The Janus kinase family of protein tyrosine kinases and their role in signaling

Cellular and Molecular Life Sciences

Volumn 55, Issue 12, 1999, Pages 1523-1534

  Yeh, T C ^a   Pellegrini, S ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

Cytokine; JAK; Protein tyrosine kinase; Receptor; Signaling; STAT

Indexed keywords

CYTOKINE; INTERFERON; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE;

AMINO TERMINAL SEQUENCE; CELL MUTANT; HOST RESISTANCE; KNOCKOUT MOUSE; MOUSE; NONHUMAN; REVIEW; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

ANIMALS; CYTOKINES; HUMANS; INTERFERONS; MICE; MICE, KNOCKOUT; PROTEIN-TYROSINE KINASES; SIGNAL TRANSDUCTION;

EID: 0032863261     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050392     Document Type: Review

References (143)

1. Pellegrini S. and Dusanter-Fourt I. (1997) The structure, regulation and function of the Janus kinases (JAKs) and signal transducer and activators of transcription (STATs). Eur. J Biochem. 248: 615-633
2. Duhe R. J. and Farrar W. L. (1998) Structural and mechanistic aspects of Janus kinases: how the two-faced god wields a double-edged sword. J. Interferon Cytokine Res. 18: 1-15
3. Binari R. and Perrimon N. (1994) Stripe-specific regulation of pair-rule genes by hopscotch, a putative Jak family tyrosine kinase in Drosophila. Genes Dev. 8: 300-312
4. Harrison D. A., McCoon P. E., Binari R., Gilman M. and Perrimon N. (1998) Drosophila unpaired encodes a secreted protein that activates the JAK signaling pathway. Genes Dev. 12: 3252-3263
5. Kawata T., Shevchenko A., Fukuzawa M., Jermyn K. A., Totty N. F., Zhukovskaya N. V. et al. (1997) SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk cell differentiation in Dictyostelium. Cell 89: 909-916
6. Wang Y. and Levy D. E. (1999) Molecular cloning and characterization of a STAT homologue in C. elegans (abstract). Keystone Symposium. Specificity in Signal Transduction
7. Nicola N. A. (1994) Guidebook to cytokines and their receptors, Oxford University Press, Oxford
8. Bazan J. F. (1990) Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87: 6934-6938
9. Thoreau C., Petridou B., Kelly P. A., Djiane J. and Mornon J.-P. (1991) Structural symmetry of the extracellular domain of the cytokine/growth hormone/prolactin receptor family and interferon receptors revealed by hydrophobic cluster analysis FEBS Lett. 282: 16-31
10. Livnah O., Stura E. A., Middleton S. A., Johnson D. L., Jolliffe L. K. and Wilson I. A. (1999) Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283: 987-990
11. Remy I., Wilson I. A. and Michnick S. W. (1999) Erythropoietin receptor activation by a ligand-induced conformation change. Science 283: 990-993
12. 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
13. Schindler C and Darnell J. E. Jr (1995) Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu. Rev. Biochem. 64: 621-651
14. Ihle J. N. and Kerr I. M. (1995) Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet. 11: 69-74
15. Leaman D. W., Leung S., Li X. and Stark G. R. (1996) Regulation of STAT-dependent pathways by growth factors and cytokines. FASEB J. 10: 1578-1588
16. Novak U., Harpur A. G., Paradiso L., Kanagasundaram V., Jaworowski A., Wilks A. F. et al. (1995) Colony-stimulating factor 1-induced STAT1 and STAT3 activation is accompanied by phosphorylation of Tyk2 in macrophages and Tyk2 and JAK1 in fibroblasts. Blood 86: 2948-2956
17. Leaman D. W., Pisharody S., Flickinger T. W., Commane M. A., Schlessinger J., Kerr I. M. et al. (1996) Roles of JAKs in activation of STATs and stimulation of c-fos gene expression by epidermal growth factor. Mol. Cell. Biol. 16: 369-375
18. Vignais M. L., Sadowski H. B., Watling D., Rogers N. C. and Gilman M. (1996) Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins. Mol. Cell. Biol. 16: 1759-1769
