A model for assembly and activation of the GM-CSF, IL-3 and IL-5 receptors: Insights from activated mutants of the common β subunit

Experimental Hematology

Volumn 28, Issue 3, 2000, Pages 231-243

  D'Andrea, Richard J ^a,b   Gonda, Thomas J ^a,c  

^a HANSON INSTITUTE   (Australia)

^b UNIVERSITY OF ADELAIDE   (Australia)

^c INSTITUTE OF MEDICAL AND VETERINARY SCIENCE   (Australia)

Author keywords

Common subunit; Cytokine receptor; Erythropoietin; GM CSF; JAK kinase

Indexed keywords

CYTOKINE RECEPTOR; ERYTHROPOIETIN; ERYTHROPOIETIN RECEPTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR RECEPTOR; INTERLEUKIN 3 RECEPTOR; INTERLEUKIN 5 RECEPTOR; JANUS KINASE; RECEPTOR SUBUNIT;

CELL PROLIFERATION; DIMERIZATION; HEMATOPOIETIC CELL; HUMAN; HUMAN CELL; MODEL; MOUSE; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; REVIEW;

EID: 0034014714     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-472X(99)00159-9     Document Type: Article

References (116)

1. Miyajima A, Mui AL, Ogorochi T, Sakamaki K (1993) Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5. Blood 82:1960.
2. Bagley C.J., Woodcock J.M., Stomski F.C., Lopez A.F. The structural and functional basis of cytokine receptor activation. lessons from the common β subunit of the granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3) and IL-5 receptors Blood. 89:1997;1471.
3. Kitamura T., Hayashida K., Sakamaki K., Yokota T., Arai K., Miyajima A. Reconstitution of functional receptors for human granulocyte/macrophage colony-stimulating factor (GM-CSF). evidence that the protein encoded by the AIC2B cDNA is a subunit of the murine GM-CSF receptor Proc Natl Acad Sci U S A. 88:1991;5082.
4. Kitamura T., Miyajima A. Functional reconstitution of the human interleukin-3 receptor. Blood. 80:1992;84.
5. Hara T., Miyajima A. Two distinct functional high affinity receptors for mouse interleukin-3 (IL-3). EMBO J. 11:1992;1875.
6. Mui A.L., Miyajima A. Cytokine receptors and signal transduction. Prog Growth Factor Res. 5:1994;15.
7. Miyajima A., Kitamura T., Harada N., Yokota T., Arai K. Cytokine receptors and signal transduction. Ann Rev Immunol. 10:1992;295.
8. Wells J.A., de Vos A.M. Hematopoietic receptor complexes. Annu Rev Biochem. 65:1996;609.
9. Goodall G.J., Bagley C.J., Vadas M.A., Lopez A.F. A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands. Growth Factors. 8:1993;87.
10. Tartaglia L.A., Dembski M., Weng X., Deng N., Culpepper J., Devos R., Richards G.J., Campfield L.A., Clark F.T., Deeds J.et al. Identification and expression cloning of a leptin receptor, OB-R. Cell. 83:1995;1263.
11. Wilks A.F., Harpur A.G. Cytokine signal transduction and the JAK family of protein tyrosine kinases. Bioessays. 16:1994;313.
12. Ihle J.N. The Janus protein tyrosine kinase family and its role in cytokine signaling. Adv Immunol. 60:1995;1.
13. O'Shea J.J. Jaks, STATs, cytokine signal transduction and immunoregulation. are we there yet? Immunity. 7:1997;1.
14. Parganas E., Wang D., Stravopodis D., Topham D.J., Marine J.C., Teglund S., Vanin E.F., Bodner S., Colamonici O.R., van Deursen J.M., Grosveld G., Ihle J.N. Jak2 is essential for signaling through a variety of cytokine receptors. Cell. 93:1998;385.
15. Aringer M., Cheng A., Nelson J.W., Chen M., Sudarshan C., Zhou Y.J., O'Shea J.J. Janus kinases and their role in growth and disease. Life Sci. 64:1999;2173.
16. Tanner J.W., Chen W., Young R.L., Longmore G.D., Shaw A.S. The conserved box 1 motif of cytokine receptors is required for association with JAK kinases. J Biol Chem. 270:1995;6523.
