General mechanisms of cytokine receptor signaling

Advances in Protein Chemistry

Volumn 52, Issue , 1998, Pages 109-140

  Carpenter, Laura Rocco ^a   Yancopoulos, George D ^a   Stahl, Neil ^a  

^a REGENERON PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; CARDIOTROPHIN 1; CILIARY NEUROTROPHIC FACTOR; CYTOKINE; CYTOKINE RECEPTOR; ERYTHROPOIETIN; GAMMA INTERFERON; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 13; INTERLEUKIN 15; INTERLEUKIN 2; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 7; INTERLEUKIN 9; LEUKEMIA INHIBITORY FACTOR; ONCOSTATIN M; PROTEIN TYROSINE PHOSPHATASE; TRANSCRIPTION FACTOR; TYROSINE KINASE RECEPTOR;

BINDING SITE; DIMERIZATION; ENZYME ACTIVATION; ENZYME SUBSTRATE; HUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; REVIEW; SIGNAL TRANSDUCTION;

EID: 0031794542     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0065-3233(08)60434-9     Document Type: Review

References (138)

1. Taga, T., and Kishimoto, T. (1997). gp130 and the interleukin-G family of cytokines. Annu. Rev. Immunol. 15, 797-819.
2. Hibi, M., Nakajima, K., and Hirano, T. (1996). IL-6 cytokine family and signal transduction: A model of the cytokine system. J. Mol. Med. 74, 1-12.
3. Stahl, N., and Yancopoulos, G. D. (1997). IL6, IL11, LIF, OSM, Cardiotrophin-1, and CNTF. In "Growth Factors and Cytokines in Health and Disease," (D. LeRoith and C. Bondy, Eds), Vol. 2B, pp. 777-809. JAI Press, Greenwich, CT.
4. Yamasaki, K., Taga, T., Hirata, Y., Yawata, H., Kawanishi, Y., Seed, B., Taniguchi, T., Hirano, T., and Kishimoto, T. (1988). Cloning and expression of the human interleukin-6 (BSF-2/IFNβ 2) receptor. Science 241, 825-828.
5. Davis, S., Aldrich, T. H., Valenzuela, D. M., Wong, V., Furth, M. E., Squinto, S. P., and Yancopoulos, G. D. (1991). The receptor for ciliary neurotrophic factor. Science 253, 59-63.
6. Taga, T., Hibi, M., Hirata, Y., Yamasaki, K., Yasukawa, K., Matsuda, T., Hirando, T., and Kishimoto, T. (1989). Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130. Cell (Cambridge: Mass.) 58, 573-581.
7. Hibi, M., Murakami, M., Saito, M., Hirano, T., Taga, T., and Kishimoto, T. (1990). Molecular cloning and expression of an IL6 signal transducer, gp130. Cell (Cambridge, Mass.) 63, 1149-1157.
8. Davis, S., Aldrich, T. H., Ip, N. Y., Stahl, N., Scherer, S., Famiggella, T., DiStefano, P. S., Curtis, R., Panayotatos, N., Gascan, H., Chevalier, S., and Yancopoulos, G. D. (1993). Released form of CNTF receptor a component as a soluble mediator of CNTF responses. Science 259, 1736-1739.
9. Robledo, O., Fourcin, M., Chevalier, S., Guillet, C., Auguste, P., Pouplard-Barthelzix, A., Pennica, D., and Gascan, H. (1997). Signaling of the cardiotrophin-1 receptor. J. Biol. Chem. 272, 4855-4863.
10. Pennica, D., Arce, V., Swanson, T. A., Vejsada, R., Pollock, R. A., Armanini, M., Dudley, K., Phillips, H. S., Rosenthal, A., Kato, A. C., and Henderson, C. E. (1996). Cardiotrophin-1, a cytokine present in embryonic muscle, supports long-term survival of spinal motoneurons. Neuron 17, 63-74.
11. Nandurkar, H. H., Hilton, D. J., Nathan, P., Willson, T., Nicola, N., and Begley, C. G. (1996). The human IL-11 receptor requires gp130 for signalling: Demonstration by molecular cloning of the receptor. Oncogene 12, 585-593.
12. Cherel, M., Sorel, M., Lebeau, B., Dubois, S., Moreau, J. F., Bataille, R., Minvielle, S., and Jacques, Y. (1995). Molecular cloning of two isoforms of a receptor for the human hematopoietic cytokine interleukin-11. Blood 86, 2534-2540.
13. Neddermann, P., Graziani, R., Ciliberto, G., and Paonessa, G. (1996). Functional expression of soluble human interleukin-11 (IL-11) receptor a and stoichiometry of in vitro IL-11 receptor complexes with gp130. J. Biol. Chem. 271, 30986-30991.
14. Baumann, H., Wang, Y., Morella, K. K., Lai, C. F., Dams, H., Hilton, D. J., Hawley, R. G., and Mackiewicz, A. (1996). Complex of the soluble IL-11 receptor and IL-11 acts as IL-6-type cytokine in hepatic and nonhepatic cells. J. Immunol. 157, 284-290.