19. Gual P., Baron V., Lequoy V. and Van Obberghen E. (1998) Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor. Endocrinology 139: 884-893
20. Marrero M. B., Schieffer B., Paxton W. G., Heerdt L., Berk B. C., Delafontaine P. et al. (1995) Direct stimulation of Jak/STAT pathway by the angiotensin II ATI receptor. Nature 375: 247-250
21. 2A receptor coupled to the Jak/STAT pathway. J. Biol. Chem. 272: 14825-14829
22. Buggy J. J. (1998) Binding of α-melanocyte-stimulating hormone to its G-protein-coupled receptor on B-lymphocytes activates the Jak/STAT pathway. Biochem. J. 331: 211-216
23. Ali M. S., Sayeski P. P., Dirksen L. B., Hayzer D. J., Marrero M. B. and Bernstein K. E. (1997) Dependence on the motif YIPP for the physical association of Jak2 kinase with the intracellular carboxyl tail of the angiotensin II ATI receptor. J. Biol. Chem. 272: 23382-23388
24. Guo D. Q., Dunbar J. D., Yang C. H., Pfeffer L. M. and Donner D. B. (1998) Induction of Jak/STAT signaling by activation of the type I TNF receptor. J. Immunol. 160: 2742-2750
25. Gatsios P., Terstegen L., Schliess F., Haussinger D., Kerr I. M., Heinrich P. C. et al. (1998) Activation of the Janus kinase/signal transducer and activator of transcription pathway by osmotic shock. J. Biol. Chem. 273: 22962-22968
26. Skov S., Nielsen M., Bregenholt S., Odum N. and Claesson M. H. (1998) Activation of Stat-3 is involved in the induction of apoptosis after ligation of major histocompatibility complex class I molecules on human jurkat T cells. Blood 91: 3566-3573
27. Hanissian S. H. and Geha R. S. (1997) Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells. Immunity 6: 379-387
28. Riedy M. C., Dutra A. S., Blake T. B., Modi W., Lal B. K., Davis J. et al. (1996) Genomic sequence, organization, and chromosomal localization of human JAK3. Genomics 37: 57-61
29. Gurniak C. B., Thomis D. C. and Berg L. J. (1997) Genomic structure and promoter region of the murine Janus-family tyrosine kinase, Jak3. DNA Cell Biol. 16: 85-94
30. Frank S. J., Yi W., Zhao Y., Goldsmith J. F., Gilliland G., Jiang J. et al. (1995) Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor. J. Biol. Chem. 270: 14776-14785
31. Velazquez L., Mogensen K. E., Barbieri G., Fellous M., Uze G. and Pellegrini S. (1995) Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon-alpha/beta and for signal transduction. J. Biol. Chem. 270: 3327-3334
32. Zhao Y., Wagner F., Frank S. J. and Kraft A. S. (1995) The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor βc chain. J. Biol. Chem. 270: 13814-13818
33. Chen M., Cheng A., Chen Y., Hymel A., Hanson E. P., Kimmel L. et al. (1997) The amino terminus of Jak3 is necessary and sufficient for binding to the common γ chain and confers ability to transmit interleukin 2-mediated signals. Proc. Natl. Acad. Sci. USA 94: 6910-6915
34. Yan H., Piazza F., Krishnan K., Pine R. and Krolewski J. J. (1998) Definition of the interferon-α receptor-binding domain on the Tyk2 kinase. J. Biol. Chem. 273: 4046-4051
35. Richter M. F., Duménil G., Uzé G., Fellous M. and Pellegrini S. (1998) Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon α/β receptor component IFNAR1. J. Biol. Chem. 273: 24723-24729
36. Cacalano N. A., Migone T. S., Bazan F., Hanson E. P., Chen M., Candotti F. et al. (1999) Autosomal SCID caused by a point mutation in the N-terminus of Jak3: mapping of the Jak3-receptor interaction domain. EMBO J. 18: 1549-1558
37. Kohlhuber F., Rogers N. C., Watling D., Feng J., Guschin D., Briscoe J. et al. (1997) A JAK1 JAK2 chimera can sustain alpha and gamma interferon responses. Mol. Cell. Biol. 17: 695-706
38. Bernards A. (1991) Predicted tyk2 protein contains two tandem protein kinase domains. Oncogene 6: 1185-1187
39. Bork P. and Gibson T. J. (1996) Applying motif and profile searches. Methods Enzymol. 266: 162-184