17. Murakami M., Narazaki M., Hibi M., Yawata H., Yasukawa K., Hamaguchi M., Taga T., Kishimoto T. Critical cytoplasmic region of the interleukin 6 signal transducer gp130 is conserved in the cytokine receptor family. Proc Natl Acad Sci U S A. 88:1991;11349.
18. VanderKuur J.A., Wang X., Zhang L., Cambell G.S., Allevato G., Billestrup N., Norstedt G., Carter-Su C. Domains of the growth hormone receptor required for association and activation of JAK2 tyrosine kinase. J Biol Chem. 269:1994;21709.
19. Watanabe S., Itoh T., Arai K.-I. JAK2 is essential for activation of c-fos and c-myc promoters and cell proliferation through the human granulocyte-macrophage colony-stimulating factor receptor in BA/F3 cells. J Biol Chem. 271:1996;12681.
20. Leonard W.J., O'Shea J.J. Jaks and STATs. biological implications Annu Rev Immunol. 16:1998;293.
21. Taniguchi T. Cytokine signaling through nonreceptor protein tyrosine kinases. Science. 268:1995;251.
22. Ihle J.N. Cytokine receptor signalling. Nature. 377:1995;591.
23. Taga T., Kishimoto T. Signaling mechanisms through cytokine receptors that share signal transducing receptor components. Curr Opin Immunol. 7:1995;17.
24. Skoda R.C. Specificity of signaling by hematopoietic cytokine receptors. instructive versus permissive effects J Recept Signal Transduct Res. 19:1999;741.
25. Ihle J.N. Stats. signal transducers and activators of transcription Cell. 84:1996;331.
26. Liu K.D., Gaffen S.L., Goldsmith M.A. JAK/STAT signaling by cytokine receptors. Curr Opin Immunol. 10:1998;271.
27. Watanabe S, Itoh T, Arai K (1997) Roles of JAK kinase in human GM-CSF receptor signals. Leukemia 11 Suppl 3:76-8:76.
28. de Groot R.P., Coffer P.J., Koenderman L. Regulation of proliferation, differentiation and survival by the IL-3/IL-5/GM-CSF receptor family. Cell Signal. 10:1998;619.
29. c chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region. Molecular and cellular Biology. 14:1994;4335.
30. Watanabe S., Itoh T., Arai K. Roles of JAK kinases in human GM-CSF receptor signal transduction. J Allergy Clin Immunol. 98:1996;S183.
31. Sakai I., Kraft A.S. The kinase domain of Jak2 mediates induction of Bcl-2 and delays cell death in hematopoietic cells. J Biol Chem. 272:1997;12350.
32. Stomski F.C., Sun Q., Bagley C.J., Woodcock J., Goodall G., Andrews R.G., Berndt M.C., Lopez A.F. Human interleukin-3 (IL-3) induces disulphide-linked IL-3 receptor α and β chain heterodimerization which is required for receptor activation but not high affinity binding. Mol Cell Biol. 16:1996;3035.
33. Lia F., Rajotte D., Clark S.C., Hoang T. A dominant negative granulocyte-macrophage colony-stimulating factor receptor α chain reveals the multimeric structure of the receptor complex. J Biol Chem. 271:1996;28287.
34. Patel N., Herrman J.M., Timans J.C., Kastelein R.A. Functional replacement of cytokine receptor extracellular domains by leucine zippers. J Biol Chem. 271:1996;30386.
35. Orban P.C., Levings M.K., Schrader J.W. Heterodimerization of the alpha and beta chains of the interleukin-3 (IL-3) receptor is necessary and sufficient for IL-3-induced mitogenesis. Blood. 94:1999;1614.
36. Jenkins B.J., D'Andrea R.J., Gonda T.J. Activating point mutations in the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors suggest the involvement of β subunit dimerization and cell type-specific molecules in signalling. EMBO J. 14:1995;4276.
