Structural and mechanistic aspects of Janus kinases: How the two-faced god wields a double-edged sword

Journal of Interferon and Cytokine Research

Volumn 18, Issue 1, 1998, Pages 1-15

  Duhe R J ^a,b   Farrar, W L ^b  

^a SAIC FREDERICK INC   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

JAK BINDING PROTEIN; JANUS KINASE; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

JANUS;

EID: 0031931647     PISSN: 10799907     EISSN: None     Source Type: Journal    
DOI: 10.1089/jir.1998.18.1     Document Type: Review

References (129)

1. 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 phosphotransferse-related catalytic domain, define a new class of protein kinase. Mol. Cell. Biol. 11, 2057-2065.
2. Editors. (1997). Janus. In: The New Encyclopaedia Britannica, 15th ed., Encyclopedia Britannica, Inc., Chicago, IL, 6, 496.
3. IHLE, J.N. (1994). The Janus kinase family and signaling through members of the cytokine receptor superfamily. Proc. Soc. Exp. Biol. Med. 206, 268-272.
4. IHLE, J.N., WITTHUHN, B.A., QUELLE, F.W., YAMAMOTO, K., THIERFELDER, W.E., KREIDER, B., and SILVENNOINEN, O. (1994). Signaling by the cytokine receptor superfamily: JAKs and STATs. TIBS 19, 222-227.
5. FIRMBACH-KRAFT, I., BYERS, M., SHOWS, T., DALLAFAVERA, R., and KROWEWSKI, J.J. (1990). tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene 5, 1329-1336.
6. VELAZQUEZ, L., FELLOUS, M., STARK, G.R., and PELLEGRINI, S. (1992). A protein tyrosine kinase in the interferon α/β signaling pathway. Cell 70, 313-322.
7. HARPUR, A.G., ANDRES, A.-C., ZIEMIECKI, A., ASTON, R.R., and WILKS, A.F. (1992). JAK2, a third member of the JAK family of protein tyrosine kinases. Oncogene 7, 1347-1353.
8. DUHÉ, R.J., RUI, H., GREENWOOD, J.D., GARVEY, K., and FARRAR, W.L. (1995). Cloning of the gene encoding rat JAK2, a protein tyrosine kinase. Gene 158, 281-285.
9. KAWAMURA, M., McVICAR, D.W., JOHNSTON, J.A., BLAKE, T.B., CHEN, Y.-Q., LAL, B.K., LLOYD, A.R., KELVIN, D.J., STAPLES, J.E., ORTALDO, J.R., and O'SHEA, J.J. (1994). Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase expressed in natural killer cells and activated leukocytes. Proc. Natl. Acad. Sci. USA 91, 6374-6378.
10. TAKAHASHI, T., and SHIRASAWA, T. (1994). Molecular cloning of rat JAK3, a novel member of the JAK family of protein tyrosine kinases. FEBS Lett. 342, 124-128.
11. BAZAN, J.F. (1990). Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87, 6934-6938.
12. COSMAN, D., LYMAN, S.D., IDZERDA, R.L., BECKMANN, M.P., PARK, L.S., GOODWIN, R.G., and MARCH, C.J. (1990). A new cytokine receptor superfamily. Trends Biochem. Sci. 15, 265-270.
13. COSMAN, D. (1993). The hematopoietin receptor superfamily. Cytokine 5, 95-106.
14. MÜLLER, 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 366, 129-135.
15. ARGETSINGER, L.S., CAMPBELL, G.S., YANG, X., WITTHUHN, B.A., SILVENNOINEN, O., IHLE, J.N., and CARTERSU, C. (1993). Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 74, 237-244.
16. 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 74, 227-236.
17. SILVENNOINEN, O., WITTHUHN, B.A., QUELLE, F.W., CLEVELAND, J.L., YI, T., and IHLE, J.N. (1993). Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. Proc. Natl. Acad. Sci. USA 90, 8429-8433.
18. 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.
19. LEBRUN, J.-J., ALI, S., SOFER, L., ULLRICH, A., and KELLY, P.A. (1994). Prolactin-induced proliferation of Nb2 cells involves tyrosine phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2. J. Biol. Chem. 269, 14021-14026.