15. Gearing, D. P., Thut, C. J., VandenBos, T., Gimpel, S. D., Delaney, P. B., King, J., Price, V., Cosman, D., and Beckmann, M. P. (1991). Leukemia inhibitory factor receptor is structurally related to the IL-6 signal transducer, gp130. EMBO J. 10, 2839-2848.
16. Gearing, D. P., Comeau, M. R., Friend, D. J., Gimpel, S. D., Thut, C. J., McGourty, J., Brasher, K. K., King, J. A., Gillis, S., Mosley, B., Ziegler, S. F., and Cosman, D. (1992). The IL-6 signal transducer, gp130: An oncostatin M receptor and affinity converter for the LIF receptor. Science 255, 1434-1437.
17. Paonessa, G., Graziani, R., De Serio, A., Savino, R., Ciapponi, L., Lahm, A., Salvati, A. L., Toniatti, C., and Ciliberto, G. (1995). Two distinct and independent sites on IL-6 trigger gp130 dimer formation and signalling. EMBO J. 14, 1942-1951.
18. Sporeno, E., Paonessa, G., Salvati, A. L., Graziani, R., Delmastro, P., Ciliberto, G., and Toniatti, C. (1994). Oncostatin M binds directly to gp130 and behaves as interleukin-6 antagonist on a cell line expressing gp130 but lacking functional oncostatin M receptors. J. Biol. Chem. 269, 10991-10995.
19. Baumann, H., Ziegler, S. F., Mosley, B., Morella, K. K., Pajovic, S., and Gearing, D. P. (1993). Reconstitution of the response to leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor in hepatoma cells. J. Biol. Chem. 268, 8414-8417.
20. Gearing, D. P., Ziegler, S. F., Comeau, M. R., Friend, D., Thoma, B., Cosman, D., Park, L., and Mosley, B. (1994). Proliferative responses and binding properties of hematopoietic cells transfected with low-affinity receptors for leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor. Proc. Natl. Acad. Sci. U.S.A. 91, 1119-1123.
21. Davis, S., Aldrich, T. H., Stahl, N., Taga, T., Kishimoto, T., Ip, N. Y., and Yancopoulos, G. D. (1993). LIFRβ and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor. Science 260, 1805-1808.
22. Stahl, N., and Yancopoulos, G. D. (1993). The alphas, betas and kinases of cytokine receptor complexes. Cell (Cambridge, Mass.) 74, 587-590.
23. Murakami, M., Hibi, M., Nakagawa, N., Nakagawa, T., Yasukawa, K., Yamanishi, K., Taga, T., and Kishimoto, T. (1993). IL6-induced homodimerization of gp130 and associated activation of a tyrosine kinase. Science 260, 1808-1810.
24. Mosley, B., De Imus, C., Friend, D., Boiani, N., Thoma, B., Park, L. S., and Cosman, D. (1996). Dual Oncostatin M (OSM) receptors. J. Biol. Chem. 271, 32635-32643.
25. Pennica, D., Shaw, K. J., Swanson, T. A., Moore, M. W., Shelton, D. L., Zioncheck, K. A., Rosenthal, A., Taga, T., Paoni, N. F., and Wood, W. I. (1995). Cardiotrophin-1. Biological activities and binding to the leukemia inhibitory factor receptor/gp130 signaling complex. J. Biol. Chem. 270, 10915-10922.
26. Ip, N. Y., Li, Y., van de Stadt, I., Panayotatos, N., Alderson, R. F., and Lindsay, R. M. (1991). Ciliary neurotrophic factor enhances neuronal survival in rat hippocampal cultures. J. Neurosci. 11, 3124-3134.
27. Stahl, N., and Yancopoulos, G. D. (1994). The tripartite CNTF receptor complex: Activation and signaling involves components shared with other cytokines. J. Neurobiol. 25, 1454-1466.
28. Ip, N. Y., McClain, J., Barrezueta, N. X., Aldrich, T. H., Pan, L., Li, Y., Wiegand, S. J., Friedman, B., Davis, S., and Yancopoulos, G. D. (1993). The α chain of the CNTF receptor is required for signalling and defines potential CNTF targets in the adult and during development. Neuron 10, 89-102.
29. Bellido, T., Stahl, N., Farruggella, T. J., Borba, V., Yancopoulos, G. D., and Manolagas, S. C. (1996). Detection of receptors for interleukin-6, interleukin-11, leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor in bone marrow stromal/ osteoblastic cells. J. Clin. Invest. 97, 431-437.
30. Frieling, J. T., Sauerwein, R. W., Wijdenes, J., Hendriks, T., and van der Linden, C. J. (1994). Soluble interleukin 6 receptor in biological fluids from human origin. Cytokine 6, 376-381.