37. D'Andrea R., Rayner J., Moretti P., Lopez A., Goodall G.J., Gonda T.J., Vadas M.A. A mutation of the common receptor subunit for interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and IL-5 that leads to ligand independence and tumorigenicity. Blood. 83:1994;2802.
38. D'Andrea R.J., Barry S.C., Moretti P.A.B., Jones K., Ellis S., Vadas M.A., Goodall G.J. Extracellular truncations of hβc, the common signaling subunit for Interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor (GM-CSF), and IL-5, lead to ligand-independent activation. Blood. 87:1996;2641.
39. D'Andrea R.J., Harrison-Findik D., Butcher C.M., Finnie J., Blumbergs P., Bartley P., McCormack M.P., Jones K., Rowland R., Gonda T.J., Vadas M.A. Dysregulated hematopoiesis and a progressive neurological disorder induced by expression of an activated form of the human common beta chain in transgenic mice. J Clin Invest. 102:1998;1951.
40. McCormack M.P., Gonda T.J. Myeloproliferative disorder and leukaemia induced in mice by different classes of constitutive mutants of the human IL-3/IL-5/GM-CSF receptor common β subunit. Oncogene. 18:1999;7190.
41. Gonda T.J., D'Andrea R.J. Activating mutations in cytokine receptors. implications for receptor function and role in disease Blood. 89:1997;355.
42. Jenkins BJ, Blake TJ, Gonda TJ (1998) Saturation mutagenesis of the β subunit of the human GM-CSF receptor reveals clustering of constitutive mutations, activation of the MAP kinase and STAT pathways and differences in subunit tyrosine phosphorylation. Blood 92:1989.
43. Watanabe S., Mui A.L., Muto A., Chen J.X., Hayashida K., Yokota T., Miyajima A., Arai K. Reconstituted human granulocyte-macrophage colony-stimulating factor receptor transduces growth-promoting signals in mouse NIH 3T3 cells. comparison with signalling in BA/F3 pro-B cells Mol Cell Biol. 13:1993;1440.
44. Takaki S., Murata Y., Kitamura T., Miyajima A., Tominaga A., Takatsu K. Recostitution of the functional receptors for murine and human interleukin-5. J Exp Med. 177:1993;1523.
45. Jenkins B.J., Bagley C.J., Woodcock J., Lopez A.F., Gonda T.J. Interacting residues in the extracellular region of the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors involved in constitutive activation. J Biol Chem. 271:1996;29707.
46. Jenkins B.J., Le F., Gonda T.J. A cell type-specific constitutive point mutant of the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors requires the GM-CSF receptor α subunit for activation. J Biol Chem. 274:1999;8669.
47. Woodcock J.M., McClure B.J., Stomski F.C., Elliott M.J., Bagley C.J., Lopez A.F. The human granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor exists as a preformed receptor complex that can be activated by GM-CSF, interleukin-3, or interleukin-5. Blood. 90:1997;3005.
48. McCormack M.P., Gonda T.J. Expression of activated mutants of the human interleukin-3/interleukin-5/granulocyte-macrophage colony-stimulating factor receptor common β subunit in primary hematopoietic cells induces factor-independent proliferation and differentiation. Blood. 90:1997;1471.
49. Okuda K., Smith L., Griffin J.D., Foster R. Signaling functions of the tyrosine residues in the βc chain of the granulocyte-macrophage colony-stimulating factor receptor. Blood. 90:1997;4759.
50. Itoh T., Liu R., Yokota T., Arai K.-I., Watanabe S. Definition of the role of tyrosine residues of the common β subunit regulating multiple signaling pathways of granulocyte-macrophage colony-stimulating factor receptor. Mol Cell Biol. 18:1998;742.