20. NARAZAKI, M., WITTHUHN, B.A., YOSHIDA, K., SILVENNOINEN, O., YASUKAWA, K., IHLE, J.N., KISHIMOTO, T., and TAGA, T. (1994). Activation of JAK2 kinase mediated by the interleukin 6 signal transducer gp130. Proc. Natl. Acad. Sci. USA 91, 2285-2289.
21. STAHL, N., BOULTON, T.G., FARRUGGELLA, T., IP, N.Y., DAVIS, S., WITTHUHN, B.A., 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-IL-6 β receptor components. Science 263, 92-95.
22. WATLING, D., GUSCHIN, D., MÜLLER, 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 366, 166-170.
23. JOHNSTON, J.A., KAWAMURA, M., KIRKEN, R.A., CHEN, Y.-Q., BLAKE, T.B., SHIBUYA, K., ORTALDO, J.R., McVICAR, D.W., and O'SHEA, J.J. (1994). Phosphorylation and activation of the JAK-3 Janus kinase in response to interleukin-2. Nature 370, 151-153.
24. WITTHUHN, B.A., SILVENNOINEN, O., MIURA, O., LAI, K.S., CWIK, C., LIU, E.T., and IHLE, J.N. (1994). Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells. Nature 370, 153-157.
25. ZENG, Y.-X., TAKAHASHI, H., SHIBATA, M., and HIROKAWA, K. (1994). JAK3 Janus kinase is involved in interleukin 7 signal pathway. FEBS Lett. 353, 289-293.
26. MALABARBA, M.G., RUI, H., DEUTSCH, H.H.J., CHUNG, J., KALTOFF, F.S., FARRAR, W.L., and KIRKEN, R.A. (1996). Interleukin-13 is a potent activator of JAK3 and STAT6 in cells expressing interleukin-2 receptor-γ and interleukin-4 receptor-α. Biochem. J. 319, 865-872.
27. SILVENNOINEN, O., IHLE, J.N., SCHLESSINGER, J., and LEVY, D.E. (1993). Interferon-induced nuclear signalling by Jak protein tyrosine kinases. Nature 366, 583-585.
28. SHUAI, K., ZIEMIECKI, A., WILKS, A.F., HARPUR, A.G., SADOWSKI, H.B., GILMAN, M.Z., and DARNELL, J.E. (1993). Polypeptide signalling to the nucleus through phosphorylation of Jak and Stat proteins. Nature 366, 580-583.
29. HOU, J., SCHINDLER, U., HENZEL, W.J., HO, T.C., BRASSEUR, M., and McKNIGHT, S.L. (1994). An interleukin-4-induced transcription factor: IL-4 Stat. Science 265, 1701-1706.
30. IHLE, J.N. (1995). Cytokine receptor signalling. Nature 377, 591-594.
31. STAHL, N., and YANCOPOULOS, G.D. (1993). The alphas, betas, and kinases of cytokine receptor complexes. Cell 74, 587-590.
32. DARNELL, J.E., Jr., 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.
33. O'SHEA, J.J. (1997). Jaks, STATs, cytokine signal transduction, and immunoregulation: are we there yet? Immunity 7, 1-11.
34. WILKS, A.F., and OATES, A.C. (1996). The JAK/STAT pathway. Cancer Surv. 27, 139-163.
35. RUI, H., KIRKEN, R.A., MALABARBA, M.G., ERWIN, R.A., SCHABER, J.D., DUHÉ, R.J., LARNER, A.C., and FARRAR, W.L. (1997). Cell-dependent activation of tyrosine kinases JAK1, JAK2 and TYK2 by prolactin in human breast cancer and hematopoietic cell lines. Submitted for publication.
36. PARK, S.Y., SAIJO, K., TAKAHASHI, T., OSAWA, M., ARASE, H., HIRAYAMA, N., MIYAKE, K., NAKAUCHI, H., SHIRASAWA, T., and SAITO, T. (1995). Developmental defects of lymphoid cells in Jak3 kinase-deficient mice. Immunity 3, 771-782.
37. THOMIS, D.C., GURNIAK, C.B., TIVOL, E., SHARPE, A.H., and BERG, L.J. (1995). Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking Jak3. Science 270, 794-797.
38. NOSAKA, T., VAN DEURSEN, J.M.A., TRIPP, R.A., THIERFELDER, W.E., WITTHUHN, B.A., McMICKLE, A.P., DOHERTY, P.C., GROSVELD, G.C., and IHLE, J.N. (1995). Defective lymphoid development in mice lacking Jak3. Science 270, 800-802.
