Negative regulation of cytokine signaling

Greenhalgh, Christopher J; Hilton, Douglas J

doi:10.1189/jlb.70.3.348

Cited by 258Cytokine Signaling Pathways and InteractionsProtein Tyrosine PhosphatasesNF-κB Signaling Pathways

Negative regulation of cytokine signaling

Greenhalgh, Christopher J, Hilton, Douglas J·2001·Journal of Leukocyte Biology

DOI 10.1189/jlb.70.3.348

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Abstract

Cytokines use complex signaling cascades to elicit their biological effects, many of which involve phosphorylation as a mechanism of activation. Rapid and efficient attenuation of cytokine signals is crucial to maintaining regulation of these processes and to preventing toxic side effects. Phosphatases have been shown to be involved in these regulatory processes, but more recent research has seen the discovery of two new families of negative regulators, the suppressor of cytokine signaling (SOCS) and protein inhibitors of signal transducer and activator of transcription (STAT) (PIAS) protein families. SOCS proteins are induced by and inhibit many cytokine-signaling systems in a classic negative-feedback loop, and the generation of transgenic and knockout models has greatly increased our understanding of their physiological functions. PIAS proteins interact with the transcriptional mediators of cytokine action, the STATs, to suppress their DNA-binding activity. These three classes of molecules form what is now emerging as an integrated system for deactivating cytokine signaling at a number of levels, from the receptor to the transcription factor.

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Activation of cytokine signaling is coupled with multiple layers of negative regulation to ensure timely down-regulation of signaling, as exemplified by the SOCS system.
“Activation of cytokine signaling is coupled with multiple layers of negative regulation to ensure timely down-regulation of signaling, as exemplified by the SOCS system (17).”
From Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element (2002) · cites this paper as [17]

