Signaling events in T lymphocytes leading to cellular activation or programmed cell death

Clinical Immunology and Immunopathology

Volumn 83, Issue 3, 1997, Pages 205-222

  Musci, Michael A ^a   Latinis, Kevin M ^a   Koretzky, Gary A ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; PROTEIN TYROSINE PHOSPHATASE; T LYMPHOCYTE RECEPTOR;

APOPTOSIS; CELL PROLIFERATION; CLONAL ANERGY; DIAGNOSIS; HUMAN; HUMAN CELL; IMMUNOPATHOLOGY; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; T LYMPHOCYTE ACTIVATION; T LYMPHOCYTE RECEPTOR GENE;

EID: 0031172485     PISSN: 00901229     EISSN: None     Source Type: Journal    
DOI: 10.1006/clin.1996.4315     Document Type: Review

References (198)

1. de la Hera A., Muller U., Olsson C., Isaaz S., Tunnacliffe A. Structure of the T cell antigen receptor (TCR): Two CD3 epsilon subunits in a functional TCR/CD3 complex. J. Exp. Med. 173:1991;7-17.
2. Manolios N., Letourneur F., Bonifacino J. S., Klausner R. D. Pairwise, cooperative and inhibitory interactions describe the assembly and probable structure of the T-cell antigen receptor. EMBO J. 10:1991;1643-1651.
3. Sun J., Leahy D., Kavathas P. Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I. J. Exp. Med. 182:1995;1275-1280.
4. Sant'Angelo D., Waterbury G., Preston-Hurlburt P., Yoon S., Medzhitov R., Hong S., Janeway C. Jr. The specificity and orientation of a TCR to its peptide-MHC class II ligands. Immunity. 4:1996;367-376.
5. Weiss A., Littman D. R. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
6. June C. H., Fletcher M. C., Ledbetter J. A., Samelson L. E. Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation. J. Immunol. 144:1990;1591-1599.
7. June C. H., Fletcher M. C., Ledbetter J. A., Schieven G. L., Siegel J. N., Phillips A. F., Samelson L. E. Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction. Proc. Natl. Acad. Sci. USA. 87:1990;7722-7726.
8. Straus D. B., Weiss A. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell. 70:1992;585-593.
9. Chu K., Littman D. R. Requirement for kinase activity of CD4-associated p56lck in antibody-triggered T cell signal transduction. J. Biol. Chem. 269:1994;24095-24101.
10. van der Geer P., Hunter T., Lindberg R. A. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol. 10:1994;251-337.
11. Doyle C., Strominger J. L. Interaction between CD4 and class II MHC molecules mediates cell adhesion. Nature. 330:1987;256-259.
12. Norment A. M., Salter R. D., Parham P., Engelhard V. H., Littman D. R. Cell-cell adhesion mediated by CD8 and MHC class I molecules. Nature. 336:1988;79-81.
13. Rudd C. E., Barber E. K., Burgess K. E., Hahn J. Y., Odysseos A. D., Sy M. S., Schlossman S. F. Molecular analysis of the interaction of p56lck with the CD4 and CD8 antigens. Adv. Exp. Med. Biol. 292:1991;85-96.
14. Glaichenhaus N., Shastri N., Littman D. R., Turner J. M. Requirement for association of p56lck with CD4 in antigen-specific signal transduction in T cells. Cell. 64:1991;511-520.
15. Chalupny N., Ledbetter J., Kavathas P. Association of CD8 with p56lck is required for early T cell signalling events. EMBO J. 10:1991;1201-1207.
16. Dianzani U., Shaw A., al-Ramadi B. K., Kubo R. T., Janeway C. A. Jr. Physical association of CD4 with the T cell receptor. J. Immunol. 148:1992;678-688.
17. Cooke M. P., Abraham K. M., Forbush K. A., Perlmutter R. M. Regulation of T cell receptor signaling by a src family protein-tyrosine kinase (p59fyn). Cell. 65:1991;281-291.
18. Tsygankov A. Y., Broker B. M., Fargnoli J., Ledbetter J. A., Bolen J. B. Activation of tyrosine kinase p60fyn following T cell antigen receptor cross-linking. J. Biol. Chem. 267:1992;18259-18262.
19. Samelson L. E., Phillips A. F., Luong E. T., Klausner R. D. Association of the fyn protein-tyrosine kinase with the T-cell antigen receptor. Proc. Natl. Acad. Sci. USA. 87:1990;4358-4362.
20. Karnitz L., Sutor S., Torigoe T., Reed J., Bell M., McKean D., Leibson P., Abraham R. Effects of p56lck deficiency on the growth and cytolytic effector function of an interleukin-2-dependent cytotoxic T-cell line. Mol. Cell. Biol. 12:1992;4521-4530.
21. Molina T., Kishihara K., Siderovski D., van Ewijk W., Narendran A., Timms E., Wakeham A., Paige C., Hartmann K., Veillette A. Profound block in thymocyte development in mice lacking p56lck. Nature. 357:1992;161-164.