40. Girault J. A., Labesse G., Mornon J. P. and Callebaut I. (1999) The amino termini of FAK and JAKs are divergent members of the band 4.1 family. Trends Biochem. Sci. 24: 54-57
41. Arpin M., Algrain M. and Louvard D. (1994) Membrane actin microfilament connections: an increasing diversity of players related to band 4.1. Curr. Opin. Cell Biol. 6: 136-141
42. Tsukita S., Yonemura S. and Tsukita S. (1997) ERM (ezrin/radixin/moesin) family from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9: 70-75
43. Chishti A. H., Kim A. C., Marfatia S. M., Lutchman M., Hanspal M., Jindal H. et al. (1998) The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem. Sci. 23: 281-282
44. Girault J. A., Labesse G., Mornon J. P. and Callebaut I. (1999) JAKs and FAKs play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction. Mol. Med. 4: 751-769
45. Macchi P., Villa A., Gillani S., Sacco M. G., Frattini A., Porta F. et al. (1995) Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature 377: 65-68
46. 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
47. Luo H., Hanratty W. P. and Dearolf C. R. (1995) An amino acid substitution in the Drosophila hopTum-1 Jak kinase causes leukemia-like hematopoietic defects. EMBO J. 14: 1412-1420
48. Tsukita S. and Yonemura S. (1997) ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22: 53-58
49. Zhu T., Goh E. L. and Lobie P. E. (1998) Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. J. Biol. Chem. 273: 10682-10689
50. Miyazaki T., Takaoka A., Nogueira L., Dikic I., Fujii H., Tsujino S. et al. (1998) Pyk2 is a downstream mediator of the IL-2 receptor-coupled Jak signaling pathway. Genes Dev. 12: 770-775
51. 1007 in the kinase activation loop. Mol. Cell. Biol. 17: 2497-2501
52. Quelle F. W., Thierfelder W., Witthuhn 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
53. Duhe R. J. and Farrar W. L. (1995) Characterization of active and inactive forms of the JAK 2 protein-tyrosine kinase produced via the baculovirus expression vector system. J. Biol. Chem. 270: 23084-23089
54. Briscoe J., Rogers N. C., Witthuhn B. A., Watling D., Harpur A. G., Wilks A. F. et al. (1996) Kinase-negative mutants of JAK1 can sustain interferon-gamma-inducible gene expression but not an antiviral state. EMBO J. 15: 799-809
55. Gauzzi M. C., Velazquez L., McKendry R., Mogensen K. E., Fellous M. and Pellegrini S. (1996) Interferon-alpha-dependent activation or Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. J. Biol.Chem. 271: 20494-20500
56. Sakai I., Nabell L. and Kraft A. S. (1995) Signal transduction by a CD16/CD7/Jak2 fusion protein. J. Biol. Chem. 270: 18420-18427
57. Luo H., Rose P., Barber D., Hanratty W. P., Lee S., Roberts T. M. et al. (1997) Mutation in Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways. Mol. Cell. Biol. 17: 1562-1571
58. Candotti F., Oakes S. A., Johnston J. A., Giliani S., Schumacher R. F., Mella P. et al. (1997) Structural and functional basis for JAK3-deficient severe combined immunodeficiency. Blood 90: 3996-4003
59. Schwaller J., Frantsre J., Aster J., Williams I. R., Tomasson M. H., Ross T. S. et al. (1998) Transformation of hematopoietic cell lines to growth-factor independence and induction of a fatal myclo- and lymphoproliferative disease in mice by retrovirally transduced TEL/JAK2 fusion genes. EMBO J. 17: 5321-5333
60. Wang Y. D., Wong K. and Wood W. I. (1995) Intracellular tyrosine residues of the human growth hormone receptor are not required for the signaling of proliferation or Jak-STAT activation. J. Biol. Chem. 270: 7021-7024
61. Nicholson S. E., Starr R., Novak U., Hilton D. J. and Layton J. E. (1996) Tyrosine residues in the granulocyte colony-stimulating factor (G-CSF) receptor mediate G-CSF-induced differentiation of murine myeloid leukemic (MI) cells. J. Biol. Chem. 271: 26947-26953
