Regulation of Proliferation, Differentiation and Survival by the IL-3/IL-5/GM-CSF Receptor Family

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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STATs and Gene Regulation

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Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt

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A family of cytokine-inducible inhibitors of signalling

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TRANSCRIPTIONAL RESPONSES TO POLYPEPTIDE LIGANDS: The JAK-STAT Pathway

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A new protein containing an SH2 domain that inhibits JAK kinases

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Targeted disruption of the mouse <i>Stat3</i> gene leads to early embryonic lethality

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CYTOKINES: COORDINATORS OF IMMUNE AND INFLAMMATORY RESPONSES

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Signalling through the lipid products of phosphoinositide-3-OH kinase

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Structure and function of a new STAT-induced STAT inhibitor

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The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

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Specific Inhibition of Stat3 Signal Transduction by PIAS3

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A novel cytokine‐inducible gene CIS encodes an SH2‐containing protein that binds to tyrosine‐phosphorylated interleukin 3 and erythropoietin receptors.

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Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene

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PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond

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Interleukin‐3, granulocyte‐macrophage colony stimulating factor and interleukin‐5 transduce signals through two STAT5 homologs.

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A central role for Stat3 in IL‐6‐induced regulation of growth and differentiation in M1 leukemia cells.

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Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene

Tsui, H. W., Siminovitch, K. A., de Souza, L., & Tsui, F. W. L. (1993) · Nature Genetics · doi:10.1038/ng0693-124 · Cited by 564 · see citing works

Bcl-2 Phosphorylation Required for Anti-apoptosis Function

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CIS, a Cytokine Inducible SH2 Protein, Is a Target of the JAK-STAT5 Pathway and Modulates STAT5 Activation

Matsumoto, A., Masuhara, M., Mitsui, K., Yokouchi, M., Ohtsubo, M., Misawa, H., Miyajima, A., & Yoshimura, A. (1997) · Blood · doi:10.1182/blood.v89.9.3148 · Cited by 528 · see citing works

Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase

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Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production.

Baffy, G., Miyashita, T., WILLIAMSON, J. R., & Reed, J. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53280-4 · Cited by 482 · see citing works

JAK2 Associates with the β c Chain of the Receptor for Granulocyte-Macrophage Colony-Stimulating Factor, and Its Activation Requires the Membrane-Proximal Region

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Suppression of interleukin‐3‐induced gene expression by a C‐terminal truncated Stat5: role of Stat5 in proliferation.

Mui, A., Wakao, H., Kinoshita, T., Kitamura, T., & Miyajima, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00600.x · Cited by 397 · see citing works

STAT3β, a splice variant of transcription factor STAT3, is a dominant negative regulator of transcription

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Interleukin 3-dependent survival by the Akt protein kinase

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Signal transduction by the high‐affinity GM‐CSF receptor: two distinct cytoplasmic regions of the common beta subunit responsible for different signaling.

Sato, N., Sakamaki, K., Terada, N., Arai, K., & Miyajima, A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06102.x · Cited by 355 · see citing works

Tyrosine Phosphorylation of DNA Binding Proteins by Multiple Cytokines

Larner, A. C., David, M., Feldman, G. M., Igarashi, K., Hackett, R. H., Webb, D. S. A., Sweitzer, S. M., Petricoin, E. F., & Finbloom, D. S. (1993) · Science · doi:10.1126/science.8378773 · Cited by 352 · see citing works

Hematopoietic Cell Phosphatase Associates with the Interleukin-3 (IL-3) Receptor β Chain and Down-Regulates IL-3-Induced Tyrosine Phosphorylation and Mitogenesis

Yi, T., Mui, A., Krystal, G., & Ihle, J. N. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7577-7586.1993 · Cited by 341 · see citing works

Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2 .

