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Science 17 December 1993: Vol. 262. no. 5141, pp. 1880 - 1883 DOI: 10.1126/science.8266078
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Articles
Science, Vol 262, Issue 5141, 1880-1883
Copyright © 1993 by American Association for the Advancement of Science
Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor
SM Russell,
AD Keegan,
N Harada,
Y Nakamura,
M Noguchi,
P Leland,
MC Friedmann,
A Miyajima,
RK Puri,
WE Paul,
and
al. et
Section on Pulmonary and Molecular Immunology, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892.
The interleukin-2 (IL-2) receptor gamma chain (IL-2R gamma) is an essential component of high- and intermediate-affinity IL-2 receptors. IL-2R gamma was demonstrated to be a component of the IL-4 receptor on the basis of chemical cross-linking data, the ability of IL-2R gamma to augment IL-4 binding affinity, and the requirement for IL-2R gamma in IL-4-mediated phosphorylation of insulin receptor substrate-1. The observation that IL-2R gamma is a functional component of the IL-4 receptor, together with the finding that IL-2R gamma associates with the IL-7 receptor, begins to elucidate why deficiency of this common gamma chain (gamma c) has a profound effect on lymphoid function and development, as seen in X-linked severe combined immunodeficiency.
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- Delineation of the Regions of Interleukin-2 (IL-2) Receptor beta Chain Important for Association of Jak1 and Jak3. Jak1-INDEPENDENT FUNCTIONAL RECRUITMENT OF Jak3 TO IL-2Rbeta.
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J. Biol. Chem.
273, 10719-10725
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- Impaired Interleukin 4 Signaling in T Helper Type 1 Cells.
- H. Huang and W. E. Paul (1998)
J. Exp. Med.
187, 1305-1313
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- Regulation of Interleukin-13 Receptor Constituents on Mature Human B Lymphocytes.
- H. Ogata, D. Ford, N. Kouttab, T. C. King, N. Vita, A. Minty, J. Stoeckler, D. Morgan, C. Girasole, J. W. Morgan, et al. (1998)
J. Biol. Chem.
273, 9864-9871
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- A Role for the Insulin-Interleukin (IL)-4 Receptor Motif of the IL-4 Receptor alpha -Chain in Regulating Activation of the Insulin Receptor Substrate 2 and Signal Transducer and Activator of Transcription 6 Pathways. ANALYSIS BY MUTAGENESIS.
- H. Y. Wang, J. Zamorano, and A. D. Keegan (1998)
J. Biol. Chem.
273, 9898-9905
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- Involvement of the IL-2 Receptor {gamma}-Chain ({gamma}c) in the Control by IL-4 of Human Monocyte and Macrophage Proinflammatory Mediator Production.
- C. S. Bonder, H. L. Dickensheets, J. J. Finlay-Jones, R. P. Donnelly, and P. H. Hart (1998)
J. Immunol.
160, 4048-4056
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- Inhibition of JAK3 and STAT6 Tyrosine Phosphorylation by the Immunosuppressive Drug Leflunomide Leads to a Block in IgG1 Production.
- K. Siemasko, A. S-F. Chong, H.-M. Jack, H. Gong, J. W. Williams, and A. Finnegan (1998)
J. Immunol.
160, 1581-1588
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- The Association of Atopy with a Gain-of-Function Mutation in the {alpha} Subunit of the Interleukin-4 Receptor.
- G. K. K. Hershey, M. F. Friedrich, L. A. Esswein, M. L. Thomas, and T. A. Chatila (1997)
N. Engl. J. Med.
337, 1720-1725
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- Full Immunologic Reconstitution Following Nonconditioned Bone Marrow Transplantation for Canine X-Linked Severe Combined Immunodeficiency.
- P. J. Felsburg, R. L. Somberg, B. J. Hartnett, S. F. Suter, P. S. Henthorn, P. F. Moore, K. I. Weinberg, and H. D. Ochs (1997)
Blood
90, 3214-3221
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- Functional cleavage of the common cytokine receptor gamma chain (gamma c) by calpain.