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IL‐10 attenuates IFN‐α‐activated STAT1 in the liver: involvement of SOCS2 and SOCS3
Shen, X., Hong, F., Nguyen, V.-A., & Gao, B. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01905-0 · Cited by 103 · see citing works
Activation of SOCS-3 Messenger Ribonucleic Acid in the Hypothalamus by Ciliary Neurotrophic Factor1
Bjørbæk, C., Elmquist, J. K., El-Haschimi, K., Kelly, J., Ahima, R. S., Hileman, S. M., & Flier, J. S. (1999) · Endocrinology · doi:10.1210/endo.140.5.6736 · Cited by 103 · see citing works
Leptin treatment increases suppressors of cytokine signaling in central and peripheral tissues
Emilsson, V., Arch, J. R. S., de Groot, R. P., Lister, C. A., & Cawthorne, M. A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00874-1 · Cited by 97 · see citing works
Negative regulation of early B lymphopoiesis by interleukin 3 and interleukin 1 alpha.
Hirayama, F., Clark, S. C., & Ogawa, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.469 · Cited by 86 · see citing works
Endotoxin-Induced Inhibition of Growth Hormone Receptor Signaling in Rat Liver in Vivo1
Mao, Y., Ling, P., Fitzgibbons, T. P., McCowen, K. C., Frick, G. P., Bistrian, B. R., & Smith, R. J. (1999) · Endocrinology · doi:10.1210/endo.140.12.7212 · Cited by 85 · see citing works
Suppressor of Cytokine Signaling (SOCS)-3 Protein Interacts with the Insulin-like Growth Factor-I Receptor
Dey, B. R., Furlanetto, R. W., & NISSLEY, P. S. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3762 · Cited by 83 · see citing works
Defective Thymocyte Development and Perturbed Homeostasis of T cells in STAT-Induced STAT Inhibitor-1/Suppressors of Cytokine Signaling-1 Transgenic Mice
Fujimoto, M., Naka, T., Nakagawa, R., Kawazoe, Y., Morita, Y., Tateishi, A., Okumura, K., Narazaki, M., & Kishimoto, T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.4.1799 · Cited by 82 · see citing works
Macrophages from motheaten and viable motheaten mutant mice show increased proliferative responses to GM-CSF: detection of potential HCP substrates in GM-CSF signal transduction.
Jiao, H., Yang, W., Berrada, K., Tabrizi, M. A., Shultz, L. D., & Yi, T. (1997) · PubMed · Cited by 81 · see citing works
Interleukin-11 Stimulates Proopiomelanocortin Gene Expression and Adrenocorticotropin Secretion in Corticotroph Cells: Evidence for a Redundant Cytokine Network in the Hypothalamo-Pituitary-Adrenal Axis*
Auernhammer, C. J., & Melmed, S. K. (1999) · Endocrinology · doi:10.1210/endo.140.4.6636 · Cited by 79 · see citing works
A Novel Ligand for an SH3 Domain of the Adaptor Protein Nck Bears an SH2 Domain and Nuclear Signaling Motifs
Matuoka, K., Miki, H., Takahashi, K., & Takenawa, T. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7492 · Cited by 75 · see citing works
Electrophoretically pure mouse interferon inhibits growth, induces liver and kidney lesions, and kills suckling mice.
Gresser, I., Aguet, M., Morel-Marogér, L., Woodrow, D. F., Puvion-dutilleul, F., Guillon, J.-C., & Maury, C. (1981) · PubMed Central · Cited by 73 · see citing works
SOCS-1, -2, -3: selective targets and functions downstream of the prolactin receptor
Tomic, S., Chughtai, N., & ALI, S. (1999) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(99)00180-x · Cited by 58 · see citing works
Expression of SOCS genes in normal and leukemic human leukocytes stimulated by prolactin, growth hormone and cytokines
Doğusan, Z. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(00)00300-3 · Cited by 58 · see citing works
A methylthioadenosine phosphorylase (MTAP) fusion transcript identifies a new gene on chromosome 9p21 that is frequently deleted in cancer
Schmid, M., Sen, M., Rosenbach, M., Carrera, C. J., Friedman, H. S., & Carson, D. A. (2000) · Oncogene · doi:10.1038/sj.onc.1203942 · Cited by 57 · see citing works
Interleukin 9 induces expression of three cytokine signal inhibitors: cytokine-inducible SH2-containing protein, suppressor of cytokine signalling (SOCS)-2 and SOCS-3, but only SOCS-3 overexpression suppresses interleukin 9 signalling
Lejeune, D., Demoulin, J., & Renauld, J. (2000) · Biochemical Journal · doi:10.1042/bj3530109 · Cited by 54 · see citing works
Thyrotropin Induces SOCS-1 (Suppressor of Cytokine Signaling-1) and SOCS-3 in FRTL-5 Thyroid Cells
Park, E. S., Kim, H., Suh, J. M., Park, S. J., Kwon, O., Kim, Y. K., Ro, H. K., Cho, B. Y., Chung, J., & Shong, M. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.3.0433 · Cited by 48 · see citing works
Negative cross-talk between interleukin-3 and interleukin-11 is mediated by suppressor of cytokine signalling-3 (SOCS-3)
Magrangeas, F., Boisteau, O., DENIS, S., Jacques, Y., & Minvielle, S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530223 · Cited by 48 · see citing works
Alterations in hepatic production and peripheral clearance of IGF-I after endotoxin
Fan, J., Char, D. J., Kolasa, A. J., Pan, W., Maitra, S. R., Patlak, C. S., Spolarics, Z., Gelato, M. C., & Lang, C. H. (1995) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1995.269.1.e33 · Cited by 43 · see citing works
DNA-binding antibodies from viable motheaten mutant mice: implications for B cell tolerance
Westhoff, C. M., Whittier, A. M., Kathol, S., McHugh, J., Zajicek, C., Shultz, L. D., & Wylie, D. E. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.6.3024 · Cited by 39 · see citing works
Cis desensitizes GH induced Stat5 signaling in rat liver cells
Karlsson, H. L., Gustafsson, J.-Å., & Mode, A. (1999) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(99)00101-x · Cited by 37 · see citing works
Can interferon induce disease?
Gresser, I. (1982) · PubMed · Cited by 37 · see citing works
Negative cross-talk between interleukin-3 and interleukin-11 is mediated by suppressor of cytokine signalling-3 (SOCS-3)
Magrangeas, F., Boisteau, O., DENIS, S., et al. (2001) · Biochemical Journal · doi:10.1042/bj3530223 · Cited by 25 · see citing works
The Viable Motheaten (mev) Mouse—A New Model for Arthritis
Kovařík, J., Kuntz, L., Ryffel, B., & Borel, J. F. (1994) · Journal of Autoimmunity · doi:10.1006/jaut.1994.1042 · Cited by 11 · see citing works