62. Goupille O., Daniel N., Bignon C., Jolivet G. and Djiane J. (1997) Prolactin signal transduction to milk protein genes: carboxy-terminal part of the prolactin receptor and its tyrosine phosphorylation are not obligatory for JAK2 and STAT5 activation. Mol. Cell. Endocrinol. 127: 155-169
63. Fujitani Y., Hibi M., Fukuda T., Takahashi-Tezuka M., Yoshida H., Yamaguchi T. et al. (1997) An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT. Oncogene 14: 751-761
64. Barahmand-Pour F., Meinke A., Groner B. and Decker T. (1998) Jak2-Stat5 interactions analyzed in yeast. J. Biol. Chem. 273: 12567-12575
65. Flores-Morales A., Pircher T. J., Silvennoinen O., Gustafsson J. A., Sanchez-Gomez M., Norstedt G. et al. (1998) In vitro interaction between STAT5 and JAK2: dependence upon phosphorylation status of STAT5 and JAK2. Mol. Cell. Endocrinol. 138: 1-10
66. Ram P. A. and Waxman D. J. (1997) Interaction of growth hormone-activated STATs with SH2-containing phosphotyrosine phosphatase SHP-1 and nuclear JAK2 tyrosine kinase. J. Biol. Chem. 272: 17694-17702
67. Fish E. N., Uddin S., Korkmaz. M., Majchrzak B., Druker B. J. and Platanias L. C. (1999) Activation of a CrkL-Stat5 signaling complex by type I interferons. J. Biol Chem. 274: 571-573
68. Hubbard S. R., Mohammadi M. and Schlessinger J. (1998) Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem. 273: 11987-11990
69. Zhou Y.-J., Hanson E. P., Chen Y.-Q., Agnuson K., Chen M., Swann P. G. et al. (1997) Distinct tyrosine phosphorylation sites in JAK3 kinase domain positively and negatively regulate its enzymatic activity. Proc. Acad. Natl. Sci. USA 94: 13850-13855
70. Gauzzi M. C., Barbieri G., Richter M. F., Uzé G., Ling L., Fellous M. et al. (1997) The amino-terminal region of Tyk2 sustains the level of interferon α receptor 1, a component of the interferon α/β receptor. Proc. Natl. Acad. Sci. USA 94: 11839-11844
71. Liu K. D., Gaffen S. L., Goldsmith M. A. and Greene W. C. (1997) Janus kinases in interleukin 2-mediated signaling: JAK1 and JAK3 are differentially regulated by tyrosine phosphorylation. Curr. Biol. 7: 817-826
72. Shimoda K., Feng J., Murakami H., Nagata S., Walling D., Rogers N. C. et al. (1997) Jak1 plays an essential role for receptor phosphorylation and Stat activation in response to granulocyte colony-stimulating factor. Blood 90: 597-604
73. Kotenko S. V., Izotova L. S., Pollack B. P., Muthukumaran G., Paukku K., Silvennoinen O. et al. (1996) Other kinases can substitute for Jak2 in signal transduction by interferon-gamma. J. Biol. Chem. 271: 17174-17182
74. Saltzman A., Stone M., Franks C., Searfoss G., Munro R., Jaye M. et al. (1998) Cloning and characterization of human Jak-2 kinase: high mRNA expression in immune cells. Biochem. Biophys. Res. Commun. 246: 627-633
75. Yoshimura A., Ohkubo T., Kiguchi T., Jenkins N. A., Gilbert D. J., Copeland N. G. et al. (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
76. Starr R., Wilson T. A., Viney E. M., Murray L. J., Rayner J. R., Jenkins B. J. et al. (1997) A family of cytokine-inducible inhibitors of signalling. Nature 387: 917-921
77. Endo T. A., Masuhara M., Yokouchi M., Suzuki R., Sakamoto H., Mitsui K. et al. (1997) A new protein containing an SH2 domain that inhibits JAK kinases. Nature 387: 921-924
78. Naka T., Narazaki M., Hirata M., Matsumoto T., Minamoto S., Aono A. et al. (1997) Structure and function of a new STAT-induced STAT inhibitor. Nature 387: 924-929
79. Auernhammer C. J., Chesnokova V., Bousquet C. and Melmed S. (1998) Pituitary corticotroph SOCS-3-novel intracellular regulation of leukemia-inhibitory factor-mediated proopiomelanocortin gene expression and adrenocorticotropin secretion. Mol. Endocrinol. 12: 954-961
80. Bjorback C., Elmquist J. K., Frantz J. D., Shoelson S. E. and Flier J. S. (1998) Identification of SOCS-3 as a potential mediator of central leptin resistance. Mol. Cell 1: 619-625
