del Rosario, F. McCormick, and L. T. Williams. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 69:413–423.
   PubMedGoogle Scholar
• Fraser, J. D., B. A. Irving, G. R. Crabtree, and A. Weiss. 1991. Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28. Science 251:313–316.
   PubMed Web of Science ®Google Scholar
• Fraser, J. D., and A. Weiss. 1992. Regulation of T-cell lymphokine gene transcription by the accessory molecule CD28. Mol. Cell. Biol. 12:4357–4363.
   PubMedGoogle Scholar
• Freeman, G. J., G. S. Gray, C. D. Gimmi, D. B. Lombard, L. J. Zhou, M. White, J. D. Fingeroth, J. G. Gribben, and L. M. Nadler. 1991. Structure, expression, and T cell costimulatory activity of the murine homologue of the human B lymphocyte activation antigen B7. J. Exp. Med. 174:625–631.
   PubMed Web of Science ®Google Scholar
• Freeman, G. J., J. G. Gribben, V. A. Boussiotis, J. W. Ng, V. A. J. Restivo, L. A. Lombard, G. S. Gray, and L. M. Nadler. 1993. Cloning of B7-2: a CTLA-4 counter-receptor that costimulates human T cell proliferation. Science 262:909–911.
   PubMed Web of Science ®Google Scholar
• Gross, J. A., T. St. John, and J. P. Allison. 1990. The murine homologue of the T lymphocyte antigen CD28: molecular cloning and cell surface expression. J. Immunol. 144:3201–3210.
   PubMed Web of Science ®Google Scholar
• Harding, F. A., J. G. McArthur, J. A. Gross, D. H. Raulet, and J. P. Allison. 1992. CD28-mediated signalling co-stimulates murine T cells and prevents induction of anergy in T-cell clones. Nature (London) 356:607–609.
   PubMed Web of Science ®Google Scholar
• Harper, K., C. Balzano, E. Rouvier, M. G. Mattei, M. F. Luciani, and P. Golstein. 1991. CTLA-4 and CD28 activated lymphocyte molecules are closely related in both mouse and human as to sequence, message expression, gene structure, and chromosomal location. J. Immunol. 147:1037–1044.
   PubMed Web of Science ®Google Scholar
• Joly, M., A. Kazlauskas, F. S. Fay, and S. Corvera. 1994. Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Science 263:684–687.
   PubMed Web of Science ®Google Scholar
• June, C. H., J. A. Bluestone, L. M. Nadler, and C. B. Thompson. 1994. The B7 and CD28 receptor families. Immunol. Today 15:321–331.
   PubMedGoogle Scholar
• June, C. H., J. A. Ledbetter, M. M. Gillespie, T. Lindsten, and C. B. Thompson. 1987. T-cell proliferation involving the CD28 pathway is associated with cyclosporine-resistant interleukin-2 gene expression. Mol. Cell. Biol. 7:4472–4481.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, A., and J. A. Cooper. 1989. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins. Cell 58:1121–1133.
   PubMedGoogle Scholar
• Kelly, K. L., and N. B. Ruderman. 1993. Insulin-stimulated phosphatidylino-sitol 3-kinase: association with a 185-kDa tyrosine-phosphorylated protein (IRS-1) and localization in a low density membrane vesicle. J. Biol. Chem. 268:4391–4398.
   PubMedGoogle Scholar
• Klippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. 1992. The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor. Mol. Cell. Biol. 12:1451–1459.
   PubMed Web of Science ®Google Scholar
• Klippel, A., J. A. Escobedo, M. Hirano, and L. T. Williams. 1994. The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity. Mol. Cell. Biol. 14:2675–2685.
   PubMedGoogle Scholar
• Kotani, K., K. Yonezawa, K. Hara, H. Ueda, Y. Kitamura, H. Sakaue, A. Ando, A. Chavanieu, B. Calas, and F. Grigorescu. 1994. Involvement of phosphoinositide 3-kinase in insulin- or IGF-1-induced membrane ruffling. EMBO J. 13:2313–2321.
   PubMedGoogle Scholar
• Lam, K., C. L. Carpenter, N. B. Ruderman, J. C. Friel, and K. L. Kelly. 1994. The phosphatidylinositol 3-kinase serine kinase phosphorylates IRS-1: stimulation by insulin and inhibition by wortmannin. J. Biol. Chem. 269:20648–20652.