Lin, E. Y., Orlofsky, A., Berger, M. S., & Prystowsky, M. B. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.151.4.1979 · Cited by 335 · see citing works

STAT3 activation is a critical step in gp130-mediated terminal differentiation and growth arrest of a myeloid cell line.

Minami, M., Inoue, M., Wei, S., Takeda, K., Matsumoto, M., Kishimoto, T., & Akira, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.3963 · Cited by 335 · see citing works

Involvement of ras p21 protein in signal-transduction pathways from interleukin 2, interleukin 3, and granulocyte/macrophage colony-stimulating factor, but not from interleukin 4.

Satoh, T., Nakafuku, M., Miyajima, A., & Kaziro, Y. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3314 · Cited by 329 · see citing works

Cloning of Murine Stat6 and Human Stat6, Stat Proteins That Are Tyrosine Phosphorylated in Responses to IL-4 and IL-3 but Are Not Required for Mitogenesis

Quelle, F. W., Shimoda, K., Thierfelder, W. E., Fischer, C. D., Kim, A., Ruben, S. M., Cleveland, J. L., Pierce, J. H., Keegan, A. D., Nelms, K. A., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3336 · Cited by 324 · see citing works

Interleukin‐3 signals through multiple isoforms of Stat5.

Azam, M., Erdjument‐Bromage, H., Bl, K., Xia, M., Quelle, F. W., Basu, R., Saris, C. J. M., Tempst, P., Ihle, J. N., & Schindler, C. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07126.x · Cited by 323 · see citing works

Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases

Knall, C., Worthen, G. S., & Johnson, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3052 · Cited by 322 · see citing works

Suppression of apoptotic death in hematopoietic cells by signalling through the IL‐3/GM‐CSF receptors.

Kinoshita, T., Yokota, T., Arai, K., et al. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07000.x · Cited by 315 · see citing works

Mice deficient for the IL-3/GM-CSF/IL-5 βc receptor exhibit lung pathology and impaired immune response, while βIL3 receptor-deficient mice are normal

Nishinakamura, R., Nakayama, N., Hirabayashi, Y., Inoue, T., Aud, D., McNeil, T., Azuma, S., Yoshida, S., Toyoda, Y., Aral, K.-I., et al. (1995) · Immunity · doi:10.1016/1074-7613(95)90046-2 · Cited by 309 · see citing works

Hematopoietic and lung abnormalities in mice with a null mutation of the common beta subunit of the receptors for granulocyte-macrophage colony-stimulating factor and interleukins 3 and 5.

Robb, L. G., Drinkwater, C. C., Metcalf, D., Li, R., Köntgen, F., Nicola, N. A., & Begley, C. G. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9565 · Cited by 297 · see citing works

Signal transduction of the human granulocyte-macrophage colony- stimulating factor and interleukin-3 receptors involves tyrosine phosphorylation of a common set of cytoplasmic proteins

Kanakura, Y., Druker, B. J., Cannistra, S., Furukawa, Y., Torimoto, Y., & Griffin, J. D. (1990) · Blood · doi:10.1182/blood.v76.4.706.706 · Cited by 271 · see citing works

Deletion of the Carboxyl-Terminal Transactivation Domain of MGF-Stat5 Results in Sustained DNA Binding and a Dominant Negative Phenotype

Moriggl, R., Gouilleux‐Gruart, V., Jähne, R., Berchtold, S., Gartmann, C. J., Liu, X., Hennighausen, L. G., Sotiropoulos, A., Groner, B., & Gouilleux, F. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5691 · Cited by 265 · see citing works

Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand.

Yi, T., & Ihle, J. N. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3350 · Cited by 263 · see citing works

The proto-oncogene product p120CBL and the adaptor proteins CRKL and c-CRK link c-ABL, p190BCR/ABL and p210BCR/ABL to the phosphatidylinositol-3' kinase pathway.