31. Narazaki, M., Yasukawa, K., Saito, T., Ohsugi, Y., Fukui, J., Koishihara, Y., Yancopoulos, G. D., Taga, T., and Kishimoto, T. (1993). Soluble forms of the interleukin-6 signal-transducing receptor component gp130 in human serum possessing a potential to inhibit signals through membrane-anchored gp130. Blood 82, 1120-1126.
32. Gaillard, J.-P., Bataille, R., Brailly, H., Zuber, C., Yasukawa, K., Attal, M., Maruo, N., Taga, T., Kishimoto, T., and Klein, B. (1993). Increased and highly stable levels of functional soluble interleukin-6 receptor in sera of patients with monoclonal gammopathy. Eur. J. Immunol. 23, 820-824.
33. Honda, M., Yamamoto, S., Cheng, M., Yasukawa, K., Suzuki, H., Saito, T., Osugi, Y., Tokunaga, T., and Kishimoto, T. (1992). Human soluble IL-6 receptor: Its detection and enhanced release by HIV infection. J. Immunol. 148, 2175-2180.
34. Frieling, J. T., van Deuren, M., Wijdenes, J., van der Meer, J. W., Clement, C., van der Linden, C. J., and Sauerwein, R. W. (1995). Circulating interleukin-6 receptor in patients with sepsis syndrome. J. Infect. Dis. 171, 469-472.
35. Kopf, M., Baumann, H., Freer, G., Freudenberg, M., Lamers, M., Kishimoto, T., Zinkernagel, R., Bluethmann, H., and Kohler, G. (1994). Impaired immune and acute-phase responses in interleukin-6 deficient mice. Nature (London) 368, 339-342.
36. DeChiara, T. M., Vejsada, R., Poueymirou, W. T., Acheson, A., Suri, C., Conover, J. C., Friedman, B., McClain, J., Pan, L., Stahl, N., Ip, N. Y., Kato, A., and Yancopoulos, G. D. (1995). Mice lacking the CNTF receptor, unlike mice lacking CNTF, exhibit profound motor neuron deficits at birth. Cell (Cambridge, Mass.) 83, 313-322.
37. Yoshida, K., Taga, T., Saito, M., Suematsu, S., Kumanogoh, A., Tanaka, T., Fujiwara, H., Hirata, M., Yamagami, T., Nakahata, T., Hirabayashi, T., Yoneda, Y., Tanaka, K., Wang, W. Z., Mori, C., Shiota, K., Yoshida, N., and Kishimoto, T. (1996). Targeted disruption of gp130, a common signal transducer for the interleukin 6 family of cytokines, leads to myocardial and hematological disorders. Proc. Natl. Acad. Sci. U.S.A. 93, 407-411.
38. Ware, C. B., Horowitz, M. C., Renshaw, B. R., Hunt, J. S., Liggit, D., Koblar, S. A., Gliniak, B. C., McKenna, H. J., Papayannopoulou, T., Thoma, B., Cheng, L., Donovan, P. J., Peschon, J. J., Bartlett, P. F., Willis, C. R., Wright, B. D., Carpenter, M. K., Davison, B. L., and Gearing, D. P. (1995). Targeted disruption of the low-affinity leukemia inhibitory factor receptor gene causes placental, skeletal, neural and metabolic defects and results in perinatal death. Development (Cambridge, UK) 121, 1283-1299.
39. Ward, L. D., Howlett, G. J., Discolo, G., Yasukawa, K., Hammacher, A., Moritz, R. L., and Simpson, R. J. (1994). High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor, and gp130. J. Biol. Chem. 269, 23286-23289.
40. Ward, L. D., Hammacher, A., Howlett, G. J., Matthews, J. M., Fabri, L., Moritz, R. L., Nice, E. C., Weinstock, J., and Simpson, R. J. (1996). Influence of interleukin-6 (IL-6) dimerization on formation of the high affinity hexameric IL-6-receptor complex. J. Biol. Chem. 271, 20138-20144.
41. De Serio, A., Graziani, R., Laufer, R., Ciliberto, G., and Paonessa, G. (1995). In vitro binding of ciliary neurotrophic factor to its receptors: Evidence for the formation of an IL-6-type hexameric complex. J. Mol. Biol. 254, 795-800.
42. Simpson, R. J., Hammacher, A., Smith, D. K., Matthews, J. M., and Ward, L. D. (1997). Interleukin-6: Structure-function relationships. Protein Sci. 6, 929-955.
43. de Vos, A. M., Ultsch, M., and Kossiakoff, A. A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
44. Savino, R., Lahm, A., Salvati, A. L., Ciapponi, L., Sporeno, E., Altamura, S., Paonessa, G., Toniatti, C., and Ciliberto, G. (1994). Generation of interleukin-6 receptor antagonists by molecular-modeling guided mutagenesis of residues important for gp130 activation. EMBO J. 13, 1357-1367.
45. Savino, R., A., L., Giorgio, M., Cabibbo, A., Tramontano, A., and Ciliberto, G. (1993). Saturation mutagenesis of the human interleukin 6 receptor-binding site: Implications for its three-dimensional structure. Proc. Natl. Acad. Sci. U.S.A. 90, 4067-4071.