39. HEIM, M.H., KERR, I.M., STARK, G.R., and DARNELL, J.E., Jr. (1995). Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway. Science 267, 1347-1349.
40. STAHL, N., FARRUGGELLA, T.J., BOULTON, T.G., ZHONG, Z., DARNELL, J.E., Jr., and YANCOPOULOS, G.D. (1995). Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors. Science 267, 1349-1353.
41. QUELLE, F.W., SHIMODA, K., THIERFELDER, W., FISCHER, C., KIM, A., RUBEN, S.M., CLEVELAND, J.L., PIERCE, J.H., KEEGAN, A.D., NELMS, K., PAUL, W.E., and IHLE, J.N. (1995). Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in response to IL-4 and IL-3 but are not required for mitogenesis. Mol. Cell. Biol. 15, 3336-3343.
42. DURBIN, J.E., HACKENMILLER, R., SIMON, M.C., and LEVY, D.E. (1996). Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease. Cell 84, 443-450.
43. 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 SCHRIEBER, R.D. (1996). Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway. Cell 84, 431-442.
44. TAKEDA, K., NOGUCHI, K., SHI, W., TANAKA, T., MATSUMOTO, M., YOSHIDA, N., KISHIMOTO, T., and AKIRA, S. (1997). Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality. Proc. Natl. Acad. Sci. USA 94, 3801-3804.
45. KAPLAN, M.H., SUN, Y.-L., HOEY, T., and GRUSBY, M.J. (1996). Impaired IL-12 responses and enhanced development of Th2 cells in Stat4-deficient mice. Nature 382, 174-177.
46. LIU, X., ROBINSON, G.W., WAGNER, K.-U., GARRETT, L., WYNSHAW-BORIS, A., and HENNIGHAUSEN, L. (1997). Stat5a is mandatory for adult mammary gland development and lactogenesis. Genes Dev. 11, 179-186.
47. UDY, G.B., TOWERS, R.P., SNELL, R.G., WILKINS, R.J., PARK, S.-H., RAM, P.A., WAXMAN, D.J., and DAVEY, H.W. (1997). Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression. Proc. Natl. Acad. Sci. USA 94, 7239-7244.
48. TAKEDA, K., TANAKA, T., SHI, W., MATSUMOTO, M., MINAMI, M., KASHIWAMURA, S., NAKANISHI, K., YOSHIDA, N., KISHIMOTO, T., and AKIRA, S. (1996). Essential role of Stat6 in IL-4 signalling. Nature 380, 627-630.
49. SHIMODA, K., VAN DEURSEN, J., SANGSTER, M.Y., SARAWAR, S.R., CARSON, R.T., TRIPP, R.A., CHU, C., QUELLE, F.W., NOSAKA, T., VIGNALI, D.A.A., DOHERTY, P.C., GROSVELD, G., PAUL, W.E., and IHLE, J.N. (1996). Lack of IL-4-induced Th2 response and IgE class switching in mice with disrupted Stat6 gene. Nature 380, 630-633.
50. KAPLAN, M.H., SCHINDLER, U., SMILEY, S.T., and GRUSBY, M.J. (1996). Stat6 is required for mediating responses to IL-4 and for the development of Th2 cells. Immunity 4, 313-319.
51. DAVID, M., PETRICON, 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.
52. PARK, O.K., SCHAEFER, T.S., and NATHANS, D. (1996). In vitro activation of Stat3 by epidermal growth factor receptor kinase. Proc. Natl. Acad. Sci. USA 93, 13704-13708.
53. PFEFFER, L.M., MULLERSMAN, J.E., PFEFFER, S.R., MURTI, A., SHI, W., and YANG, C.H. (1997). STAT3 as an adaptor to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor. Science 276, 1418-1420.
54. KLINGMÜLLER, U., LORENZ, U., CANTLEY, L.C., NEEL, B.G., and LODISH, H.F. (1992). Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738.
55. JIAO, H., BERRADA, K., YANG, W., TABRIZI, M., PLATANIAS, L.C., and YI, T. (1996). Direct associationwith and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. Mol. Cell. Biol. 16, 6985-6992.