22. Stein P. L., Lee H. M., Rich S., Soriano P. pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells. Cell. 70:1992;741-750.
23. Lancki D. W., Fields P., Qian D., Fitch F. W. Induction of lytic pathways in T cell clones derived from wild-type or protein tyrosine kinase Fyn mutant mice. Immunol. Rev. 146:1995;117-144.
24. Qian D., Griswold-Prenner I., Rosner M. R., Fitch F. W. Multiple components of the T cell antigen receptor complex become tyrosine-phosphorylated upon activation. J. Biol. Chem. 268:1993;4488-4493.
25. Irving B. A., Chan A. C., Weiss A. Functional characterization of a signal transducing motif present in the T cell antigen receptor zeta chain. J. Exp. Med. 177:1993;1093-1103.
26. Shiue L., Zoller M. J., Brugge J. S. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J. Biol. Chem. 270:1995;10498-10502.
27. Flaswinkel H., Barner M., Reth M. The tyrosine activation motif as a target of protein tyrosine kinases and SH2 domains. Semin. Immunol. 7:1995;21-27.
28. Chan A. C., Iwashima M., Turck C. W., Weiss A. ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR zeta chain. Cell. 71:1992;649-662.
29. Straus D. B., Weiss A. The CD3 chains of the T cell antigen receptor associate with the ZAP-70 tyrosine kinase and are tyrosine phosphorylated after receptor stimulation. J. Exp. Med. 178:1993;1523-1530.
30. Chan A. C., Kadlecek T. A., Elder M. E., Filipovich A. H., Kuo W. L., Iwashima M., Parslow T. G., Weiss A. ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency. Science. 264:1994;1599-1601.
31. Roifman C. A mutation in zap-70 protein tyrosine kinase results in a selective immunodeficiency. J. Clin. Immunol. 15:1995;52S-62S.
32. Iwashima M., Irving B. A., van Oers N. S., Chan A. C., Weiss A. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science. 263:1994;1136-1139.
33. Koretzky G. A. Role of the CD45 tyrosine phosphatase in signal transduction in the immune system. FASEB J. 7:1993;420-426.
34. Justement L. B., Brown V. K., Lin J. Regulation of B-cell activation by CD45: A question of mechanism. Immunol. Today. 15:1994;399-406.
35. Berger S. A., Mak T. W., Paige C. J. Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells. J. Exp. Med. 180:1994;471-476.
36. Corvaia N., Reischl I. G., Kroemer E., Mudde G. C. Modulation of Fc gamma receptor-mediated early events by the tyrosine phosphatase CD45 in primary human monocytes. Consequences for interleukin-6 production. Eur. J. Immunol. 25:1995;738-744.
37. Dixon J. E. Structure and catalytic properties of protein tyrosine phosphatases. Ann. N.Y. Acad. Sci. 766:1995;18-22.
38. Hall L. R., Streuli M., Schlossman S. F., Saito H. Complete exon-intron organization of the human leukocyte common antigen (CD45) gene. J. Immunol. 141:1988;2781-2787.
39. Rothstein D. M., Saito H., Streuli M., Schlossman S. F., Morimoto C. The alternative splicing of the CD45 tyrosine phosphatase is controlled by negative regulatory trans-acting splicing factors. J. Biol. Chem. 267:1992;7139-7147.
40. Pilarski L. M., Deans J. P. Selective expression of CD45 isoforms and of maturation antigens during human thymocyte differentiation: Observations and hypothesis. Immunol. Lett. 21:1989;187-198.
41. Deans J. P., Serra H. M., Shaw J., Shen Y. J., Torres R. M., Pilarski L. M. Transient accumulation and subsequent rapid loss of messenger RNA encoding high molecular mass CD45 isoforms after T cell activation. J. Immunol. 148:1992;1898-1905.
42. Chui D., Ong C. J., Johnson P., Teh H. S., Marth J. D. Specific CD45 isoforms differentially regulate T cell receptor signaling. EMBO J. 13:1994;798-807.
43. McKenney D. W., Onodera H., Gorman L., Mimura T., Rothstein D. M. Distinct isoforms of the CD45 protein-tyrosine phosphatase differentially regulate interleukin 2 secretion and activation signal pathways involving Vav in T cells. J. Biol. Chem. 270:1995;24949-24954.
44. Thomas M. L. The regulation of B- and T-lymphocyte activation by the transmembrane protein tyrosine phosphatase CD45. Curr. Opin. Cell Biol. 6:1994;247-252.
45. Koretzky G. A., Kohmetscher M. A., Kadleck T., Weiss A. Restoration of T cell receptor-mediated signal transduction by transfection of CD45 cDNA into a CD45-deficient variant of the Jurkat T cell line. J. Immunol. 149:1992;1138-1142.
46. Hovis R. R., Donovan J. A., Musci M. A., Motto D. G., Goldman F. D., Ross S. E., Koretzky G. A. Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45. Science. 260:1993;544-546.
47. Volarevic S., Niklinska B. B., Burns C. M., June C. H., Weissman A. M., Ashwell J. D. Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains. Science. 260:1993;541-544.