81. Adams T. E., Hansen J. A., Starr R., Nicola N. A., Hilton D. J. and Billestrup N. (1998) Growth hormone preferentially induces the rapid, transient expression of SOCS-3, a novel inhibitor of cytokine receptor signaling. J. Biol. Chem. 273: 1285-1287
82. Thiel S., Behrmann I., Dittrich E., Muys L., Tavernier J., Wijdenes J. et al. (1998) Internalization of the interleukin 6 signal transducer gp130 does not require activation of the Jak/STAT pathway. Biochem. J. 330: 47-54
83. Heinrich P. C., Berhrmann I., Müller-Newen G., Schaper F. and Graeve L. (1998) Interleukin-6-type cytokine signaling through the gp130/Jak/STAT pathway. Biochem. J. 334: 297-314
84. Hochstrasser M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30: 405-439
85. Kim T. K. and Maniatis T. (1996) Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273: 1717-1719
86. Strous G. J., Kerkhof P. van, Govers R., Rotwein P. and Schwartz A. L. (1997) Growth hormone-induced signal transduction depends on an intact ubiquitin system. J. Biol. Chem. 272: 40-43
87. 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
88. Callus B. A. and Mathey-Prevot B. (1998) Interleukin-3-induced activation of the JAK/STAT pathway is prolonged by proteasome inhibitors. Blood 91: 3182-3192
89. Jaster R., Zhu Y., Pless M., Bhattacharya S., Mathey-Prevot B. and D'Andrea A. D. (1997) JAK2 is required for induction of the murine DUB-1 gene. Mol. Cell. Biol. 17: 3364-3372
90. Tonks N. K. and Nell B. G. (1996) From form to function: signaling by protein tyrosine phosphatases. Cell 87: 365-368
91. Yi T., Mui A. L.-F., Krystal G. and Ihle J. N. (1993) Hematopoietic cell phosphatase associates with the interleukin-3 (IL3) receptor β chain and down regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol. Cell. Biol. 13: 7577-7586
92. Klingmuller U., Lorenz U., Cantley L. C., Nell B. G. and Lodish H. F. (1995) Specific recruitment of the hematopoietic protein tyrosine phosphatase SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80: 729-738
93. Migone T.-S., Cacalano N. A., Taylor N., Yi T., Waldmann T. A. and Johnston J. A. (1998) Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor: loss of SHP-1 expression in human T-lymphotropic virus type 1-transformed T cells. Proc. Natl. Acad. Sci. USA 95: 3845-3850
94. Kim H., Hawley T. S., Hawley R. G. and Bauman H. (1998) Protein tyrosine phosphatase 2 (SHP-2) moderates signaling by gp130 but is not required for the induction of acute-phase plasma protein genes in hepatic cells. Mol. Cell. Biol. 18: 1525-1533
95. Fernandez L., Flores-Morales A., Lahuna O., Sliva D., Norstedt G., Haldosen L.-A. et al. (1998) Desensitization of the growth hormone-induced Janus kinase 2 (Jak2)/Signal transducer and activator of transcription 5 (Stat5) signaling pathway requires protein synthesis and phospholipase C. Endocrinology 139: 1815-1824
96. David M., Petricoin E. 3rd and Larner A. C. (1996) Activation of protein kinase A inhibits interferon induction of the Jak/Stat pathway in U266 cells. J. Biol. Chem. 271: 4585-4588
97. Sengupta T. K., Schmitt E. M. and Ivashkiv L. B. (1996) Inhibition of cytokines and JAK-STAT activation by distinct signaling pathways. Proc. Natl. Acad. Sci. USA 93: 9499-9504
98. Duhe 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 95: 126-131
99. Rodig S., Meraz M. A., White J. M., Lampe P. A., Riley J. K., Arthur C. D. et al. (1998) Disruption of the Jak1 gene demonstrates obligatory and non redundant roles of the Jaks in cytokine-induced biologic responses. Cell 93: 373-383
100. Neubauer H., Cumano A., Müller M., Wu H., Huffstadt U. and Pfeffer K. (1998) Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 93: 397-409
101. Parganas E., Wang D., Stravopodis D., Topham D., Marine J.-C., Teglund D. J. et al. (1998) Jak2 is essential for signaling through a variety of cytokine receptors. Cell 93: 385-395