56. DUHÉ, R.J., EVANS, G.A., ERWIN, R.A., KIRKEN, R.A., COX, G.W., and FARRAR, W.L. (1998). Nitric oxide and thiol redox regulation of Janus kinase activity. Proc. Natl. Acad. Sci. USA (in press).
57. 1 receptor. Nature 375, 247-250.
58. CHANG, M.-S., CHANG, G.-D., LEU, J.-H., HUANG, F.-L., CHOU, C.-K., HUANG, C.-J., and LO, T.-B. (1996). Expression, characterization, and genomic structure of carp JAK1 kinase gene. DNA Cell Biol. 15, 827-844.
59. SMITH, L.C., and DAVIDSON, E.H. (1994). The echinoderm immune system: characters shared with vertebrate immune systems and characters arising later in deuterostome phylogeny. Ann NY Acad. Sci. 712, 213-226.
60. SUN, S.-C., LINDSTRÖM, BOMAN, H.G., FAYE, I., and SCHMIDT, O. (1990). Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 250, 1729-1732.
61. RIZKI, T.H., and RIZKI, R.M. (1994). Parasitoid-induced cellular immune deficiency in Drosophila. Ann. NY Acad. Sci. 712, 178-194.
62. BINARI, R., and PERRIMON, N. (1994). Stripe-specific regulation of pair-rule genes by hopscotch, a putative Jak family tyrosine kinse in Drosophila. Genes Dev. 8, 300-312.
63. YAN, R., LUO, H., DARNELL, J.E., Jr., and DEAROLF, C.R. (1996). A JAK-STAT pathway regulates wing vein formation in Drosophila. Proc. Natl. Acad. Sci. USA 93, 5842-5847.
64. BECRAFT, P.W., STINARD, P.S., and McCARTY, D.R. (1996). CRINKLY4: a TNFR-like receptor kinase involved in maize epidermal differentiation. Science 273, 1406-1409.
65. YANG, X., CHUNG, D., and CEPKO, C.L. (1993). Molecular cloning of the murine JAK1 protein tyrosine kinase and its expression in the mouse central nervous system. J. Neurosci. 13, 3006-3017.
66. CONWAY, G., MARGOLIATH, A., WONG-MADDEN, S., ROBERTS, R.J., and GILBERT, W. (1997). Jak1 kinase is required for cell migrations and anterior specification in zebrafish embryos. Proc. Natl. Acad. Sci. USA 94, 3082-3087.
67. SMITH, M.R., DUHÉ, R.J., LIU, Y.-L., and FARRAR, W.L. (1997). Microinjected cDNA encoding JAK2 protein-tyrosine kinase induces DNA synthesis in NIH 3T3 cells. FEBS Lett. 408, 327-330.
68. MEYDAN, N., GRUNBERGER, T., DADI, H., SHAHAR, M., ARPAIA, E., LAPIDOT, Z., LEEDER, J.S., FREEDMAN, M., COHEN, A., GAZIT, A., LEVITZKI, A., and ROIFMAN, C.M. (1996). Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature 379, 645-648.
69. HARRISON, D.A., BINARI, R., NAHREINI, T.S., GILMAN, M., and PERRIMON, N. (1995). Activation of a Drosophila Janus kinase (JAK) causes hematopoietic neoplasia and developmental defects. EMBO J. 14, 2857-2865.
70. DANIAL, N.N., PERNIS, A., and ROTHMAN, P.B. (1995). Jak-STAT signaling induced by the v-abl oncogene. Science 269, 1875-1877.
71. XU, X., KANG, S.-H., HEIDENREICH, O., OKERHOLM, M., O'SHEA, J.J., and NERENBERG, M.I. (1995). Constitutive activation of different Jak tyrosine kinases in human T cell leukemia virus type 1 (HTLV-1) Tax protein or virus-transformed cells. J. Clin. Invest. 96, 1548-1555.
72. MIGONE, T.-S., LIN, J.-X., CERESETO, A., MULLOY, J.C., O'SHEA, J.J., FRANCHINI, G., and LEONARD, W.J. (1995). Constitutively activated Jak-STAT pathway in T cells transformed with HTLV-1. Science 269, 79-81.
73. ZHUANG, H., NIU, Z., HE, T.-C., PATEL, S.V., and WOJCHOWSKI, D.M. (1995). Erythropoietin-dependent inhibition of apoptosis is supported by carboxyl-truncated receptor forms and blocked by dominant-negative forms of Jak2. J. Biol. Chem. 270, 14500-14504.