46. Kruse, N., Tony-H.-P., and Sebald, W. (1992). Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid-replacement. EMBO J. 11, 3237-3244.
47. Panayotatos, N., Radziejewska, E., Acheson, A., Pearsall, D., Thadani, A., and Wong, V. (1993). Exchange of a single amino acid interconverts the specific activity and gel mobility of human and rat ciliary neurotrophic factors. J. Biol. Chem. 268, 19000-19003.
48. Murakami, M., Narazaki, M., Hibi, M., Yawata, H., Yasukawa, K., Hamaguchi, M., Taga, T., and Kishimoto, T. (1991). Critical cytoplasmic region of the interleukin 6 signal transducer gp130 is conserved in the cytokine receptor family. Proc. Natl. Acad. Sci. U.S.A. 88, 11349-11353.
49. Ip, N. Y., Nye, S. N., Boulton, T. G., Davis, S., Taga, T., Li, Y., Birren, S. J., Yasukawa, K., Kishimoto, T., Anderson, D. J., Stahl, N., and Yancopoulos, G. D. (1992). CNTF and LIF act on neuronal cells via shared signalling pathways that involve the IL-6 signal transducing receptor component gp130. Cell (Cambridge, Mass.) 69, 1121-1132.
50. Stahl, N., Davis, S., V., W., Taga, T., Kishimoto, T., Ip, N. Y., and Yancopoulos, G. D. (1993). Crosslinking of CNTF and LIF to endogenous and reconstructed receptor complexes identifies LIF binding protein as a CNTF receptor component. J. Biol. Chem. 268, 7628-7631.
51. Velazquez, L., Fellous, M., Stark, G. R., and Pellegrini, S. (1992). A protein kinase in the interferon α/β signaling pathway. Cell (Cambridge, Mass.) 70, 313-322.
52. Watling, D., Guschin, D., Muller, M., Silvennoinen, O., Witthuhn, B. A., Quelle, F. W., Rogers, N. C., Schindler, C., Stark, G. R., Ihle, J. N., and Kerr, I. M. (1993). Complementation by the protein tyrosine kinase JAK2 of a mutant cell line defective in the interferon-γ signal transduction pathway. Nature (London) 366, 166-170.
53. Muller, M., Briscoe, J., Laxton, C., Guschin, D., Ziemiecki, A., Silvennoinen, O., Harpur, A. G., Barbieri, G., Witthuhn, B. A., Schindler, C., Pellegrini, S., Wilks, A. F., Ihle, J. N., Stark, G. R., and Kerr, I. M. (1993). The protein tyrosine kinase JAK1 complements defects in interferon-α/β and -γ signal transduction. Nature (London) 366, 129-135.
54. Witthuhn, B. A., Quelle, F. W., Silvennoinen, O., Yi, T., Tang, B., Miura, O., and Ihle, J. N. (1993). JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell (Cambridge, Mass.) 74, 227-236.
55. Argetsinger, L. S., Campbell, G. S., Yang, X., Witthuhn, B. A., Silvennoinen, O., Ihle, J. N., and Carter-Su, C. (1993). Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell (Cambridge, Mass.) 74, 237-244.
56. Stahl, N., Boulton, T. G., Farruggella, T., Ip, N. Y., Davis, S., Witthuhn, B., Quelle, F. W., Silvennoinen, O., Barbieri, G., Pellegrini, S., Ihle, J. N., and Yancopoulos, G. D. (1994). Association and activation of Jak-Tyk kinases by CNTF-LIF-OSM-IL6 β receptor components. Science 263, 92-95.
57. Lütticken, C., Wegenka, U. M., Yuan, J., Buschmann, J., Schindler, C., Ziemiecki, A., Harpur, A. G., Wilks, A. F., Yasukawa, K., Taga, T., Kishimoto, T., Barbieri, G., Pellegrini, S., Sendtner, M., Heinrich, P. C., and Horn, F. (1994). Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130. Science 263, 89-92.
58. Rui, H., Kirken, R. A., and Farrar, W. L. (1994). Activation of receptor-associated tyrosine kinase Jak2 by prolactin. J. Biol. Chem. 269, 5364-5368.
59. c chains with Jak1 and Jak3: Implications for XSCID and XCID. Science 266, 1042-1044.
60. Miyazaki, T., Kawahara, A., Fujii, H., Nakagawa, Y., Minami, Y., Liu, Z.-J., Oishi, I., Silvennoinen, O., Witthuhn, B. A., Ihle, J. N., and Taniguchi, T. (1994). Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. Science 266, 1045-1047.
61. Nicholson, S. E., Oates, A. C., Harpur, A. G., Ziemiecki, A., Wilks, A. F., and Layton, J. E. (1994). Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation. Proc. Natl. Acad. Sci., U.S.A. 91, 2958-2988.
62. tyk2, and interferon-α-activated tyrosine kinase, is physically associated with and interferon-α receptor. J. Biol. Chem. 269, 3518-3522.