51. Livnah O., Stura E.A., Middleton S.A., Johnson D.L., Jolliffe L.K., Wilson I.A. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science. 283:1999;987.
52. Syed R.S., Reid S.W., Li C., Cheetham J.C., Aoki K.H., Liu B., Zhan H., Osslund T.D., Chirino A.J., Zhang J., Finer-Moore J., Elliott S., Sitney K., Katz B.A., Matthews D.J., Wendoloski J.J., Egrie J., Stroud R.M. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 395:1998;511.
53. Livnah O., Stura E.A., Johnson D.L., Middleton S.A., Mulcahy L.S., Wrighton N.C., Dower W.J., Jolliffe L.K., Wilson I.A. Functional mimicry of a protein hormone by a peptide agonist. the Epo receptor complex at 2.8 A Science. 23:1996;464.
54. Remy I., Wilson I.A., Michnick S.W. Erythropoietin receptor activation by a ligand-induced conformation change. Science. 283:1999;990.
55. Devos R., Guisez Y., Van der Heyden J., White D.W., Kalai M., Fountoulakis M., Plaetinck G. Ligand-independent dimerization of the extracellular domain of the leptin receptor and determination of the stoichiometry of leptin binding. J Biol Chem. 272:1997;18304.
56. Muto A., Watanabe S., Miyajima A., Yokota T., Arai K.-I. The β subunit of human granulocyte-macrophage colony-stimulating factor receptor forms a homodimer and is activated via association with the α subunit. J Exp Med. 183:1996;1911.
57. Woodcock J.M., Zacharakis B., Plaetinck G., Bagley C.J., Qiyu S., Hercus T.R., Tavernier J., Lopez A.F. Three residues in the common β chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF. EMBO J. 13:1994;5176.
58. Lock P., Metcalf D., Nicola N.A. Histidine-36 of the human common beta chain of the receptor is critical for high-affinity binding of human granulocyte-macrophage colony-stimulating factor. Proc Natl Acad Sci U S A. 91:1994;252.
59. Woodcock J.M., Bagley C.J., Zacharakis B., Lopez A.F. A single tyrosine residue in the membrane proximal domain of the GM-CSF, IL-3 and IL-5 receptor common β chain is necessary and sufficient for high affinity binding and signalling by all three ligands. J Biol Chem. 271:1996;25999.
60. Sun Q, Jones K, McClure B, Cambareri B, Zacharakis B, Iversen PO, Stomski FC, Woodcock JM, Bagley CJ, D'Andrea R, Lopez AF (1999) Simultaneous antagonism of interleukin-5, granulocyte-macrophage colony-stimulating factor, and interleukin-3 stimulation of human eosinophils by targetting the common cytokines binding site of their receptors. Blood 94:1943.
61. Bargmann C.I., Hung M.C., Weinberg R.A. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell. 45:1986;649.
62. Sternberg M.J., Gullick W.J. Neu receptor dimerization. Nature. 339:1989;587.
63. Weiner D.B., Liu J., Cohen J.A., Williams W.V., Greene M.I. A point mutation in the neu oncogene mimics ligand induction of receptor aggregation. Nature. 339:1989;230.
64. Webseter M.K., Donoghue D.J. Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia. EMBO J. 15:1996;520.
65. Sakamaki K., Wang H.M., Miyajima I., Kitamura T., Todokoro K., Harada N., Miyajima A. Ligand-dependent activation of chimeric receptors with the cytoplasmic domain of the interleukin-3 receptor beta subunit (beta IL3). J Biol Chem. 268:1993;15833.
66. Gaffen S.L., Lai S.Y., Longmore G.D., Liu K.D., Goldsmith M.A. Genetic evidence for an additional factor required for erythropoietin-induced signal transduction. Blood. 94:1999;74.