74. MACCHI, P., VILLA, A., GILIANI, S., SACCO, M.G., FRATTINI, A., PORTA, F., UGAZIO, A.G., JOHNSTON, J.A., CANDOTTI, F., O'SHEA, J.J., VEZZONI, P., and NOTARANGELO, L.D. (1995). Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature 377, 65-68.
75. GENETICS COMPUTER GROUP. (1994). Program manual for GCG package, version 8. Madison, Wisconsin.
76. HIGGINS, D.G., THOMPSON, J.D., and GIBSON, T.J. (1996). Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266, 383-402.
77. LOBIE, P.E., RONSIN, B., SILVENNOINEN, O., HALDOSÉN, L.-A., NORSTEDT, G., and MOREL, G. (1996). Constitutive nuclear localization of Janus kinases 1 and 2. Endocrinology 137, 4037-4045.
78. DOMANSKI, P., YAN, H., WITTE, M.M., KROWELSKI, J., and COLAMONICI, O.R. (1995). Homodimerization and intermolecular tyrosine phosphorylation of the Tyk-2 tyrosine kinase. FEBS Lett. 374, 317-322.
79. 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. USA 94, 6910-6915.
80. c chain. J. Biol. Chem. 270, 13814-13818.
81. FRANK, S.J., YI, W., ZHAO, Y., GOLDSMITH, J.F., GILLILAND, G., JIANG, J., SAKAI, I., and KRAFT, A.S. (1995). Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor. J. Biol. Chem. 270, 14776-14785.
82. 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.
83. tyk2 tyrosine kinase. Mol. Cell. Biol. 14, 8133-8142.
84. QUELLE, F.W., THIERFELDER, W., WITTUHN, B.A., TANG, B., COHEN, S., and IHLE, J.N. (1995). Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor. J. Biol. Chem. 270, 20775-20780.
85. ZHUANG, H., PATEL, S.V., HE, T.-C., SONSTEBY, S.K., NIU, Z., and WOJCHOWSKI, D.M. (1994). Inhibition of erythropoietin-induced mitogenesis by a kinase-deficient form of Jak2. J. Biol. Chem. 269, 21411-21414.
86. ZHUANG, H., PATEL, S.V., HE, T.-C., SONSTEBY, S.K., NIU, Z., and WOJCHOWSKI, D.M. (1994). Dominant negative effects of a carboxy-truncated Jak2 mutant on Epo-induced proliferation and Jak2 activation. Biochem. Biophys. Res. Commun. 204, 278-283.
87. DUHÉ, R.J., and FARRAR, W.L. (1995). Characterization of active and inactive forms of the JAK2 protein-tyrosine kinase produced via the baculovirus expression vector system. J. Biol. Chem. 270, 23084-23089.
88. VELAZQUEZ, L., MOGENSEN, K.E., BARBIERI, G., FELLOUS, M., UZÉ, G., and PELLEGRINI, S. (1995). Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon-α/β and for signal transduction. J. Biol. Chem. 270, 3327-3334.
89. LAI, K.S., JIN, Y., GRAHAM, D.K., WITTHUHN, B.A., IHLE, J.N., and LIU, E.T. (1995). A kinase-deficient splice variant of the human JAK3 is expressed in hematopoietic and epithelial cancer cells. J. Biol. Chem. 270, 25028-25036.
90. BRISCOE, J., ROGERS, N.C., WITTHUHN, B.A., WATLING, D., HARPUR, A.G., WILKS, A.F., STARK, G.R., IHLE, J.N., and KERR, I.M. (1996). Kinase-negative mutants of JAK1 can sustain interferon-γ-inducible gene expression but not an antiviral state. EMBO J. 15, 799-809.
91. GAUZZI, M.C., VELAZQUEZ, L., McKENDRY, R., MOGENSEN, K.E., FELLOUS, M., and PELLEGRINI, S. (1996). Interferon-α-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. J. Biol. Chem. 271, 20494-20500.
92. 1007 in the kinase activation loop. Mol. Cell. Biol. 17, 2497-2501.
93. LUO, H., ROSE, P., BARBER, D., HANRATTY, W.P., LEE, S., ROBERTS, T.M., D'ANDREA, A.D., and DEAROLF, C.R. (1997). Mutation in the Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways. Mol. Cell. Biol. 17, 1562-1571.
