CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP

European Journal of Immunology

Volumn 29, Issue 11, 1999, Pages 3507-3515

  Edmunds, Catherine ^a   Parry, Richard V ^a   Burgess, Steven J ^a   Reaves, Barbara ^b   Ward, Stephen G ^a,b  

^a UNIVERSITY OF BATH   (United Kingdom)

^b University of Bath   (United Kingdom)

Author keywords

CD28; SHIP; T lymphocyte

Indexed keywords

CD28 ANTIGEN; CD3 ANTIGEN; INOSITOL POLYPHOSPHATE; PHOSPHATASE;

ANIMAL CELL; ARTICLE; CELL MEMBRANE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME LOCALIZATION; HYBRIDOMA; IMMUNOPRECIPITATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; T LYMPHOCYTE;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ANIMALS; ANTIGENS, CD28; CATALYSIS; CHO CELLS; CRICETINAE; ENZYME ACTIVATION; GENE EXPRESSION; HUMANS; MICE; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PRECIPITIN TESTS; SRC HOMOLOGY DOMAINS; TUMOR CELLS, CULTURED; TYROSINE;

EID: 0032702790     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1521-4141(199911)29:11<3507::AID-IMMU3507>3.0.CO;2-9     Document Type: Article

References (37)

1. Ward, S. G., June, C. H. and Olive, D., PI 3-kinase: a pivotal pathway in T cell activation. Immunol. Today 1996. 17: 187-197.
2. Ward, S. G., Wilson, A., Turner, L., Westwick, J. and Sansom, D. M., Inhibition of CD28-mediated T cell costimulation by the PI 3-kinase inhibitor wortmannin. Eur. J. Immunol. 1995. 25: 526-532.
3. Ueda, Y., Levine, B., Freeman, G. J., Nadler, L. M., June, C. H. and Ward, S. G., Both CD28 ligands CD80 (B7.1) and CD86 (B7.2) activate PI 3-kinase and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion. Int. Immunol. 1995. 7: 957-966.
4. Han, J., Luby-Phelps, K., Das, B., Shu, X., Xia, Y., Mosteller, R. D., Krishna, M., Falck, J. R., White, M. and Broek, D., Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine trisphosphatases by Vav. Science 1998. 279: 558-561.
5. Bolland, S., Pearse, R. N., Kurosaki, T. and Ravetch, J. V., SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 1998. 8: 509-516.
6. 3/Tec kinase dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 1998. 17: 1961-1972.
7. Alessi, D. and Cohen, P., Mechanism of activation and function of PKB. Curr. Opin. Genet. Dev. 1998. 8: 55-62.
8. Dudek, H., Datta, S. R., Franke, T. F., Birnbaum, M. J., Copper, G. M., Segal, R. A., Kaplan, D. R. and Greenberg, M. E., Regulation of neuronal survival by the serine/threonine kinase Akt. Science 1997. 275: 661-664.
9. Kulik, G., Klippel, A. and Weber, M. J., Anti-apoptotic signaling by the insulin-like growth factor-1 receptor, PI 3-kinase and Akt. Mol. Cell. Biol. 1997. 17: 1595-1606.
10. Kauffmann-Zeh, A., Rodriguez-Viciana, P., Ulrich, E., Gilbert, C., Coffer, P., Downward, J. and Evan, G., Suppression of c-Myc-induced apoptosis by Ras signaling through PI 3-kinase and PKB. Nature 1997. 385: 544-548.
11. L. Immunity 1995. 3: 87-95.
12. Toker, A. and Cantley, L. C., Signaling through the lipid products of phosphoinositide 3-OH kinase. Nature 1997. 387: 673-676.
13. 3 5-phosphatase. Proc. Natl. Acad. Sci. USA 1996. 93: 1689-1693.
14. Chacko, G. W., Tridandapani, S., Damen, J. E., Liu, L., Krystal, G. and Coggeshall, K. M., Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase SHIP. J. Immunol. 1997. 157: 2234-2238.
15. Ono, M., Bolland, S., Tempst, P. and Ravetch, J. V., Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 1997. 383: 263-266.
16. Tridandapani, S., Kelley, T., Cooney, D., Pradhan, M. and Coggeshall, K. M., Negative signaling in B cells. Immunol. Today 1997. 18: 424-427.
17. Liu, Q., Oliveira-Dos-Santos, A. J., Mariathason, S., Bouchard, D., Jones, J., Sarao, R., Kozieradzki, I., Ohashi, P. S., Penninger, J. M. and Dumont, D. J., The inositol polyphosphate 5-phosphatase SHIP is a crucial negative regulator of B cell antigen receptor signaling. J. Exp. Med 1998. 188: 1333-1342.