Sattler, M., Salgia, R., Okuda, K., et al. (1996) · PubMed · Cited by 257 · see citing works

Naturally Occurring Dominant Negative Variants of Stat5

Wang, D., Stravopodis, D. J., Teglund, S., Kitazawa, J., & Ihle, J. N. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6141 · Cited by 252 · see citing works

Cloning and Characterization of Novel CIS Family Genes

Masuhara, M., Sakamoto, H., Matsumoto, A., Suzuki, R., Yasukawa, H., Mitsui, K., Wakioka, T., Tanimura, S., Sasaki, A. T., Misawa, H., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7484 · Cited by 248 · see citing works

Requirement of Lyn and Syk tyrosine kinases for the prevention of apoptosis by cytokines in human eosinophils.

Yousefi, S., Hoessli, D. C., Blaser, K., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1407 · Cited by 235 · see citing works

R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways

Marte, B. M., Rodriguez-Viciana, P., Wennström, S., Warne, P. H., & Downward, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00028-5 · Cited by 223 · see citing works

Mouse oncostatin M: an immediate early gene induced by multiple cytokines through the JAK‐STAT5 pathway.

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Activation of the Janus Kinase/STAT (Signal Transducer and Activator of Transcription) Signal Transduction Pathway by Interleukin-6-Type Cytokines Promotes Osteoblast Differentiation

Bellido, T., Borba, V. Z. C., Roberson, P. K., & Manolagas, S. C. (1997) · Endocrinology · doi:10.1210/endo.138.9.5364 · Cited by 212 · see citing works

Differentiation and growth arrest signals are generated through the cytoplasmic region of gp130 that is essential for Stat3 activation.

Yamanaka, Y., Nakajima, K., Fukada, T., Hibi, M., & Hirano, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00500.x · Cited by 211 · see citing works

Two distinct functional high affinity receptors for mouse interleukin‐3 (IL‐3).

Hara, T., & Miyajima, A. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05239.x · Cited by 206 · see citing works

p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein.

Duronio, V., Welham, M. J., Abraham, S., Dryden, P., & Schrader, J. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1587 · Cited by 205 · see citing works

Granulocyte-macrophage colony-stimulating factor, interleukin-3, and steel factor induce rapid tyrosine phosphorylation of p42 and p44 MAP kinase

Okuda, K., Sanghera, J., Pelech, S., et al. (1992) · Blood · doi:10.1182/blood.v79.11.2880.bloodjournal79112880 · Cited by 203 · see citing works

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.

Corey, S. J., Eguinoa, A., Puyana-Theall, K., Bolen, J. B., Cantley, L. C., Mollinedo, F., Jackson, T., Hawkins, P. T., & Stephens, L. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05929.x · Cited by 193 · see citing works

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

Bagley, C. J., Woodcock, J. M., Stomski, F. C., et al. (1997) · Blood · doi:10.1182/blood.v89.5.1471 · Cited by 192 · see citing works

The Proto-oncogene Product c-Cbl Becomes Tyrosine Phosphorylated by Stimulation with GM-CSF or Epo and Constitutively Binds to the SH3 Domain of Grb2/Ash in Human Hematopoietic Cells

Odai, H., Sasaki, K., Iwamatsu, A., Hanazono, Y., Tanaka, T., Mitani, K., Yazaki, Y., & Hirai, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10800 · Cited by 177 · see citing works

Granulocyte-macrophage colony-stimulating factor, interleukin-3, and steel factor induce rapid tyrosine phosphorylation of p42 and p44 MAP kinase

Okuda, K., Sanghera, J., Pelech, S., et al. (1992) · Blood · doi:10.1182/blood.v79.11.2880.2880 · Cited by 177 · see citing works

Interleukin-3 and granulocyte-macrophage colony-stimulating factor mediate rapid phosphorylation and activation of cytosolic c-raf.