   PubMed Web of Science ®Google Scholar
• Lenschow, D. J., A. I. Sperling, M. P. Cooke, G. Freeman, L. Rhee, D. C. Decker, G. Gray, L. M. Nadler, C. C. Goodnow, and J. A. Bluestone. 1994. Differential up-regulation of the B7-1 and B7-2 costimulatory molecules after Ig receptor engagement by antigen. J. Immunol. 153:1990–1997.
   PubMed Web of Science ®Google Scholar
• Lenschow, D. J., Y. Zeng, J. R. Thistlethwaite, A. Montag, W. Brady, M. G. Gibson, P. S. Linsley, and J. A. Bluestone. 1992. Long-term survival of xenogeneic pancreatic islet grafts induced by CTLA4lg. Science 257:789–792.
   PubMed Web of Science ®Google Scholar
• Lindstein, T., C. H. June, J. A. Ledbetter, G. Stella, and C. B. Thompson. 1989. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science 244:339–343.
   PubMed Web of Science ®Google Scholar
• Linsley, P. S., J. Bradshaw, M. Urnes, L. Grosmaire, and J. A. Ledbetter. 1993. CD28 engagement by B7/BB-1 induces transient down-regulation of CD28 synthesis and prolonged unresponsiveness to CD28 signaling. J. Im-munol. 150:3161–3169.
   PubMed Web of Science ®Google Scholar
• Linsley, P. S., W. Brady, L. Grosmaire, A. Aruffo, N. K. Damle, and J. A. Ledbetter. 1991. Binding of the B cell activation antigen B7 to CD28 co-stimulates T cell proliferation and interleukin 2 mRNA accumulation. J. Exp. Med. 173:721–730.
   PubMed Web of Science ®Google Scholar
• Linsley, P. S., P. M. Wallace, J. Johnson, M. G. Gibson, J. L. Greene, J. A. Ledbetter, C. Singh, and M. A. Tepper. 1992. Immunosuppression in vivo by a soluble form of the CTLA-4 T cell activation molecule. Science 257:792–795.
   PubMed Web of Science ®Google Scholar
• Littman, D. R., Y. Thomas, P. J. Maddon, L. Chess, and R. Axel. 1985. The isolation and sequence of the gene encoding T8: a molecule defining functional classes of T lymphocytes. Cell 40:237–246.
   PubMed Web of Science ®Google Scholar
• Lu, Y., C. A. Phillips, J. M. Bjorndahl, and J. M. Trevillyan. 1994. CD28 signal transduction: tyrosine phosphorylation and receptor association of phosphoinositide-3 kinase correlate with Ca(21)-independent costimulatory activity. Eur. J. Immunol. 24:2732–2739.
   PubMedGoogle Scholar
• Lu, Y., C. A. Phillips, J. M. Bjorndahl, and J. M. Trevillyan. 1995. Phos-phatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: studies with a selective inhibitor, wortmannin. Eur. J. Immunol. 25:533–537.
   PubMedGoogle Scholar
• Marengere, L. E., Z. Songyang, G. D. Gish, M. D. Schaller, J. T. Parsons, M. J. Stern, L. C. Cantley, and T. Pawson. 1994. SH2 domain specificity and activity modified by a single residue. Nature (London) 369:502–505.
   PubMed Web of Science ®Google Scholar
• Mosmann, T. 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65:55–63.
   PubMed Web of Science ®Google Scholar
• Okada, T., L. Sakuma, Y. Fukui, O. Hazeki, and M. Ui. 1994. Blockage of chemotactic peptide-induced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidylinositol 3-kinase. J. Biol. Chem. 269:3563–3567.
   PubMed Web of Science ®Google Scholar
• Pagès, F., M. Ragueneau, R. Rottapel, A. Truneh, J. Nunes, J. Imbert, and D. Olive. 1994. Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling. Nature 369:327–329. (Erratum, 370:157.)
   PubMed Web of Science ®Google Scholar
• Prasad, K. V., Y. C. Cai, M. Raab, B. Duckworth, L. Cantley, S. E. Shoelson, and C. E. Rudd. 1994. 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.
   PubMed Web of Science ®Google Scholar
• Schwartz, R. H. 1992. Costimulation of T lymphocytes: the role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy. Cell 71:1065–1068.