18. Liu, L., Damen, J. E., Ware, M., Hughes, M. and Krystal, G., SHIP, a new player in cytokine-induced signaling. Leukemia 1997. 11: 181-184.
19. Ward, S. G., CD28: a signaling perspective. Biochem. J. 1996. 318: 361-377.
20. Pages, F., Ragueneau, M., Klasen, S., Battifora, M., Couez, D., Sweet, R., Truneh, A., Ward, S. G. and Olive, D., Two distinct intra-cytoplasmic regions of the T cell adhesion molecule CD28 participate in PI 3-kinase association. J. Biol. Chem. 1996. 271: 9403-9409.
21. Damen, J., Liu, L., Ware, M. D., Ermolaeva, M., Majerus, P. W. and Krystal, G., Multiple forms of the SH2-containing inositol phosphatase SHIP are generated by C-terminal truncation. Blood 1998. 92: 1199-1205.
22. Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G., Ravichandran, K. S., Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J. Biol. Chem. 1997, 272: 10396-10401.
23. 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell 1995. 83: 821-830.
24. Woscholski, R. and Parker, P. J., Inositol lipid 5-phosphatases: traffic signals and signal traffic. Trends Biochem. Sci. 1997. 22: 427-431.
25. Tridandapani, S., Kelley, T., Pradhan, M., Cooney, D., Justement, L. B. and Coggeshall, K. M., Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B cell Fcγ immunoreceptor-based inhibition peptide motif. Mol. Cell. Biol. 1997. 17: 4305-4311.
26. Osborne, M. A., Zenner, G., Lubinus, M., Zhang, Z., Cantley, L. C., Majerus, P., Burn, P. and Kochan, J. P., The inositol 5-phosphatase SHIP binds to immuno-receptor signaling motifs and respond to high affinity IgE receptor aggregation. J. Biol. Chem. 1996. 271: 29271-29278.
27. Liu, L., Jefferson, A. B., Zhang, X., Norris, F. A., Majerus, P. W., Krystal, G., A novel phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase associates with the IL-3 receptor. J. Biol. Chem. 1996. 271: 29729-29733.
28. ras. Eur. J. Immunol. 1995. 25: 1044-1050.
29. Nunes, J., Truneh, A., Olive, D. and Cantrell, D. A., Signal transduction by CD28 costimulatory receptor on T cells: B7.1 and B7.2 regulation of tyrosine kinase adaptor molecules. J. Biol. Chem. 1996. 271: 1591-1598.
30. SHIP a signal transduction molecule with inositol polyphosphate 5-phosphatase activity. Genes Dev. 1996. 10: 1084-1095.
31. Parry, R., Reif, K., Smith, G., Sansom D. M., Hemmings, B. A. and Ward, S. G., Ligation of the T cell costimulatory receptor CD28 activates the serine/threonine protein kinase PKB. Eur. J. Immunol. 1997. 27: 2495-2502.
32. Klasen, S., Pages, F., Peyron, J. F., Cantrell, D. A., Olive, D., Two distinct regions of the CD28 intracytoplasmic domain are involved in the tyrosine phosphorylation of Vav and GTPase activating protein-associated p62 protein. Int. Immunol. 1998. 10: 481-489.
33. 2. Science 1997. 275: 665-668.
34. Frech, M., Andjelkovic, M., Ingley, E., Reddy, K. K., Falck, J. R. and Hemmings, B. A., High affinity binding of inositol phosphates and phosphoinositides to the Pleckstrin homology domain of RAC-PKB and their influence on kinase activity. J. Biol. Chem. 1997. 272: 8474-8481.
35. Klippel, A., Kavanaugh, W.M., Pot, D. and Williams, L. T., A specific product of PI 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 1997. 17: 338-344.
36. Wright, K., Ward, S. G., Kolios, G. and Westwick, J., Activation of PI 3-kinase by IL-13: an inhibitory signal for inducible nitric oxide synthase expression in the epithelial cell line HT-29. J. Biol. Chem. 1997. 272: 12626-12633.
37. Ward, S. G., Westwick, J., Hall, N. and Sansom, D. M., Ligation of CD28 receptor by B7 induces the formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation. Eur. J. Immunol. 1993. 23: 2572.