48. Desai D. M., Sap J., Schlessinger J., Weiss A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell. 73:1993;541-554.
49. Desai D. M., Sap J., Silvennoinen O., Schlessinger J., Weiss A. The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation. EMBO J. 13:1994;4002-4010.
50. Motto D. G., Musci M. A., Koretzky G. A. Surface expression of a heterologous phosphatase complements CD45 deficiency in a T cell clone. J. Exp. Med. 180:1994;1359-1366.
51. Cooper J. A., Gould K. L., Cartwright C. A., Hunter T. Tyr527 is phosphorylated in pp60c-src: Implications for regulation. Science. 231:1986;1431-1434.
52. Nada S., Okada M., MacAuley A., Cooper J. A., Nakagawa H. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature. 351:1991;69-72.
53. Ostergaard H. L., Shackelford D. A., Hurley T. R., Johnson P., Hyman R., Sefton B. M., Trowbridge I. S. Expression of CD45 alters phosphorylation of the lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines. Proc. Natl. Acad. Sci. USA. 86:1989;8959-8963.
54. McFarland E. D., Hurley T. R., Pingel J. T., Sefton B. M., Shaw A., Thomas M. L. Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor. Proc. Natl. Acad. Sci. USA. 90:1993;1402-1406.
55. Koretzky G. A., Kohmetscher M., Ross S. CD45-associated kinase activity requires lck but not T cell receptor expression in the Jurkat T cell line. J. Biol. Chem. 268:1993;8958-8964.
56. Burns C. M., Sakaguchi K., Appella E., Ashwell J. D. CD45 regulation of tyrosine phosphorylation and enzyme activity of src family kinases. J. Biol. Chem. 269:1994;13594-13600.
57. D'Oro U., Sakaguchi K., Appella E., Ashwell J. D. Mutational analysis of Lck in CD45-negative T cells: Dominant role of tyrosine 394 phosphorylation. Mol. Cell. Biol. 16:1996;4996-5003.
58. Bruyns E., Hendricks-Taylor L. R., Meuer S., Koretzky G. A., Schraven B. Identification of the sites of interaction between lymphocyte phosphatase-associated phosphoprotein (LPAP) and CD45. J. Biol. Chem. 270:1995;31372-31376.
59. Kitamura K., Maiti A., Ng D. H., Johnson P., Maizel A. L., Takeda A. Characterization of the interaction between CD45 and CD45-AP. J. Biol. Chem. 270:1995;21151-21157.
60. McFarland E. D., Thomas M. L. CD45 protein-tyrosine phosphatase associates with the WW domain-containing protein, CD45AP, through the transmembrane region. J. Biol. Chem. 270:1995;28103-28107.
61. Furukawa T., Itoh M., Krueger N. X., Streuli M., Saito H. Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 zeta chain. Proc. Natl. Acad. Sci. USA. 91:1994;10928-10932.
62. Stover D. R., Walsh K. A. Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases. Mol. Cell. Biol. 14:1994;5523-5532.
63. Kuhne M. R., Pawson T., Lienhard G. E., Feng G. S. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem. 268:1993;11479-11481.
64. Li W., Nishimura R., Kashishian A., Batzer A. G., Kim W. J., Cooper J. A., Schlessinger J. A new function for a phosphotyrosine phosphatase: Linking GRB2-Sos to a receptor tyrosine kinase. Mol. Cell. Biol. 14:1994;509-517.
65. Tauchi T., Feng G. S., Marshall M. S., Shen R., Mantel C., Pawson T., Broxmeyer H. E. The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells. J. Biol. Chem. 269:1994;25206-25211.
66. Tauchi T., Feng G. S., Shen R., Hoatlin M., Bagby G. C. Jr., Kabat D., Lu L., Broxmeyer H. E. Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways. J. Biol. Chem. 270:1995;5631-5635.
67. Tivol E. A., Borriello F., Schweitzer A. N., Lynch W. P., Bluestone J. A., Sharpe A. H. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity. 3:1995;541-547.
68. Krummel M. F., Allison J. P. CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation. J. Exp. Med. 182:1995;459-465.
69. Waterhouse P., Penninger J. M., Timms E., Wakeham A., Shahinian A., Lee K. P., Thompson C. B., Griesser H., Mak T. W. Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4. Science. 270:1995;985-988.
70. Marengere L. E., Waterhouse P., Duncan G. S., Mittrucker H. W., Feng G. S., Mak T. W. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-04. Science. 272:1996;1170-1173.
71. Ravichandran K. S., Lee K. K., Songyang Z., Cantley L. C., Burn P., Burakoff S. J. Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. Science. 262:1993;902-905.
72. Baldari C. T., Pelicci G., Di Somma M. M., Milia E., Giuli S., Pelicci P. G., Telford J. L. Inhibition of CD4/p56lck signaling by a dominant negative mutant of the Shc adaptor protein. Oncogene. 10:1995;1141-1147.
73. Shultz L. D., Schweitzer P. A., Rajan T. V., Yi T., Ihle J. N., Matthews R. J., Thomas M. L., Beier D. R. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell. 73:1993;1445-1454.