94. KAPLAN, D.H., GREENLUND, A.C., TANNER, J.W., SHAW, A.S., and SCHREIBER, R.D. (1996). Identification of an interferon-γ receptor α chain sequence required for JAK-1 binding. J. Biol. Chem. 271, 9-12.
95. YAN, H., KRISHNAN, K., LIM, J.T.E., CONTILLO, L.G., and KROLEWSKI, J.J. (1996). Molecular characterization of an alpha interferon receptor 1 subunit (IFNαR1) domain required for TYK2 binding and signal transduction. Mol. Cell. Biol. 16, 2074-2082.
96. VANDERKUUR, J.A., WANG, X., ZHANG, L., CAMPBELL, G.S., ALLEVATO, G., BILLESTRUP, N., NORSTEDT, G., and CARTER-SU, C. (1994). Domains of the growth hormone receptor required for association and activation of the JAK2 tyrosine kinase. J. Biol. Chem. 269, 21709-21717.
97. HACKETT, R.H., WANG, Y.-D., and LARNER, A.C. (1995). Mapping of the cytoplasmic domain of the human growth hormone receptor required for the activation of Jak2 and Stat proteins. J. Biol. Chem. 270, 21326-21330.
98. DASILVA, L., HOWARD, O.M.Z., RUI, H., KIRKEN, R.A., and FARRAR, W.L. (1994). Growth signaling and JAK2 association mediated by membrane-proximal cytoplasmic regions of prolactin receptors. J. Biol. Chem. 269, 18267-18270.
99. c chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region. Mol. Cell. Biol. 14, 4335-4341.
100. HE, T.-C., JIANG, N., ZHUANG, H., QUELLE, D.E., and WOJCHOWSKI, D.M. (1994). The extended Box 2 subdomain of erythropoietin receptor is nonessential for Jak2 activation yet critical for efficient mitogenesis in FDC-ER cells. J. Biol. Chem. 269, 18291-18294.
101. SOTIROPOULOS, A., PERROT-APPLANAT, M., DINERSTEIN, H., PALLIER, A., POSTEL-VINAY, M.-C., FINIDORI, J., and KELLY, P.A. (1994). Distinct cytoplasmic regions of the growth hormone receptor are required for activation of JAK2, mitogen-activated protein kinase, and transcription. Endocrinology 135, 1292-1298.
102. MALABARBA, M.G., KIRKEN, R.A., RUI, H., KOETTNITZ, K., KAWAMURA, M., O'SHEA, J.J., KALTHOFF, F.S., and FARRAR, W.L. (1995). Activation of JAK3, but not JAK1, is critical to interleukin-4 (IL4) stimulated proliferation and requires a membrane-proximal region of IL4 receptor α. J. Biol. Chem. 270, 9630-9637.
103. KIRKEN, R.A., RUI, H., MALABARBA, M.G., HOWARD, O.M.Z., KAWAMURA, M., O'SHEA, J.J., and FARRAR, W.L. (1995). Activation of JAK3, but not JAK1, is critical for IL-2-induced proliferation and STAT5 recruitment by a COOH-terminal region of the IL-2 receptor β-chain. Cytokine 7, 689-700.
104. HANKS, S.K., QUINN, A.M., and HUNTER, T. (1988). The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42-52.
105. YIN, T., SHEN, R., FENG, G.-S., and YANG, Y.-C. (1997). Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases. J. Biol. Chem. 272, 1032-1037.
106. TOSHIKAZU, T., ARITA, T., HIGUCHI, M., ASAO, H., ENDO, K., KURODA, H., TANAKA, N., MURATA, K., ISHII, N., and SUGAMURA, K. (1997). STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signalling for cell growth and c-myc induction. Immunity 6, 449-457.
107. 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., TANAGUCHI, T., FUJITA, T., KANAKURA, Y., KOMIYA, S., and YOSHIMURA, A. (1997). A new protein containing an SH2 domain that inhibits JAK kinases. Nature 387, 921-924.
108. STARR, R., WILLSON, 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 387, 917-921.
109. 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 387, 924-929.