67. Ogata N., Kouro T., Yamada A., Koike M., Hanai N., Ishikawa T., Takatsu K. JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor α and βc subunit, respectively, and are activated upon IL-5 stimulation. Blood. 91:1998;2264.
68. Stomski F.C., Woodcock J.M., Zacharakis B., Bagley C.J., Sun Q., Lopez A.F. Identification of a cys motif in the common β chain of the interleukin 3, granulocyte-macrophage colony-stimulating factor, and interleukin 5 receptors essential for disulfide-linked receptor heterodimerization and activation of all three receptors. J Biol Chem. 273:1998;1192.
69. Le F., Stomski F.C., Woodcock J.M., Lopez A.F., Gonda T.J. The role of disulfide-linked dimerization in IL-3 receptor signalling and biological activity. J Biol Chem. In Press:2000.
70. Kouro T., Kikuchi Y., Kanazawa H., Hirokawa K., Harada N., Shiiba M., Wakao H., Takaki S., Takatsu K. Critical proline residues of the cytoplasmic domain of the IL-5 receptor α chain and its function in IL-5-mediated activation of JAK kinase and STAT5. Int Immunol. 8:1996;237.
71. Takaki S., Kanazawa H., Shiiba M., Takatsu K. A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor α chain and its function in IL-5-mediated growth signal transduction. Mol Cell Biol. 14:1994;7404.
72. Polotskaya A., Zhao Y., Lilly M.L., Kraft A.S. A critical role for the cytoplasmic domain of the granulocyte- macrophage colony-stimulating factor alpha receptor in mediating cell growth. Cell Growth Differ. 4:1993;523.
73. Polotskaya A., Zhao Y., Lilly M.B., Kraft A.S. Mapping the intracytoplasmic regions of the alpha granulocyte- macrophage colony-stimulating factor receptor necessary for cell growth regulation. J Biol Chem. 269:1994;14607.
74. Barry S.C., Moretti P.A.B., Korpeleinen E., D'Andrea R., Lopez A.F., Vadas M.A., Goodall G.J. Roles of the N-terminal and C-terminal domains of the IL-3 receptor α chain in receptor function. Blood. 89:1997;842.
75. Matsuguchi T., Zhao Y., Lilly M.B., Kraft A.S. The cytoplasmic domain of granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor α subunit is essential for both GM-CSF-mediated growth and differentiation. J Biol Chem. 272:1997;17450.
76. Ronco L.V., Doyle S.E., Raines M., Park L.S., Gasson J.C. Conserved amino acids in the human granulocyte-macrophage colony-stimulating factor receptor-binding subunit essential for tyrosine phosphorylation and proliferation. Journal of Immunology. 154:1995;3444.
77. Doyle S.E., Gasson J.C. Characterization of the role of the human granulocyte-macrophage colony-stimulating factor receptor alpha subunit in the activation of JAK2 and STAT5. Blood. 92:1998;867.
78. Evans C.A., Pierce A., Winter S.A., Spooncer E., Heyworth C.M., Whetton A.D. Activation of granulocyte-macrophage colony-stimulating factor and interleukin-3 receptor subunits in a multipotential hematopoietic progenitor cell line leads to differential effects on development. Blood. 94:1999;1504.
79. Weiss M., Yokoyama C., Shikama Y., Naugle C., Druker B., Sieff C.A. Human granulocyte-macrophage colony-stimulating factor receptor signal transduction requires the proximal cytoplasmic domains of the alpha and beta subunits. Blood. 82:1993;3298.
80. Nelson B.H., Lord J.D., Greenberg P.D. A membrane-proximal region of the interleukin-2 receptor gamma c chain sufficient for Jak kinase activation and induction of proliferation in T cells. Mol Cell Biol. 16:1996;309.
81. Miyazaki T., Kawahara A., Fujii H., Nakagawa Y., Minami Y., Liu Z.-J., Oishi I., Silvennoinen O., Witthuhn B.A., Ihle J.N., Taniguchi T. Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. Science. 266:1994;1045.