74. Yi T., Mui A. L., Krystal G., Ihle J. N. Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol. Cell. Biol. 13:1993;7577-7586.
75. Yi T., Ihle J. N. Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand. Mol. Cell. Biol. 13:1993;3350-3358.
76. David M., Chen H. E., Goelz S., Larner A. C., Neel B. G. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 15:1995;7050-7058.
77. Klingmuller U., Lorenz U., Cantley L. C., Neel B. G., Lodish H. F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell. 80:1995;729-738.
78. Burshtyn D. N., Scharenberg A. M., Wagtmann N., Rajagopalan S., Berrada K., Yi T., Kinet J. P., Long E. O. Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor. Immunity. 4:1996;77-85.
79. Chen H. E., Chang S., Trub T., Neel B. G. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 16:1996;3685-3697.
80. Lorenz U., Ravichandran K. S., Burakoff S. J., Neel B. G. Lack of SHPTP1 results in src-family kinase hyperactivation and thymocyte hyperresponsiveness. Proc. Natl. Acad. Sci. USA. 93:1996;9624-9629.
81. Plas D. R., Johnson R., Pingel J. T., Matthews R. J., Dalton M., Roy G., Chan A. C., Thomas M. L. Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. Science. 272:1996;1173-1176.
82. Mizuno K., Katagiri T., Hasegawa K., Ogimoto M., Yakura H. Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells. J. Exp. Med. 184:1996;457-464.
83. Clapham D. E. Calcium signaling. Cell. 80:1995;259-268.
84. Nishibe S., Wahl M. I., Hernandez-Sotomayor S. M., Tonks N. K., Rhee S. G., Carpenter G. Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation. Science. 250:1990;1253-1256.
85. Clipstone N. A., Crabtree G. R. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature. 367:1992;695-697.
86. Izquierdo M., Leevers S. J., Marshall C. J., Cantrell D. p21ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes. J. Exp. Med. 178:1993;1199-1208.
87. Hallberg B., Rayter S. I., Downward J. Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation. J. Biol. Chem. 269:1994;3913-3916.
88. Izquierdo M., Bowden S., Cantrell D. The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor. J. Exp. Med. 180:1994;401-406.
89. Downward J. The GRB2/Sem-5 adaptor protein. FEBS Lett. 338:1994;113-117.
90. Sieh M., Batzer A., Schlessinger J., Weiss A. GRB2 and phospholipase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation. Mol. Cell. Biol. 14:1994;4435-4442.
91. Ravichandran K. S., Lorenz U., Shoelson S. E., Burakoff S. J. Interaction of Shc with Grb2 regulates association of Grb2 with mSOS. Mol. Cell. Biol. 15:1995;593-600.
92. Motto D. G., Ross S. E., Jackman J. K., Sun Q., Olson A. L., Findell P. R., Koretzky G. A. In vivo association of Grb2 with pp116, a substrate of the T cell antigen receptor-activated protein tyrosine kinase. J. Biol. Chem. 269:1994;21608-21613.
93. Buday L., Egan S. E., Rodriguez Viciana P., Cantrell D. A., Downward J. A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. J. Biol. Chem. 269:1994;9019-9023.
94. Huang X., Li Y., Tanaka K., Moore K. G., Hayashi J. I. Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase C gamma 1, Grb2, and phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA. 92:1995;11618-11622.
95. Motto D. G., Musci M. A., Ross S. E., Koretzky G. A. Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C-gamma-1 in T cells. Mol. Cell. Biol. 16:1996;2823-2829.
96. Jackman J. K., Motto D. G., Sun Q., Tanemoto M., Turck C. W., Peltz G. A., Koretzky G. A., Findell P. R. Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells. J. Biol. Chem. 270:1995;7029-7032.
97. Motto D. G., Ross S. E., Wu J., Hendricks-Taylor L. R., Koretzky G. A. Implication of the Grb2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. J. Exp. Med. 183:1996;1937-1943.
98. Donovan J. A., Wange R. L., Langdon W. Y., Samelson L. E. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J. Biol. Chem. 269:1994;22921-22924.
99. Meisner H., Conway B. R., Hartley D., Czech M. P. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol. Cell. Biol. 15:1995;3571-3578.
100. Fournel M., Davidson D., Weil R., Veillette A. Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes. J. Exp. Med. 183:1996;301-306.
101. Margolis B., Hu P., Katzav S., Li W., Oliver J. M., Ullrich A., Weiss A., Schlessinger J. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature. 356:1992;71-74.
102. Musacchio A., Gibson T., Rice P., Thompson J., Saraste M. The PH domain: A common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci. 18:1993;343-348.
103. Adams J. M., Houston H., Allen J., Lints T., Harvey R. The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene. 7:1992;611-618.
104. Tarakhovsky A., Turner M., Schaal S., Mee P. J., Duddy L. P., Rajewsky K., Tybulewicz V. L. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature. 374:1995;467-470.