63. Ziemiecki, A., Harpur, A. G., and Wilks, A. F. (1994). JAK protein tyrosine kinases: Their role in cytokine signalling. Trends Cell Biol. 4, 207-212.
64. Taniguchi, T. (1995). Cytokine signaling through nonreceptor protein tyrosine kinases. Science 268, 251-255.
65. Wilks, A. F., Harpur, A. G., Kurban, R. R., Ralph, S. J., Zurcher, G., and Ziemiecki, A. (1991). Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol. Cell. Biol. 11, 2057-2065.
66. Chen, M., Cheng, A., Chen, Y.-Q., Hymel, A., Hanson, E. P., Kimmel, L., Minami, Y., Taniguchi, T., Changelian, P. S., and O'Shea, J. J. (1997). The amino terminus of JAK3 is necessary and sufficient for binding to the common γ chain and confers the ability to transmit interleukin 2-mediated signals. Proc. Natl. Acad. Sci. U.S.A. 94, 6910-6915.
67. c chain. J. Biol. Chem. 270, 13814-13818.
68. Tanner, J. W., Chen, W., Young, R. L., Longmore, G. D., and Shaw, A. S. (1995). The conserved box 1 motif of cytokine receptors is required for association with JAK kinases. J. Biol. Chem. 270, 6523-6530.
69. Murata, T., Noguchi, P. D., and Puri, R. K. (1995). Receptors for interleukin (IL)-4 do not associate with the common gamma chain, and IL-4 induces the phosphorylation of JAK2 tyrosine kinase in human colon carcinoma cells. J. Biol. Chem. 270, 30829-30836.
70. Stahl, N., Farruggella, T. J., Boulton, T. G., Zhong, Z., Darnell, J. E., and Yancopoulos, G. D. (1995). Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors. Science 267, 1349-1353.
71. Noguchi, M., Yi, H., Rosenblatt, H. M., Filipovitch, A. H., Adelstein, S., Modi, W. S., McBride, O. W., and Leonard, W. J. (1993). Interleukin-2 receptor γ chain mutation results in X-linked severe combined immunodeficiency in humans. Cell (Cambridge, Mass.) 73, 147-157.
72. Kitamura, T., Sato, N., Arai, K.-I., and Miyajima, A. (1991). Expression cloning of the human IL-3 receptor cDNA reveals a shared β subunit for the human IL-3 and GM-CSF receptors. Cell (Cambridge, Mass.) 66, 1165-1174.
73. Nicholson, S. E., Novak, U., Ziegler, S. F., and Layton, J. E. (1995). Distinct regions of the granulocyte colon-stimulating factor receptor are required for tyrosine phosphorylation of the signaling molecules JAK2, Stat3, and p42, p44MAPK. Blood 86, 3698-3704.
74. Tanaka, N., Asao, H., Ohbo, K., Ishii, N., Takeshita, T., Nakamura, M., Sasaki, H., and Sugamura, K. (1994). Physical association of JAK1 and JAK2 tyrosine kinases with the interleukin 2 receptor beta and gamma chains. Proc. Natl. Acad. Sci. U.S.A. 91, 7271-7275.
75. Yin, T., Tsan, M. L.-S., and Yang, Y.-C. (1994). JAK1 kinase forms complexes with interleukin-4 receptor and 4PS/Insulin receptor substrate-1-like protein and is activated by interleukin-4 and interleukin-9 in T lymphocytes. J. Biol. Chem. 269, 26614-26617.
76. van der Geer, P., Hunter, T., and Lindberg, R. A. (1994). Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol. 10, 251-337.
77. Glass, D. J., Bowen, D. C., Stitt, T. N., Radziejewski, C., Bruno, J., Ryan, T. E., Gies, D. R., Shah, S., Mattsson, K., Burden, S. J., DiStefano, P. S., Valenzuela, D. M., DeChiara, T. M., and Yancopoulos, G. D. (1996). Agrin acts via a MuSK receptor complex. Cell (Cambridge, Mass.) 85, 513-523.
78. Sanicola, M., Hession, C., Worley, D., Carmillo, P., Ehrenfels, C., Walus, L., Robinson, S., Jaworski, G., Wei, H., Tizard, R., Whitty, A., Pepinsky, R. B., and Cate, R. L. (1997). Glial cell line-derived neurotrophic factor-dependent RET activation can be mediated by two different cell-surface accessory proteins. Proc. Natl. Acad. Sci. U.S.A. 94, 6238-6243.
79. Darnell, J. E., Kerr, I. M., and Stark, G. R. (1994). Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264, 1415-1421.
80. Decker, T., Lew, D. J., Mirkovitch, J., and Darnell, J. E., Jr. (1991). Cytoplasmic activation of GAF, an IFN-γ-regulated DNA-binding factor. EMBO J. 10, 927-932.
81. Schindler, C., Shuai, K., Prezioso, V. R., and Darnell, J. E., Jr. (1992). Interferon-dependent tyrosine phosphorylation of a latent cytoplasmic transcription factor. Science 257, 809-813.