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STAT5A-Deficient Mice Demonstrate a Defect in Granulocyte-Macrophage Colony-Stimulating Factor–Induced Proliferation and Gene Expression

Feldman, G. M., Rosenthal, L. A., Liu, X., Hayes, M. P., Wynshaw-Boris, A. J., Leonard, W. J., Hennighausen, L. G., & Finbloom, D. S. (1997) · Blood · doi:10.1182/blood.v90.5.1768 · Cited by 175 · see citing works

Investigation of neutrophil signal transduction using a specific inhibitor of phosphatidylinositol 3-kinase.

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IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases.

Sato, S., Katagiri, T., Takaki, S., Kikuchi, Y., Hitoshi, Y., Yonehara, S., Tsukada, S., Kitamura, D., Watanabe, T., Witte, O. N., et al. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.6.2101 · Cited by 170 · see citing works

Involvement of STAT3 in the Granulocyte Colony-stimulating Factor-induced Differentiation of Myeloid Cells

Shimozaki, K., Nakajima, K., Hirano, T., & Nagata, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25184 · Cited by 169 · see citing works

Comparison of the roles of mitogen-activated protein kinase kinase and phosphatidylinositol 3-kinase signal transduction in neutrophil effector function

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The intracellular signal transduction mechanism of interleukin 5 in eosinophils: the involvement of lyn tyrosine kinase and the Ras-Raf-1-MEK-microtubule-associated protein kinase pathway.

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A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction

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Multiple cytokines activate phosphatidylinositol 3-kinase in hemopoietic cells. Association of the enzyme with various tyrosine-phosphorylated proteins.

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An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT

Fujitani, Y., Hibi, M., Fukada, T., Takahashi-Tezuka, M., Yoshida, H., Yamaguchi, T., Sugiyama, K., Yamanaka, Y., Nakajima, K., & Hirano, T. (1997) · Oncogene · doi:10.1038/sj.onc.1200907 · Cited by 156 · see citing works

Regulation of Bcl-2 expression by oncogenic Ras protein in hematopoietic cells.

Kinoshita, T., Yokota, T., Arai, K., et al. (1995) · PubMed · Cited by 152 · see citing works

Functionally Distinct Isoforms of STAT5 Are Generated by Protein Processing

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Constitutive activation of mitogen-activated protein kinase pathway in acute leukemia cells

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Multiple hemopoietic growth factors stimulate activation of mitogen-activated protein kinase family members

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Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3'-kinase.

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A1, a Bcl-2 family member, prolongs cell survival and permits myeloid differentiation

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G-Protein-coupled Receptors and Fcγ-receptors Mediate Activation of Akt/Protein Kinase B in Human Phagocytes

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The Amino-terminal Portion of the JAK2 Protein Kinase Is Necessary For Binding and Phosphorylation of the Granulocyte-Macrophage Colony-stimulating Factor Receptor β Chain

Zhao, Y., Wagner, F. H., Frank, S. J., & Kraft, A. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.13814 · Cited by 140 · see citing works

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

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Constitutive activation of protein kinase B and phosphorylation of p47 phox by a membrane-targeted phosphoinositide 3-kinase

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A novel pathway from phosphorylation of tyrosine residues 239/240 of Shc, contributing to suppress apoptosis by IL‐3.

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Interleukin-5, interleukin-3, and granulocyte-macrophage colony-stimulating factor cross-compete for binding to cell surface receptors on human eosinophils.

Lopez, A. F., Vadas, M. A., Woodcock, J. M., Milton, S., Lewis, A., Elliott, M. J., Gillis, D., Ireland, R., Olwell, E., & Park, L. S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54292-7 · Cited by 129 · see citing works

Tyrosine phosphorylation and activation of a new mitogen-activated protein (MAP)-kinase cascade in human neutrophils stimulated with various agonists

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Granulocyte-Macrophage Colony-stimulating Factor Stimulates JAK2 Signaling Pathway and Rapidly Activates p93 , STAT1 p91, and STAT3 p92 in Polymorphonuclear Leukocytes

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