105. Zhang R., Alt F. W., Davidson L., Orkin S. H., Swat W. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature. 374:1995;470-473.
106. Fischer K. D., Zmuldzinas A., Gardner S., Barbacid M., Bernstein A., Guidos C. Defective T-cell receptor signalling and positive selection of Vav-deficient CD4+ CD8+ thymocytes. Nature. 374:1995;474-477.
107. Wu J., Motto D. G., Koretzky G. A., Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity. 4:1996;593-602.
108. Tuosto L., Michel F., Acuto O. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. J. Exp. Med. 184:1996;1161-1167.
109. H. Onodera, D. G. Motto, G. A. Koretzky, D. M. Rothstein, Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to vav by distinct isoforms of the CD45 protein tyrosine phosphatase, J. Biol. Chem.
110. Ashwell J. D., Cunningham R. E., Noguchi P. D., Hernandez D. Cell growth cycle block of T cell hybridomas upon activation with antigen. J. Exp. Med. 165:1987;173-194.
111. Mercep M., Bluestone J. A., Noguchi P. D., Ashwell J. D. Inhibition of transformed T cell growth in vitro by monoclonal antibodies directed against distinct activating molecules. J. Immunol. 140:1988;324-335.
112. Ucker D. S., Ashwell J. D., Nickas G. Activation-driven T cell death. I. Requirements for de novo transcription and translation and association with genome fragmentation. J. Immunol. 143:1989;3461-3469.
113. Shi Y. F., Sahai B. M., Green D. R. Cyclosporin A inhibits activation-induced cell death in T-cell hybridomas and thymocytes. Nature. 339:1989;625-626.
114. Smith C. A., Williams G. T., Kingston R., Jenkinson E. J., Owen J. J. T. Antibodies to CD3/T-cell receptor complex induce death by apoptosis in immature T cells in thymic cultures. Nature. 377:1989;181-183.
115. Jones L. A., Chin L. T., Longo D. L., Kruisbeek A. M. Peripheral clonal elimination of functional T cells. Science. 250:1990;1726-1729.
116. Murphy K. M., Heimberger A. B., Loh D. Y. Induction by antigen of intrathymic apoptosis of CD4 + CD8 + TCRlo thymocytes in vivo. Science. 250:1990;1720-1723.
117. Ucker D. S., Meyers J., Obermiller P. S. Activation-driven T cell death. II. Quantitative differences alone distinguish stimuli triggering nontransformed T cell proliferation or death. J. Immunol. 149:1992;1583-1592.
118. Shi Y. F., Szalay M. G., Paskar L., Sahai B. M., Boyer M., Singh B., Green D. R. Activation-induced cell death in T cell hybridomas is due to apoptosis. Morphologic aspects and DNA fragmentation. J. Immunol. 145:1990;3945.
119. Dhein J., Walczak H., Baumler C., Debatin K. M., Krammer P. H. Autocrine T-cell suicide mediated by APO-1/(Fas/CD95). Nature. 373:1995;438-441.
120. Brunner T., Mogil R. J., LaFace D., Yoo N. J., Mahboubi A., Echeverri F., Martin S. J., Force W. R., Lynch D. H., Ware C. F. Cell-autonomous Fas (CD95)/Fas-ligand interaction mediates activation-induced apoptosis in T-cell hybridomas. Nature. 373:1995;441-444.
121. Park C. G., Lee S. Y., Kandala G., Lee S. Y., Choi Y. A novel gene product that couples TCR signaling to Fas(CD95) expression in activation-induced cell death. Immunity. 4:1996;583-591.
122. Alderson M. R., Tough T. W., Davis-Smith T., Braddy S., Falk B., Schooley K. A., Goodwin R. G., Smith C. A., Ramsdell F., Lynch D. H. Fas ligand mediates activation-induced cell death in human T lymphocytes. J. Exp. Med. 181:1995;71-77.
123. Ju S. T., Panka D. J., Cui H., Ettinger R., el-Khatib M., Sherr D. H., Stanger B. Z., Marshak-Rothstein A. Fas(CD95)/FasL interactions required for programmed cell death after T-cell activation. Nature. 373:1995;444-448.
124. Vignaux F., Vivier E., Malissen B., Depraetere V., Nagata S., Golstein P. TCR/CD3 coupling to Fas-based cytotoxicity. J. Exp. Med. 181:1995;781-786.
125. Yang Y., Mercep M., Ware C. F., Ashwell J. D. Fas and activation-induced Fas ligand mediate apoptosis of T cell hybridomas: Inhibition of Fas ligand expression by retinoic acid and glucocorticoids. J. Exp. Med. 181:1995;1673-1682.
126. Schreiber S. L., Crabtree G. R. The mechanism of action of cyclosporin A and FK506. Immunol. Today. 13:1992;136-142.
127. Anel A., Buferne M., Boyer C., Schmitt-Verhulst A. M., Golstein P. T cell receptor-induced Fas ligand expression in cytotoxic T lymphocyte clones is blocked by protein tyrosine kinase inhibitors and cyclosporin A. Eur. J. Immunol. 24:1994;2469-2476.