110. YOSHIMURA, A., OHKUBA, T., KIGUCHI, T., JENKINS, N.A., GILBERT, D.J., COPELAND, N.G., HARA, T., and MIYAJIMA, A. (1995). A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. EMBO J. 14, 2816-2826.
111. NIELSEN, M., KALTOFT, K., NORDAHL, M., RÖPKE, C., GEISLER, C., MUSTELIN, T., DOBSON, P., SVEJGAARD, A., and ØDUM, A. (1997). Constitutive activation of a slowly migrating isoform of Stat3 in mycosis fungoides: tyrphostin AG490 inhibits Stat3 activation and growth of mycosis fungoides tumor cell lines. Proc. Natl. Acad. Sci. USA 94, 6764-6769.
112. 2 cells and mouse mammary gland explants. Proc. Natl. Acad. Sci. USA 91, 5232-5236.
113. HELDIN, C.-H. (1995). Dimerization of cell surface receptors in signal transduction. Cell 80, 213-223.
114. CUNNINGHAM, B.C., ULTSCH, M., DE VOS, A.M., MULKERRIN, M.G., CLAUSER, K.R., and WELLS, J.A. (1991). Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821-825.
115. 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.
116. GERTLER, A., GROSCLAUDE, J., STRASBURGER, C.J., NIR, S., and DJIANE, J. (1996). Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization. J. Biol. Chem. 271, 24482-24491.
117. LIVNAH, O., STURA, E.A., JOHNSON, D.L., MIDDLETON, S.A., MUCAHY, 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, 464-171.
118. WALTER, M.R., WINDSOR, W.T., NAGABHUSHAN, T.L., LUNDELL, D.J., LUNN, C.A., ZAUODNY, P.J., and NARULA, S.K. (1995). Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor. Nature 376, 230-235.
119. O'NEAL, K.D., and YU-LEE, L.-Y. (1993). The proline-rich motif (PRM): a novel feature of the cytokine/hematopoietin receptor superfamily. Lymphokine Cytokine Res. 12, 309-312.
120. 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 USA 88, 11349-11353.
121. NAKAMURA, Y., RUSSELL, S.M., MESS, S.A., FRIEDMANN, M., ERDOS, M., FRANCOIS, C., JAQUES, Y., ADELSTEIN, S., and LEONARD, W.J. (1994). Heterodimerization of the IL-2 receptor β- and γ-chain cytoplasmic domains is required for signalling. Nature 369, 330-333.
122. WATOWICH, S.S., HILTON, D.J., and LODISH, H.F. (1994). Activation and inhibition of erythropoietin receptor function: role of receptor dimerization. Mol. Cell. Biol. 14, 3535-3549.
123. STOMSKI, F.C., SUN, Q., BAGLEY, C.J., WOODCOCK, J., GOODALL, G., ANDREWS, R.K., BERNDT, M.C., and LOPEZ, R.K. (1996). Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor α- and β-chain heterodimerization, which is required for receptor activation but not high-affinity binding. Mol. Cell. Biol. 16, 3035-3046.
124. DAVIS, S., ALDRICH, T.H., STAHL, N., PAN, L., 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.
125. YI, W., KIM, S.-O., JINAG, J., PARK, S.-H., KRAFT, A.S., WAXMAN, D.J., and FRANK, S.J. (1996). Growth hormone receptor cytoplasmic domain differentially promotes tyrosine phosphorylation of signal transducers and activators of transcription 5b and 3 by activated JAK2 kinase. Mol. Endocrinol. 10, 1425-1443.
126. COLAMONICI, O.R., DOMANSKI, P., SWEITZER, S.M., LARNER, A., and BULLER, R.M.L. (1995). Vaccinia virus B18R gene encodes a type I interferon-binding protein that blocks interferon a transmembrane signaling. J. Biol. Chem. 270, 15974-15978.
127. HUBBARD, S.R., WEI, L., ELLIS, L., and HENDRICKSON, W.A. (1994). Crystal structure of the tyrosine kinae domain of the human insulin receptor. Nature 372, 746-754.
128. MOHAMMADI, M., SCHLESSINGER, J., and HUBBARD, S.R. (1996). Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86, 577-587.
129. PELLEGRINI, S., JOHN, J., SHEARER, M., KERR, I.M., and STARK, G.R. (1989). Use of a selectable marker regulated by alpha interferon to obtain mutations in the signaling pathway. Mol. Cell. Biol. 9, 4605-4612.