102. Nosaka T., Deursen J. M. A. van, Witthuhn B. A., McMickle A. P., Doherty P. C., Grosveld G. C. et al. (1995) Defective lymphoid development in mice lacking Jak3. Science 270: 800-802
103. Park S. Y., Saijo K., Takahashi T., Osawa M., Arase H., Hirayama N. et al. (1995) Developmental defects of lymphoid cells in Jak3 kinase-deficient mice. Immunity 3: 771-782
104. 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
105. Di Santo J. P., Müller W., Guy-Grand D., Fisher A. and Rajewsky K. (1995) Lymphoid development in mice with a targeted deletion of the interleukin-2 receptor γ chain. Proc. Natl. Acad. Sci. USA 92: 377-381
106. Cao X., Shores E. W., Hu-Li J., Anver M. R., Kelsall B. L., Russell S. M. et al. (1995) Defective lymphoid development in mice lacking expression of the common cytokine receptor γ chain. Immunity 2: 223-238
107. Eynon E. E., Kuida K. and Flavell R. (1996) Disruption of cytokine signaling in lymphoid development: unique contributions of the common cytokine gamma chain and the JAK3 kinase. J. Interferon Cytokine Res. 16: 677-684
108. Thomis D. C. and Berg L. J. (1997) The role of Jak3 in lymphoid development, activation, and signaling. Curr. Opin. Immunol. 9: 541-547
109. Baird A. M., Thomis D. C. and Berg L. J. (1998) T cell development and activation in Jak3-deficient mice. J. Leukoc. Biol. 63: 669-677
110. Saijo K., Park S. Y., Ishida Y., Arase H. and Saito T. (1997) Crucial role of Jak3 in negative selection of self-reactive T cells. J. Exp. Med. 185: 351-356
111. Notarangelo L. D. (1996) Immunodeficiencies caused by genetic defects in protein kinases. Curr. Opin. Immunol. 8: 448-453
112. Russell S. M., Tayebi N., Nakajima H., Riedy M. C. Roberts J. L., Aman M. J. et al. (1995) Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. Science 270: 797-800
113. Lacronique V., Boureux A., Valle V. D., Poirel H., Quang C. T., Mauchauffe M. et al. (1997) A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science 278: 1309-1312
114. Peeters P., Raynaud S. D., Cools J., Wlodarska I., Grosgeorge J., Philip P. et al. (1997) Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia. Blood 90: 2535-2540
115. Migone T. S., Lin J. X., Cereseto A., Mulloy J. C., O'Shea J. J., Franchini G. et al. (1995) Constitutively activated Jak-STAT pathway in T cells transformed with HTLV-I. Science 269; 79-81
116. Lee Y. H. and Yun Y. (1998) HBx protein of hepatitis B virus activates Jak1-STAT signaling. J. Biol. Chem. 273: 25510-25515
117. Danial N. N., Pernis A. and Rothman P. B. (1995) Jak-STAT signaling induced by the v-abl oncogene. Science 269: 1875-1877
118. Danial N. N., Losman J. A., Lu T., Yip N., Krishnan K., Krolewski J. et al. (1998) Direct interaction of Jak1 and v-Abl is required for v-Abl-induced activation of STATs and proliferation. Mol. Cell. Biol. 18: 6795-6804
119. Zhu M., Berry J. A., Russell S. M. and Leonard W. J. (1998) Delineation of the regions of interleukin-2 (IL-2) receptor β chain important for association of Jak1 and Jak3. J. Biol. Chem. 273: 10719-10725
120. Lobic P. E., Ronsin B., Sivennoinen O., Haldosén L.-A., Norstedt G. and Morel G. (1996) Constitutive nuclear localization of Janus kinases 1 and 2. Endocrinology 137: 4037-4045
121. Yetter A., Uddin S., Krolewski J. J., Jiao H., Yi T. and Platanias L. (1995) Association of the interferon-dependent tyrosine kinase Tyk2 with the hematopoietic cell phosphatase. J. Biol. Chem. 270: 18179-18182
122. Jiao H., Berrada K., Yang W., Tabrizi M., Platanias L. C. and Yi T. (1996) Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain containing protein tyrosine phosphatase SHP-1. Mol. Cell. Biol. 16: 6985-6992
123. Tabrizi M., Yang W., Jiao H., Devries H., Platanias L. C., Arico M. et al. (1998) Reduced Tyk2 SHP-1 interaction and lack of SHP-1 mutation in a kindred of familial hemophagocytic lymphohistiocytosis. Leukemia 12: 200-206