128. Brunner T., Nam J. Y., LaFace D., Ware C. F. Activation-induced cell death in murine T cell hybridomas: Differential regulation of Fas (CD95) versus Fas ligand expression by cyclosporin A and FK506. Int. Immunol. 8:1996;1017-1026.
129. Takahashi T., Tanaka M., Inazawa J., Abe T., Suda T., Nagata S. Human Fas ligand: Gene structure, chromosomal location and species specificity. Int. Immunol. 6:1994;1567-1574.
130. Latinis K. M., Carr L. L., Peterson E. J., Norian L. A., Eliason S. L., Kocetzky G. A. Regulation of CD95 (Fas) ligand expression by TCR-mediated signaling events. J. Immunol. 1997.
131. Hodge M. R., Ranger A. M., de la Brouse F. C., Hoey T., Grusby M. J., Glimcher L. H. Hyperproliferation and dysregulation of IL-4 expression in NF-ATp-deficient mice. Immunity. 4:1996;397-405.
132. Liu Y., Janeway C. A. Jr. Cells that present both specific ligand and costimulatory activity are the most efficient inducers of clonal expansion of normal CD4 T cells. Proc. Natl. Acad. Sci. USA. 89:1992;3845-3849.
133. Reiser H., Freeman G. J., Razi-Wolf Z., Gimmi C. D., Benacerraf B., Nadler L. M. Murine B7 antigen provides an efficient costimulatory signal for activation of murine T lymphocytes via the T-cell receptor/CD3 complex. Proc. Natl. Acad. Sci. USA. 89:1992;271-275.
134. Freeman G. J., Borriello F., Hodes R. J., Reiser H., Gribben J. G., Ng J. W., Kim J., Goldberg J. M., Hathcock K., Laszlo G. Murine B7-2, an alternative CTLA4 counter-receptor that costimulates T cell proliferation and interleukin 2 production. J. Exp. Med. 178:1993;2185-2192.
135. Freeman G. J., Gribben J. G., Boussiotis V. A., Ng J. W., Restivo V. A. Jr., Lombard L. A., Gray G. S., Nadler L. M. Cloning of B7-2: A CTLA-4 counter-receptor that costimulates human T cell proliferation. Science. 262:1993;909-911.
136. Tan P., Anasetti C., Hansen J. A., Melrose M., Brunvand M., Bradshaw J., Ledbetter J. A., Linsley P. S. Induction of alloantigen-specific hyporesponsiveness in human T lymphocytes by blocking interaction of CD28 with its natural ligand B7/BB1. J. Exp. Med. 177:1993;165-173.
137. Lindsten T., June C. H., Ledbetter J. A., Stella G., Thompson C. B. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science. 244:1989;339-343.
138. Fraser J. D., Irving B. A., Crabtree G. R., Weiss A. Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28. Science. 251:1991;313-316.
139. Fraser J. D., Weiss A. Regulation of T-cell lymphokine gene transcription by the accessory molecule CD28. Mol. Cell. Biol. 12:1992;4357-4363.
140. Fraser J. D., Newton M. E., Weiss A. CD28 and T cell antigen receptor signal transduction coordinately regulate interleukin 2 gene expression in response to superantigen stimulation. J. Exp. Med. 175:1992;1131-1134.
141. Boise L. H., Minn A. J., Noel P. J., June C. H., Accavitti M. A., Lindsten T., Thompson C. B. CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-XL. Immunity. 3:1995;87-98.
142. Boise L. H., Noel P. J., Thompson C. B. CD28 and apoptosis. Curr. Opin. Immunol. 7:1995;620-625.
143. Noel P. J., Boise L. H., Green J. M., Thompson C. B. CD28 costimulation prevents cell death during primary T cell activation. J. Immunol. 157:1996;636-642.
144. Radvanyi L. G., Shi Y., Homayoun V., Sharma A., Dhala R., Mills G. B., Miller R. G. CD28 costimulation inhibits TCR-induced apoptosis during a primary T cell response. J. Immunol. 156:1996;1788-1798.
145. van Parijs L., Ibraghimov A., Abbas A. K. The Roles of costimulation and Fas in T cell apoptosis and peripheral tolerance. Immunity. 4:1996;321-328.
146. Hengartner M. O., Ellis R. E., Horvitz H. R. Caenorhabditis elegans. Nature. 356:1992;494-499.
147. Hengartner M. O., Horvitz H. R. C. elegans. Cell. 76:1994;665-676.
148. Horvitz H. R., Shaham S., Hengartner M. O. The genetics of programmed cell death in the nematodeCaenorhabditis elegans. CSH Sym. Quan. Biol. 59:1994;377-385.
149. Watanabe-Fukunaga R., Brannan C. I., Copeland N. G., Jenkins N. A., Nagata S. Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis. Nature. 356:1992;314-317.
150. Takahashi T., Tanaka M., Brannan C. I., Jenkins N. A., Copeland N. G., Suda T., Nagata S. Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand. Cell. 76:1994;969-976.