82. Shuai, K., Schindler, C., Prezioso, V. R., and Darnell, J. E., Jr. (1992). Activation of transcription by IFN-γ: Tyrosine phosphorylation of a 91-kDa binding protein. Science 258, 1808-1812.
83. Fu, X. Y., Schindler, C., Improta, T., Aebersold, R., and Darnell, J. E., Jr. (1992). The proteins of ISGF-3, the interferon α-induced transcriptional activator, define a gene family involved in signal transduction. Proc. Natl. Acad. Sci. U.S.A. 89, 7840-7843.
84. Schindler, C., Fu, X., Improta, T., Aebersold, R., and Darnell, J. E. (1992). Proteins of transcription factor ISGF-3: One encodes the 91- and 84-kDa ISGF-3 proteins that are activated by interferon α. Proc. Natl. Acad. Sci. U.S.A. 89, 7836-7839.
85. Zhong, Z., Wen, Z., and Darnell, J. E. (1994). Stat3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264, 95-98.
86. Shuai, K., Horvath, C. M., Huang, L. H. T., Qureshi, S. A., Cowburn, D., and Darnell, J. E., Jr. (1994). Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell (Cambridge, Mass.) 76, 821-828.
87. Schindler, C. and Darnell, J. E., Jr. (1995). Transcriptional responses to polypeptide ligands: The JAK-STAT pathway. Annu. Rev. Biochem. 64, 621-651.
88. Akira, S., Nishio, Y., Inoue, M., Wang, X.-J., Wei, S., Matsusaka, T., Yoshida, K., Sudo, T., Naruto, M., and Kishimoto, T. (1994). Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway. Cell (Cambridge, Mass.) 77, 63-71.
89. Yamamoto, K., Quelle, F. W., Thierfelder, W. E., Kreider, B. L., Gilbert, D. J., Jenkins, N. A., Copeland, N. G., Silvennoinen, O., and Ihle, J. N. (1994). Stat4, a novel gamma interferon activation site-binding protein expressed in early myeloid differentiation. Mol. Cell. Biol. 14, 4342-4349.
90. Wakao, H., Gouilleux, F., and Groner, B. (1994). Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response. EMBO J. 13, 2182-2191.
91. Hou, J., Schindler, U., Henzel, W. J., Ho, T. G., Brasseur, M., and McKnight, S. L. (1994). An interleukin-4-induced transcription factor: IL-4 Stat. Science 265, 1701-1706.
92. Pawson, T., and Gish, G. D. (1992). SH2 and SH3 domains: From structure to function. Cell (Cambridge, Mass.) 71, 359-362.
93. Wegenka, U. M., Lutticken, C., Buschmann, J., Yuan, J., Lottspeich, F., Muller-Esterl, W., Schinkler, C., Roeb, E., Heinrich, P. C., and Horn, F. (1994). The interleukin-6-activated acute-phase response factor is antigenically and functionally related to members of the signal transducer and activator of transcription (STAT) family. Mol. Cell. Biol. 14, 3186-3196.
94. Tian, S. S., Lamb, P., Seidel, H. M., Stein, R. B., and Rosen, J. (1994). Rapid activation of the STAT3 transcription factor by granulocyte colony-stimulating factor. Blood 84, 1760-1764.
95. Baumann, H., Morell, K. K., White, D. W., Dembski, M., Bailon, P. S., Kim, H., Lai, C.-F., and Tartaglia, L. A. (1996). The full-length leptin receptor has signaling capabilities of interleukin-6 cytokine receptors. Proc. Natl. Acad. Sci. U.S.A. 93, 8374-8378.
96. Thierfelder, W. E., van Deursen, J. M., Yamamoto, K., Tripp, R. A., Sarawar, S. R., Carson, R. T., Sangster, M. Y., Vignali, D. A. A., Doherty, P. C., Grosveld, G. C., and Ihle, J. N. (1996). Requirement for Stat4 in interleukin-12 mediated responses of natural killer and T cells. Nature (London) 382, 171-174.
97. Ihle, J. N. (1996). STATs: Signal transducers and activators of transcription. Cell (Cambridge, Mass.) 84, 331-334.
98. Takeda, K., Tanaka, T., Shi, W., Matsumoto, M., Minami, M., Kashiwamura, S.-I., Nakanishi, K., Yoshida, N., Kishimoto, T., and Akira, S. (1996). Essential role of Stat6 in IL-4 signalling. Nature (London) 380, 627-630.
99. Durbin, J. E., Hackenmiller, R., Simon, M. C., and Levy, D. E. (1996). Targeted disruption of the mouse Stall gene results in compromised innate immunity to viral disease. Cell (Cambridge, Mass.) 84, 443-450.
100. Meraz, M. A., White, J. M., Sheehan, K. C. F., Bach, E. A., Rodig, S. J., Dighe, A. S., Kaplan, D. H., Riley, J. K., Greenlund, A. C., Campbell, D., Carver-Moore, K., DuBois, R. N., Clark, R., Aguet, M., and Schreiber, R. D. (1996). Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway. Cell (Cambridge, Mass.) 84, 431-442.