82. Russell S.M., Johnston J.A., Noguchi M., Kawamura M., Bacon C.M., Friedmann M., Berg M., McVicar D.W., Witthuhn B.A., Silvennoinen O., Goldman A.S., Schmalstieg F.C., Ihle J.N., O'Shea J.J., Leonard W.J. Interaction of IL-2RB and gc chains with Jak 1 and Jak3. Implications for XSCID and XCID Science. 266:1994;1042.
83. Boussiotis V.A., Barber D.L., Nakarai T., Freeman G.J., Gribben J.G., Bernstein G.M., D'Andrea A.D., Ritz J., Nadler L.M. Prevention of T cell anergy by signaling through the gamma c chain of the IL-2 receptor. Science. 266:1994;1039.
84. Nelson BH, McIntosh BC, Rosencrans LL, Greenberg PD (1997) Requirement for an initial signal from the membrane-proximal region of the interleukin 2 receptor gamma(c) chain for Janus kinase activation leading to T cell proliferation. Proc Natl Acad Sci U S A 94:1878.
85. Lai S.Y., Xu W., Gaffen S.L., Liu K.D., Longmore G.D., Greene W.C., Goldsmith M.A. The molecular role of the common gamma c subunit in signal transduction reveals functional asymmetry within multimeric cytokine receptor complexes. Proc Natl Acad Sci U S A. 93:1996;231.
86. Dorsch M., Fan P.D., Danial N.N., Rothman P.B., Goff S.P. The thrombopoietin receptor can mediate proliferaton without activation of the Jak-STAT pathway. J Exp Med. 186:1997;197.
87. Machide M., Mano H., Todokoro K. Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain. Oncogene. 11:1995;619.
88. Tsubokawa M., Tohyama Y., Tohyama K., Asahi M., Inazu T., Nakamura H., Saito H., Yamamura H. Interleukin-3 activates Syk in a human myeloblastic leukemia cell line, AML193. Eur J Biochem. 249:1997;792.
89. Torigoe T., O'Connor R., Santoli D., Reed J.C. Interleukin-3 regulates the activity of the LYN protein-tyrosine kinase in myeloid-committed leukemic cell lines. Blood. 80:1992;617.
90. Anderson S.M., Jorgensen B. Activation of src-related tyrosine kinases by IL-3. J Immunol. 155:1995;1660.
91. Corey S., Eguinoa A., Puyana Theall K., Bolen J.B., Cantley L., Mollinedo F., Jackson T.R., Hawkins P.T., Stephens L.R. Granulocyte macrophage-colony stimulating factor stimulates both association and activation of phosphoinositide 3OH-kinase and src-related tyrosine kinase(s) in human myeloid derived cells. EMBO J. 12:1993;2681.
92. Hanazono Y., Chiba S., Sasaki K., Mano H., Miyajima A., Arai K., Yazaki Y., Hirai H. c-fps/fes protein-tyrosine kinase is implicated in a signaling pathway triggered by granulocyte-macrophage colony-stimulating factor and interleukin-3. EMBO J. 12:1993;1641.
93. Linnekin D., Howard O.M., Park L., Farrar W., Ferris D., Longo D.L. Hck expression correlates with granulocyte-macrophage colony-stimulating factor-induced proliferation in HL-60 cells. Blood. 84:1994;94.
94. Nakamura N., Chin H., Miyasaka N., Miura O. An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells. J Biol Chem. 271:1996;19483.
95. Sakai I., Nabell L., Kraft A.S. Signal transduction by a CD16/CD7/Jak2 fusion protein. J Biol Chem. 270:1995;18420.
96. Frank S.J., Yi W., Zhao Y., Goldsmith J.F., Gilliland G., Jiang J., Sakai I., Kraft A.S. Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor. J Biol Chem. 270:1995;1476.
97. Fambrough D., McClure K., Kazlauskas A., Lander E.S. Diverse signaling pathways activated by growth factor receptors induce broadly overlapping, rather than independent, sets of genes. Cell. 97:1999;727. [see comments].
98. Pawson T., Saxton T.M. Signaling networks - do all roads lead to the same genes? Cell. 97:1999;675. [comment].