151. Fisher G. H., Rosenberg F. J., Straus S. E., Dale J. K., Middleton L. A., Lin A. Y., Strober W., Lenardo M. J., Puck J. M. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome. Cell. 81:1995;935-946.
152. Rieux-Laucat F., Le Deist F., Hivroz C., Roberts I. A., Debatin K. M., Fischer A., de Villartay J. P. Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity. Science. 268:1995;1347-1349.
153. Adachi M., Suematsu S., Suda T., Watanabe D., Fukuyama H., Ogasawara J., Tanaka T., Yoshida N., Nagata S. Enhanced and accelerated lymphoproliferation in Fas-null mice. Proc. Natl. Acad. Sci. USA. 93:1996;2131-2136.
154. Wu J., Wilson J., He J., Xiang L., Schur P. H., Mountz J. D. Fas ligand mutation in a patient with systemic lupus erythematosus and lymphoproliferative disease. J. Clin. Invest. 98:1996;1107-1113.
155. Cohen P. L., Eisenberg R. A. Lpr and gld: Single gene models of systemic autoimmunity and lymphoproliferative disease. Annu. Rev. Immunol. 9:1991;243-269.
156. Bellgrau D., Gold D., Selawry H., Moore J., Franzusoff A., Duke R. C. A role for CD95 ligand in preventing graft rejection. Nature. 377:1995;630-632.
157. Griffith T. S., Brunner T., Fletcher S. M., Green D. R., Ferguson T. A. Fas ligand-induced apoptosis as a mechanism of immune privilege. Science. 270:1995;1189-1192.
158. Griffith T. S., Yu X., Herndon J. M., Green D. R., Ferguson T. A. CD95-induced apoptosis of lymphocytes in an immune priveleged site induces immunological tolerance. Immunity. 5:1996;7-16.
159. Trauth B. C., Klas C., Peters A. M., Matzku S., Moller P., Falk W., Debatin K. M., Krammer P. H. Monoclonal antibody-mediated tumor regression by induction of apoptosis. Science. 245:1989;301-305.
160. Yonehara S., Ishii A., Yonehara M. A cell-killing monoclonal antibody (anti-Fas) to a cell surface antigen co-downregulated with the receptor of tumor necrosis factor. J. Exp. Med. 169:1989;1747-1756.
161. Itoh N., Yonehara S., Ishii A., Yonehara M., Mizushima S., Sameshima M., Hase A., Seto Y., Nagata S. The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis. Cell. 66:1991;233-243.
162. Oehm A., Behrmann I., Falk W., Pawlita M., Maier G., Klas C., Li-Weber M., Richards S., Dhein J., Trauth B. C. Purification and molecular cloning of the APO-1 cell surface antigen, a member of the tumor necrosis factor/nerve growth factor receptor superfamily: Sequence identity with the Fas antigen. J. Biol. Chem. 267:1992;10709-10715.
163. Nagata S., Golstein P. The Fas death factor. Science. 267:1995;1449-1456.
164. Itoh N., Nagata S. A novel protein domain required for apoptosis: Mutational analysis of human Fas antigen. J. Biol. Chem. 268:1993;10932-10937.
165. Tartaglia L. A., Ayres T. M., Wong G. H., Goeddel D. V. A novel domain within the 55 kd TNF receptor signals cell death. Cell. 74:1993;845-853.
166. Boldin M. P., Varfolomeev E. E., Pancer Z., Mett I. L., Camonis J. H., Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270:1995;7795-7798.
167. Chinnaiyan A. M., O'Rourke K., Tewari M., Dixit V. M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 81:1995;505-512.
168. Hsu H., Xiong J., Goeddel D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell. 81:1995;495-504.
169. Stanger B. Z., Leder P., Lee T. H., Kim E., Seed B. RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell. 81:1995;513-523.
170. Schoenfeld H. J., Poeschl B., Frey J. R., Loetscher H., Hunziker W., Lustig A., Zulauf M. Efficient purification of recombinant human tumor necrosis factor beta fromEscherichia coli. J. Biol. Chem. 266:1991;3863-3869.
171. Banner D. W., D'Arcy A., Janes W., Gentz R., Schoenfeld H. J., Broger C., Loetscher H., Lesslauer W. Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation. Cell. 73:1993;431-445.
172. Enari M., Hug H., Nagata S. Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature. 375:1995;78-81.
173. Los M., Van de Craen M., Penning L. C., Schenk H., Westendorp M., Baeuerle P. A., Droge W., Krammer P. H., Fiers W., Schulze-Osthoff K. Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis. Nature. 375:1995;81-83.
174. Tewari M., Dixit V. M. Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product. J. Biol. Chem. 270:1995;3255-3260.
175. Nicholson D. W., Ali A., Thornberry N. A., Vaillancourt J. P., Ding C. K., Gallant M., Gareau Y., Griffin P. R., Labelle M., Lazebnik Y. A. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 376:1995;37-43.