101. Heim, M. K., Kerr, I. M., Stark, G. R., and Darnell, J. E. (1995). Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway. Science 267, 1347-1349.
102. Seidel, H. M., Milocco, L. H., Lamb, P., Darnell, J. E., Jr., Stein, R. B., and Rosen, J. (1995). Spacing of palindromic half sites as a determinanl of selective STAT (signal transducers and activators of transcription) DNA binding and transcriptional activity. Proc. Natl. Acad. Sci. U.S.A. 92, 3041-3045.
103. Kotanides, H., and Reich, N. C. (1996). Interleukin-4-induced STAT6 recognizes and activates a target site in the promoter of the interleukin-4 receptor gene. J. Biol. Chem. 271, 25555-25561.
104. Schindler, U., Wu, P., Rothe, M., Brasseur, M., and McKnight, S. L. (1995). Components of Stat recognition code: Evidence for two layers of molecular selectivity. Immunity 2, 689-697.
105. Boulton, T. G., Zhong, Z., Wen, Z., Darnell, J. E., Jr., Stahl, N., and Yancopoulos, G. D. (1995). STAT3 activation by cytokines utilizing gp130 and related transducers involves a secondary modification requiring an H7-sensitive kinase. Proc. Natl. Acad. Sci. U.S.A. 92, 6915-6919.
106. Zhang, X., Blenis, J., Li, H.-C., Schindler, C., and Chen-Kiang, S. (1995). Requirement of serine phosphorylation for formation of STAT-promoter complexes. Science 267, 1990-1994.
107. Wen, Z., Zhong, Z., and Darnell, J. E., Jr. (1995). Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. Cell (Cambridge, Mass.) 82, 241-250.
108. Boulton, T. G., Stahl, N., and Yancopoulos, G. D. (1994). Ciliary neurotrophic factor/ leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induces tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors. J. Biol. Chem. 269, 11648-11655.
109. David, M., Petricoin, E., III, Benjamin, C., Pine, R., Weber, M. J., and Larner, A. C. (1995). Requirement for MAP kinase (ERK2) activity in interferon α-and interferon β-stimulated gene expression through STAT proteins. Science 269, 1721-1723.
110. Korzus, E., Nagase, H., Rydell, R., and Travis, J. (1997). The mitogen-activated protein kinase and JAK-STAT signaling pathways are required for an oncostatin M-responsive element-mediated activation of matrix metalloproteinase 1 gene expression. J. Biol. Chem. 272, 1188-1196.
111. Fukuda, T., Hibi, M., Yamanaka, Y., Yakahasi-Tezuka, M., Fujilani, Y., Tamaguchi, T., Nakajima, K., and Hirano, T. (1996). Two signals are necessary for cell proliferation induced by a cytokine receptor gp130: Involvement of STAT3 in anti-apoptosis. Immunity 5, 449-460.
112. Greenlund, A. C., Farrar, M. A., Viviano, B. L., and Schreiber, R. D. (1994). Ligand induced IFNγ receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). EMBO J. 13, 1591-1600.
113. Tartaglia, L. A., Dembski, M., Weng, X., Deng, N., Culpepper, J., Devos, R., Richards, G. J., Campfield, L. A., Clark, F. T., Deeds, J., Muir, C., Sanker, S., Moriarty, A., Moore, K. J., Smutko, J. S., Mays, G. G., Woolf, E. A., Monroe, C. A., and Tepper, R. I. (1995). Identification and expression cloning of a leptin receptor, OB-R. Cell (Cambridge, Mass.) 83, 1263-1271.
114. Drachman, J. G., and Kaushansky, K. (1997). Dissecting the thrombopoietin receptor: Functional elements of the Mpl cytoplasmic domain. Proc. Natl. Acad. Sci. U.S.A. 94, 2350-2355.
115. Greenlund, A. C., Morales, M. O., Viviano, B. L., Yan, H., Krolewski, J., and Schreiber, R. D. (1995). Stat recruitment by tyrosine-phosphorylated cytokine receptors: An ordered reversible affinity-driven process. Immunity 2, 677-687.
116. Gerhartz, C., Heesel, B., Sasse, J., Hemmann, U., Landgraf, C., Schneider-Mergener, J., Horn, F., Heinrich, P. C., and Graeve, L. (1996). Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130. II. Src homology SH2 domains define the specificity of STAT factor activation. J. Biol. Chem. 271, 12991-12998.
117. Klingmuller, U., Lorenz, U., Cantley, L. C., Neel, B. G., and Lodish, H. F. (1995). Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of Jak2 and termination of proliferative signals. Cell (Cambridge, Mass.) 80, 729-738.
118. D'Ambrosio, D., Hippen, K. L., Minskoff, S. A., Mellman, I., Pani, G., Siminovitch, K. A., and Cambier, J. C. (1995). Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by FcγRIIB1. Science 268, 293-297.