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PNAS
94, 11534-11539
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- HMG-I(Y) Phosphorylation Status as a Nuclear Target Regulated through Insulin Receptor Substrate-1 and the I4R Motif of the Interleukin-4 Receptor.
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J. Biol. Chem.
272, 25083-25090
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- An interleukin 4 (IL-4)-independent pathway for CD4+ T cell IL-4 production is revealed in IL-4 receptor-deficient mice.
- N. Noben-Trauth, L. D. Shultz, F. Brombacher, J. F. Urban Jr., H. Gu, and W. E. Paul (1997)
PNAS
94, 10838-10843
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- An Interleukin (IL)-13 Receptor Lacking the Cytoplasmic Domain Fails to Transduce IL-13-Induced Signals and Inhibits Responses to IL-4.
- P. L. Orchansky, S. D. Ayres, D. J. Hilton, and J. W. Schrader (1997)
J. Biol. Chem.
272, 22940-22947
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- Modulation of Interleukin (IL)-13 Binding and Signaling by the gamma c Chain of the IL-2 Receptor.
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J. Biol. Chem.
272, 20251-20258
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- Receptor-associated constitutive protein tyrosine phosphatase activity controls the kinase function of JAK1.
- S. J. Haque, Q. Wu, W. Kammer, K. Friedrich, J. M. Smith, I. M. Kerr, G. R. Stark, and B. R. G. Williams (1997)
PNAS
94, 8563-8568
| Abstract »
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- Interleukin-15 Triggers Activation and Growth of the CD8 T-Cell Pool in Extravascular Tissues of Patients With Acquired Immunodeficiency Syndrome.
- C. Agostini, L. Trentin, R. Sancetta, M. Facco, C. Tassinari, A. Cerutti, M. Bortolin, A. Milani, M. Siviero, R. Zambello, et al. (1997)
Blood
90, 1115-1123
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- Interleukin 4 (IL-4) or IL-7 Prevents the Death of Resting T Cells: Stat6 Is Probably Not Required for the Effect of IL-4.
- A. Vella, T. K. Teague, J. Ihle, J. Kappler, and P. Marrack (1997)
J. Exp. Med.
186, 325-330
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- Two Discrete Regions of Interleukin-2 (IL2) Receptor beta Independently Mediate IL2 Activation of a PD98059/Rapamycin/Wortmannin-insensitive Stat5a/b Serine Kinase.
- R. A. Kirken, M. G. Malabarba, J. Xu, L. DaSilva, R. A. Erwin, X. Liu, L. Hennighausen, H. Rui, and W. L. Farrar (1997)
J. Biol. Chem.
272, 15459-15465
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- Clonal Proliferation and Cytokine Requirement of Murine Progenitors for Natural Killer Cells.
- Y. Aiba, F. Hirayama, and M. Ogawa (1997)
Blood
89, 4005-4012
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- Activation of Phosphatidylinositol 3-Kinase by Interleukin-13. AN INHIBITORY SIGNAL FOR INDUCIBLE NITRIC-OXIDE SYNTHASE EXPRESSION IN EPITHELIAL CELL LINE HT-29.
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J. Biol. Chem.
272, 12626-12633
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- Intermediate Affinity Interleukin-2 Receptor Mediates Survival via a Phosphatidylinositol 3-Kinase-dependent Pathway.
- A. Gonzalez-Garcia, I. Merida, C. Martinez-A, and A. C. Carrera (1997)
J. Biol. Chem.
272, 10220-10226
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- Interleukin-4 Signaling in B Lymphocytes from Patients with X-linked Severe Combined Immunodeficiency.
- N. Taylor, F. Candotti, S. Smith, S. A. Oakes, T. Jahn, J. Isakov, J. M. Puck, J. J. O'Shea, K. Weinberg, and J. A. Johnston (1997)
J. Biol. Chem.
272, 7314-7319
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- A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain.
- Y. Wang, B.-J. Shen, and W. Sebald (1997)
PNAS
94, 1657-1662
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