176. Tewari M., Quan L. T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D. R., Poirier G. G., Salvesen G. S., Dixit V. M. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
177. Tewari M., Beidler D. R., Dixit V. M. CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 270:1995;18738-18741.
178. Casciola-Rosen L., Nicholson D. W., Chong T., Rowan K. R., Thornberry N. A., Miller D. K., Rosen A. Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death. J. Exp. Med. 183:1996;1957-1964.
179. Yuan J., Shaham S., Ledoux H. M., Ellis, Horvitz H. R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell. 75:1993;641-652.
180. Kuida K., Lippke J. A., Ku G., Harding M. W., Livingston D. J., Su M. S., Flavell R. A. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science. 267:1995;2000-2003.
181. Li P., Allen H., Banerjee S., Franklin S., Herzog L., Johnston C., McDowell J., Paskind M., Rodman L., Salfeld J. Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell. 80:1995;401-411.
182. Enari M., Talanian R. V., Wong W. W., Nagata S. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature. 380:1996;723-726.
183. Schlegel J., Peters I., Orrenius S., Miller D. K., Thornberry N. A., Yamin T. T., Nicholson D. W. CPP32/apopain is a key interleukin 1 beta converting enzyme-like protease involved in Fas-mediated apoptosis. J. Biol. Chem. 271:1996;1841-1844.
184. Takahashi A., Alnemri E. S., Lazebnik Y. A., Fernandes-Alnemri T., Litwack G., Moir R. D., Goldman R. D., Poirier G. G., Kaufmann S. H., Earnshaw W. C. Cleavage of lamin A by Mch2α but not CPP32: Multiple interleukin 1β-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl. Acad. Sci. USA. 93:1996;8395-8400.
185. Sato T., Irie S., Kitada S., Reed J. C. FAP-1: A protein tyrosine phosphatase that associates with Fas. Science. 268:1995;411-415.
186. Boldin M. P., Goncharov T. M., Goltsev Y. V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell. 85:1996;803-815.
187. Fernandes-Alnemri T., Armstrong R. C., Krebs J., Srinivasula S. M., Wang L., Bullrich F., Fritz L. C., Trapani J. A., Tomaselli K. J., Litwack G., Alnemri E. S. In vitro activation of CPP32 and Mch3 and Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl. Acad. Sci. USA. 93:1996;7464-7469.
188. Muzio M., Chinnaiyan A. M., Kischkel F. C., O'Rourke K., Shevchenko A., Ni J., Scaffidi C., Bretz J. D., Zhang M., Gentz R., Mann N., Krammer P. H., Peter M. E., Dixit V. M. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell. 85:1996;817-827.
189. Cifone M. G., De Maria R., Roncaioli P., Rippo M. R., Azuma M., Lanier L. L., Santoni A., Testi R. Apoptotic signaling through CD95 (Fas/Apo-1) activates an acidic sphingomyelinase. J. Exp. Med. 180:1994;1547-1552.
190. Kolesnick R. N., Haimovitz-Friedman A., Fuks Z. The sphingomyelin signal transduction pathway mediates apoptosis for tumor necrosis factor, Fas, and ionizing radiation. Biochem. Cell Biol. 72:1994;471-474.
191. Tepper C. G., Jayadev S., Liu B., Bielawska A., Wolff R., Yonehara S., Hannun Y. A., Seldin M. F. Role for ceramide as an endogenous mediator of Fas-induced cytotoxicity. Proc. Natl. Acad. Sci. USA. 92:1995;8443-8447.
192. De Maria R., Boirivant M., Cifone M. G., Roncaioli P., Hahne M., Tschopp J., Pallone F., Santoni A., Testi R. Functional expression of Fas and Fas ligand on human gut lamina propria T lymphocytes: A potential role for the acidic sphingomyelyinase pathway in normal immunoregulation. J. Clin. Invest. 97:1996;316-322.
193. Gulbins E., Bissonnette R., Mahboubi A., Martin S., Nishioka W., Brunner T., Baier G., Baier-Bitterlich G., Byrd C., Lang F. FAS-induced apoptosis is mediated via a ceramide-initiated RAS signaling pathway. Immunity. 2:1995;341-351.
194. Westwick J. K., Bielawska A. E., Dbaibo G., Hannun Y. A., Brenner D. A. Ceramide activates the stress-activated protein kinases. J. Biol. Chem. 270:1995;22689-22692.
195. Latinis K., Koretzky G. Fas ligation induces apoptosis and Jun Kinase activation independently of CD45 and Lck in Human T cells. Blood. 87:1996.
196. Wilson D. J., Fortner K. A., Lynch D. H., Mattingly R. R., Macara I. G., Posada J. A., Budd R. C. JNK, but not MAPK, activation is associated with Fas-mediated apoptosis in human T cells. Eur. J. Immunol. 26:1996;989-994.
197. Xia Z., Dickens M., Raingeaud J., Davis R. J., Greenberg M. E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 270:1995;1326-1331.
198. Verheij M., Bose R., Lin X. H., Yao B., Jarvis W. D., Grant S., Birrer M. J., Szabo E., Zon L. I., Kyriakis J. M., Haimovitz-Friedman A., Fuks Z., Kolesnick R. N. Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis. Nature. 380:1996;75-79.