124. Fuhrer D. K., Feng G. and Yang Y. (1995) Syp associates with gp130 and Janus kinase 2 in response to interleukin-11 in 3T3-L1 adipocytes. J. Biol. Chem. 270: 24826-24830
125. Ali S., Chen Z., Lebrun J. J., Vogel W., Kharitonenkov A., Kelly P. A. et al. (1996) PTPID is a positive regulator of the prolactin signal leading to beta-casein promoter activation EMBO J. 15: 135-142
126. Yin T., Shen R., Feng G.-S. and Yang Y.-C. (1997) Molecular characterisation of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases. J. Biol. Chem. 272: 1032-1037
127. Kim S.-O., Jiang J., Yi W., Feng G.-S. and Frank S. J. (1998) Involvement of the Src homology 2 containing tyrosine phosphatase SHP-2 in growth hormone signaling. J. Biol. Chem. 273: 2344-2354
128. Xia K., Mukhopadhyay N. K., Inborn R. C, Barber D. L., Rose P. E., Lee R. S. et al. (1996) The cytokine-activated tyrosine kinase JAK2 activates Raf-1 in a p21ras-dependent manner. Proc. Natl. Acad. Sci. USA 93: 11681-11686
129. Stancato L. F., Sakatsume M., David M., Dent P., Dong F., Petricoin E. F. et al. (1997) Beta interferon and oncostatin M activate Raf-1 and mitogen-activated protein kinase through a JAK1-dependent pathway. Mol. Cell. Biol. 17: 3833-3840
130. Zong C., Yan R., August A., Darnell J. E. and Hanafusa H. (1996) Unique signal transduction of Eyk: constitutive stimulation of the JAK-STAT pathway by an oncogenic receptor-type tyrosine kinase. EMBO J. 15: 4515-4525
131. Uddin S., Sher D. A., Alsayed Y., Pons S., Colamonici O. R., Fish E. et al. (1997) Interaction of p59 Tyn with interferon-activated Jak kinases. Biochem. Biophys. Res. Commun. 235: 83-88
132. Takahashi-Tezuka M., Hibi M., Fujitani Y., Fukada T., Yumaguchi T. and Hirano T. (1997) Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through JAK. Oncogene 14: 2273-2282
133. Flati V., Haque S. J. and Williams B. R. G. (1996) Interferon-α-induced phosphorylation and activation of cytosolic phospholipase A2 is required for the formation of interferon-stimulated gene factor three. EMBO J. 15; 1566-1571
134. VanderKuur J., Allevato G., Billestrup N., Norstedt G. and Carter-Su C. (1995) Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SH association with Grb2. J. Biol. Chem. 270: 7587-7593
135. Giordano V., De Falco G., Chiari R., Quinto I., Pelicci P. G., Bartholomew L. et al. (1997) She mediates IL-6 signaling by interacting with gp130 and Jak2 kinase J. Immunol 158:4097-4103
136. Chauhan D., Kharbanda S. M., Ogata A., Urashima M., Frank D. and Malik N. (1995) Oncostatin M induces association of Grb2 with Janus kinas JAK2 in multiple myeloma cells. J. Exp. Med. 182; 1801-1806
137. Uddin S., Gardziola C., Dangat A., Yi T. and Platanias L. C. (1996) Interaction of the c-cbl proto-oncogene product with the Tyk2 protein tyrosine kinase, Biochem. Biophys. Res. Commun. 225: 833-838
138. Ahmad S., Alsayed Y. M., Druker B. J. and Platanias L. C. (1997) The type I Interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein. J. Biol. Chem. 272: 29991-29994
139. Uddin S., Sweet M., Colamonici O. R., Krolewski J. J. and Platanias L. C. (1997) The var proto-oncogene product (p95 vav) interacts with the Tyk2 protein tyrosine kinase. FEBS Lett. 403: 31-34
140. Platanias L. C., Uddin S., Yetter A., Sun X. J. and White M. F. (1996) The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2. J. Biol. Chem. 271: 278-282
141. Takeshita T., Arita T., Higuchi M., Asao H., Endo K., Kuroda H. et al. (1997) STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction. Immunity 6: 449-457
142. Giorgetti-Peraldi S., Peyrade F., Baron V. and Van Obberghen E. (1995) Involvement of Janus kinases in the insulin signaling pathway. Eur. J. Biochem. 234: 656-660
143. Takaoka A., Tanaka N., Mitani Y., Miyazaki T., Fujii H., Sato M. et al. (1999) Protein tyrosine kinase Pyk2 mediates the Jak-dependent activation of MAPK and Stat1 in IFN-α but not IFN-α, signaling. EMBO J. 18: 2480-2488