   PubMed Web of Science ®Google Scholar
• Secrist, J. P., L. A. Burns, L. Karnitz, G. A. Koretzky, and R. T. Abraham. 1993. Stimulatory effects of the protein tyrosine phosphatase inhibitor, per-vanadate, on T-cell activation events. J. Biol. Chem. 268:5886–5893.
   PubMed Web of Science ®Google Scholar
• Sethna, M. P., L. van Parjis, A. H. Sharpe, A. K. Abbas, and G. J. Freeman. 1994. A negative regulatory function of B7 revealed in B7-1 transgenic mice. Immunity 1:415–421.
   PubMedGoogle Scholar
• Shahinian, A., K. Pfeffer, K. P. Lee, T. M. Kundig, K. Kishihara, A. Wakeham, K. Kawai, P. S. Ohashi, C. B. Thompson, and T. W. Mak. 1993. Differential T cell costimulatory requirements in CD28-deficient mice. Science 261:609–612.
   PubMed Web of Science ®Google Scholar
• Stack, J. H., and S. D. Emr. 1994. Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities. J. Biol. Chem. 269:31552–31562.
   PubMed Web of Science ®Google Scholar
• Stein, P. H., J. D. Fraser, and A. Weiss. 1994. The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 39-kinase. Mol. Cell. Biol. 14:3392–3402.
   PubMedGoogle Scholar
• Thelen, M., M. P. Wymann, and H. Langen. 1994. Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes. Proc. Natl. Acad. Sci. USA 91:4960–4964.
   PubMed Web of Science ®Google Scholar
• Thompson, C. B., T. Lindsten, J. A. Ledbetter, S. L. Kunkel, H. A. Young, S. G. Emerson, J. M. Leiden, and C. H. June. 1989. CD28 activation pathway regulates the production of multiple T-cell-derived lymphokines/cytokines. Proc. Natl. Acad. Sci. USA 86:1333–1337.
   PubMed Web of Science ®Google Scholar
• Townsend, S. E., and J. P. Allison. 1993. Tumor rejection after direct co-stimulation of CD81 T cells by B7-transfected melanoma cells. Science 259:368–370.
   PubMed Web of Science ®Google Scholar
• Tuveson, D. A., R. H. Carter, S. P. Soltoff, and D. T. Fearon. 1993. CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase. Science 260:986–989.
   PubMed Web of Science ®Google Scholar
• Verweij, C. L., M. Geerts, and L. A. Aarden. 1991. Activation of interleukin-2 gene transcription via the T-cell surface molecule CD28 is mediated through an NF-κB-like response element. J. Biol. Chem. 266:14179–14182.
   PubMedGoogle Scholar
• Walunas, T. L., D. J. Lenschow, C. Y. Bakker, P. S. Linsley, G. J. Freeman, J. M. Green, C. B. Thompson, and J. A. Bluestone. 1994. CTLA-4 can function as a negative regulator of T cell activation. Immunity 1:405–413.
   PubMed Web of Science ®Google Scholar
• Ward, S. G., A. Wilson, L. Turner, J. Westwick, and D. M. Sansom. 1995. Inhibition of CD28-mediated T cell costimulation by the phosphoinositide 3-kinase inhibitor wortmannin. Eur. J. Immunol. 25:526–532.
   PubMedGoogle Scholar
• Weiss, A., and J. B. Imboden. 1987. Cell surface molecules and early events involved in human T lymphocyte activation. Adv. Immunol. 41:1–38.
   PubMed Web of Science ®Google Scholar
• Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263–274.
   PubMed Web of Science ®Google Scholar
• Weiss, A., B. Manger, and J. Imboden. 1986. Synergy between the T3/antigen receptor complex and Tp44 in the activation of human T cells. J. Immunol. 137:819–825.
   PubMed Web of Science ®Google Scholar
• Williams, T. M., D. M. Moolten, H. Makni, H. W. Kim, J. A. Kant, and M. Kamoun. 1992. CD28-stimulated IL-2 gene expression in Jurkat T cells occurs in part transcriptionally and is cyclosporine-A sensitive. J. Immunol. 148:2609–2616. (Erratum, 149:745.)
   PubMedGoogle Scholar
• Yeh, J. I., E. A. Gulve, L. Rameh, and M. J. Birnbaum. 1995. The effects of wortmannin on rat skeletal muscle: dissociation of signaling pathways for insulin- and contraction-activated hexose transport. J. Biol. Chem. 270:2107–2111.
   PubMedGoogle Scholar