119. Ali, S., Chen, Z., Lebrun, J.-J., Vogel, W., Kharitonenkov, A., Kelly, P. A., and Ullrich, A. (1996). PTP1D is a positive regulator of the prolactin signal leading to β-casein promoter activation. EMBO J. 15, 135-142.
120. Lechleider, R. J., Freeman, R. M., and Neel, B. G. (1993). Tyrosyl phosphorylation and growth factor association of the human corkscrew homologue, SH-PTP2. J. Biol. Chem. 268, 13434-13438.
121. Kharitonenkov, A., Schnekenburger, J., Chen, Z., Knyazev, P., Sli, S., Zwick, E., White, M., and Ullrich, A. (1995). Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction. J. Biol. Chem. 270, 29189-29193.
122. David, M., Zhou, G., Pine, R., Dixon, J. E., and Larner, A. C. (1996). The SH2 domain-containing tyrosine phosphatase PTP1D is required for interferon α/β-induced gene expression. J. Biol. Chem. 271, 15862-15865.
123. Lechleider, R. J., Freemen, R. M., and Neel, B. G. (1993). Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2. J. Biol. Chem. 268, 13434-13438.
124. Li, W., Nishimura, R., Kashishian, A., Batzer, A. G., Kim, W. J., Cooper, J. A., and Schlessinger, J. (1994). A new function for a phosphotyrosine phosphatase: Linking GRB2-Sos to a receptor tyrosine kinase. Mol. Cell. Biol. 14, 509-517.
125. Pluskey, S., Wandless, T. J., Walsh, C. T., and Shoelson, S. E. (1995). Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains. J. Biol. Chem. 270, 2897-2900.
126. Symes, A., Stahl, N., Reeves, S. A., Farruggella, T., Servidei, T., Gearan, T., Yancopoulos, G. D., and Fink, J. S. (1997). The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression. Curr. Biol. 7, 697-700.
127. Carpenter, L. R., Symes, A., Farruggella, T. J., Karow, M., Yancopoulos, G. D., and Stahl, N. (1997). Enhancing leptin response by preventing SHP-2 interaction with ObR. Proc. Natl. Acad. Sci. U.S.A. 95, 6061-6066.
128. Servidei, T., Aoki, Y., Lews, S. E., Symes, A., Fink, J. S., and Reeves, S. A. (1998). Coordinate regulation of STAT signaling and c-fos expression by the tyrosine phosphatase SHP-2. J. Biol. Chem. 273, 6233-6241.
129. Starr, R., Wilson, T. A., Viney, E. M., Murray, L. J. L., Rayner, J. R., Jenkins, B. J., Gonda, T. J., Alexander, W. S., Metcalf, D., Nicola, N. A., and Hilton, D. J. (1997). A family of cytokine-inducible inhibitors of signalling. Nature (London) 387, 917-921.
130. Endo, T. A., Masuhara, M., Yokouchi, M., Suzuki, R., Sakamoto, H., Mitsui, K., Matsumoto, A., Tanimura, S., Ohtsubo, M., Misawa, H., Miyazaki, T., Leonor, N., Taniguchi, T., Fujita, T., Kanakura, Y., Komiya, S., and Yoshimura, A. (1997). A new protein containing an SH2 domain that inhibits JAK kinases. Nature (London) 387, 921-924.
131. Naka, T., Narazaki, M., Hirata, M., Matsumoto, T., Minamoto, S., Aono, A., Nishimoto, N., Kajita, T., Taga, T., Yoshizaki, K., Akira, S., and Kishimoto, T. (1997). Structure and function of a new STAT-induced STAT inhibitor. Nature (London) 387, 924-928.
132. Kim, T. K., and Maniatis, T. (1996). Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273, 1714-1719.
133. Haspel, R. L., Salditt-Georgieff, M., and Darnell, J. E., Jr. (1996). The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase. EMBO J. 15, 6262-6268.
134. Yu, C.-L., and Burakoff, S. J. (1997). Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation. J. Biol. Chem. 272, 14017-14020.
135. Fountoulakis, M., Mesa, C., Schmid, G., Gentz, R., Manneberg, M., Zulauf, M., Dembic, Z., and Garotta, G. (1995). Interferon γ receptor extracellular domain expressed as IgG fusion protein in Chinese hamster ovary cells. J. Biol. Chem. 270, 3958-3964.
136. Economides, A., Yancopoulos, G. D., and Stahl, N. (1997). Unpublished data.
137. Livnah, O., Stura, E. A., Johnson, D. L., Middleton, S. A., Mulcahy, L. S., Wrighton, N. C., Dower, W. J., Jolliffe, L. K., and Wilson, I. A. (1996). Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å. Science 273, 464-471.
138. Cwirla, S. E., Balasubramanian, P., Duffin, D. J., Wagstrom, C. R., Gates, C. M., Singer, S. C., Davis, A. M., Tansik, R. L., Mattheakis, L. C.,