99. Longmore G.D., You Y., Molden J., Liu K.D., Mikami A., Lai S.Y., Pharr P., Goldsmith M.A. Redundant and selective roles for erythropoietin receptor tyrosines in erythropoiesis in vivo. Blood. 91:1998;870.
100. Damen J.E., Wakao H., Miyajima A., Krosl J., Humphries R.K., Cutler R.L., Krystal G. Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. EMBO J. 14:1995;5557.
101. Gobert S., Chretien S., Gouilleux F., Muller O., Pallard C., Dusanter-Fourt I., Groner B., Lacombe C., Gisselbrecht S., Mayeux P. Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation. EMBO J. 15:1996;2434.
102. Klingmuller U., Bergelson S., Hsiao J.G., Lodish H.F. Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5. Proc Natl Acad Sci U S A. 93:1996;8324.
103. Klingmuller U., Wu H., Hsiao J.G., Toker A., Duckworth B.C., Cantley L.C., Lodish H.F. Identification of a novel pathway important for proliferation and differentiation of primary erythroid progenitors. Proc Natl Acad Sci U S A. 94:1997;3016.
104. Wu H., Klingmuller U., Besmer P., Lodish H.F. Interaction of the erythropoietin and stem cell factor receptors. Nature. 377:1995;242.
105. Wu H., Klingmuller U., Acurio A., Hsiao J.G., Lodish H.F. Functional interaction of erythropoietin and stem cell factor receptors is essential for erythroid colony formation. Proc Natl Acad Sci USA. 94:1997;1806.
106. Yamauchi T., Ueki K., Tobe K., Tamemoto H., Sekine N., Wada M., Honjo M., Takahashi M., Takahashi T., Hirai H., Tushima T., Akanuma Y., Fujita T., Komuro I., Yazuki Y., Kadowaki T. Tyrosine phosphorylation of the EGF receptor by the kinase Jak2 is induced by growth hormone. Nature. 390:1997;91.
107. Yamauchi T., Ueki K., Tobe K., Tamemoto H., Sekine N., Wada M., Honjo M., Takehashi M.T.T., Hirai H., Tsushima T., Akanuma Y., Fujita T., Komuro T., Yazaki Y., Kadowaski T. Growth hormone-induced tyrosine phosphorylation of EGF receptor as an essential element leading to MAP kinase activation and gene expression. Endocr J. 45:1998;S27-S31.
108. IL-3 receptor-deficient mice are normal. Immunity. 2:1995;211.
109. Hanazono Y., Sasaki K., Nitta H., Yazaki Y., Hirai H. Erythropoietin induces tyrosine phosphorylation of the β chain of the GM-CSF receptor. Biuochem Biophys Res Commun. 208:1995;1060.
110. IL-3. Blood. 89:1997;432.
111. de Rooij J., Bos J.L. Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene. 14:1997;623.
112. Pan C.X., Fukunaga R., Yonehara S., Nagata S. Unidirectional cross-phosphorylation between the granulocyte colony-stimulating factor and interleukin-3 receptors. J Biol Chem. 268:1993;25818.
113. Cornelis S., Fache I., Van der Heyden J., Guisez Y., Tavernier J., Devos R., Fiers W., Plaetinck G. Characterization of critical residues in the cytoplasmic domain of the human interleukin-5 receptor alpha chain required for growth signal transduction. Eur J Immunol. 25:1995;1857.
114. Zhao Y., Wagner F., Frank S.J., Kraft A.S. The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor beta c chain. J Biol Chem. 270:1995;13814.
115. Rao P., Mufson R.A. A membrane proximal domain of the human interleukin-3 receptor beta c subunit that signals DNA synthesis in NIH 3T3 cells specifically binds a complex of Src and Janus family tyrosine kinases and phosphatidylinositol 3-kinase. J Biol Chem. 270:1995;6886.
116. Yu H., Chen J.K., Feng S., Dalgarno D.C., Brauer A.W., Schreiber S.L. Structural basis for the binding of proline-rich peptides to SH3 domains. Cell. 76:1994;933.