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Sorted by citations

The JAK/STAT signaling pathway
Rawlings, J. S., Rosler, K. M., & Harrison, D. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.00963 · Cited by 1,858 · see citing works
Regulation of JAK–STAT signalling in the immune system
Shuai, K., & Liu, B. (2003) · Nature reviews. Immunology · doi:10.1038/nri1226 · Cited by 1,379 · see citing works
Activated STAT signaling in human tumors provides novel molecular targets for therapeutic intervention.
Buettner, R., Mora, L. B., & Jove, R. (2002) · PubMed · Cited by 1,021 · see citing works
IL-6 and related cytokines as the critical lynchpins between inflammation and cancer
Taniguchi, K., & Karin, M. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.01.001 · Cited by 713 · see citing works
Tuning the Cytokine Responses: An Update on Interleukin (IL)-4 and IL-13 Receptor Complexes
Junttila, I. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00888 · Cited by 687 · see citing works
Suppressors of cytokine signalling (SOCS) in the immune system
Alexander, W. S. (2002) · Nature reviews. Immunology · doi:10.1038/nri818 · Cited by 645 · see citing works
SOCS-1 Participates in Negative Regulation of LPS Responses
Nakagawa, R., Naka, T., Tsutsui, H., Fujimoto, M., Kimura, A., Abe, T., Seki, E., Sato, S., Takeuchi, O., Takeda, K., et al. (2002) · Immunity · doi:10.1016/s1074-7613(02)00449-1 · Cited by 638 · see citing works
Targeting the STAT3 signaling pathway in cancer: Role of synthetic and natural inhibitors
Siveen, K. S., Sikka, S., Surana, R., Dai, X., Zhang, J., Kumar, A. P., Tan, B. K. H., Sethi, G., & Bishayee, A. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.12.005 · Cited by 637 · see citing works
IL-13 receptors and signaling pathways: An evolving web
Hershey, G. K. K. (2003) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2003.1333 · Cited by 612 · see citing works
MicroRNAs regulate critical genes associated with multiple myeloma pathogenesis
Pichiorri, F., Suh, S.-S., Ladetto, M., Kuehl, M., Palumbo, T., Drandi, D., Taccioli, C., Zanesi, N., Alder, H., Hagan, J. P., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806202105 · Cited by 563 · see citing works
Complex modulation of cell type-specific signaling in response to type I interferons
van Boxel-Dezaire, A. H. H., Rani, M. R. S., & Stark, G. R. (2006) · Immunity · doi:10.1016/j.immuni.2006.08.014 · Cited by 530 · see citing works
Subversion Mechanisms by Which Leishmania Parasites Can Escape the Host Immune Response: a Signaling Point of View
Olivier, M., Gregory, D. J., & Forget, G. (2005) · Clinical Microbiology Reviews · doi:10.1128/cmr.18.2.293-305.2005 · Cited by 497 · see citing works
Lipid Metabolism, Apoptosis and Cancer Therapy
Huang, C., & Freter, C. E. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16010924 · Cited by 447 · see citing works
UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
Malakhova, O. A., Kim, K. I. I., Luo, J.-K., Zou, W., Kumar, K. G., Fuchs, S. Y., Shuai, K., & Zhang, D. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601149 · Cited by 430 · see citing works
Regulation of myeloid development and function by colony stimulating factors
Barreda, D. R. (2003) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2003.09.010 · Cited by 403 · see citing works
Inhibition of Th1 Differentiation by IL-6 Is Mediated by SOCS1
Diehl, S. A., Anguíta, J., Hoffmeyer, A., Zapton, T., Ihle, J. N., Fikrig, E., & Rincón, M. (2000) · Immunity · doi:10.1016/s1074-7613(00)00078-9 · Cited by 402 · see citing works
Spinning molecular immunology into successful immunotherapy
Pardoll, D. M. (2002) · Nature reviews. Immunology · doi:10.1038/nri774 · Cited by 360 · see citing works
The T Cell Protein Tyrosine Phosphatase Is a Negative Regulator of Janus Family Kinases 1 and 3
Simoncic, P. D., Lee-Loy, A., Barber, D. L., Tremblay, M. L., & McGlade, C. J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00697-8 · Cited by 354 · see citing works
Protein ISGylation modulates the JAK-STAT signaling pathwayPreprint
Malakhova, O. A., Yan, M., Malakhov, M. P., Yuan, Y., Ritchie, K. J., Kim, K. I., Peterson, L. F., Shuai, K., & Zhang, D. (2003) · Genes & Development · doi:10.1101/gad.1056303 · Cited by 317 · see citing works
SOCS-1, a negative regulator of cytokine signaling, is frequently silenced by methylation in multiple myeloma
Galm, O., Yoshikawa, H., Esteller, M., Osieka, R., & Herman, J. G. (2003) · Blood · doi:10.1182/blood-2002-06-1735 · Cited by 308 · see citing works
Interferon Gamma in Successful Pregnancies1
Murphy, S. P., Tayade, C., Ashkar, A. A., Hatta, K., Zhang, J., & Croy, B. A. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.073353 · Cited by 305 · see citing works
The role of the JAK/STAT signal pathway in rheumatoid arthritis
Malemud, C. J. (2018) · Therapeutic Advances in Musculoskeletal Disease · doi:10.1177/1759720x18776224 · Cited by 303 · see citing works
SP-RING for SUMO
Hochstrasser, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00519-0 · Cited by 281 · see citing works
STAT1 as a key modulator of cell death
Kim, H. S., & Lee, M. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.09.003 · Cited by 280 · see citing works
Involvement of Suppressor of Cytokine Signaling-3 as a Mediator of the Inhibitory Effects of IL-10 on Lipopolysaccharide-Induced Macrophage Activation
Berlato, C., Cassatella, M. A., Kinjyo, I., Gatto, L., Yoshimura, A., & Bazzoni, F. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.12.6404 · Cited by 267 · see citing works
Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases
Hafizi, S., & Dahlbäck, B. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2006.04.004 · Cited by 261 · see citing works
CD8+ T Cell–Mediated Skin Disease in Mice Lacking IRF-2, the Transcriptional Attenuator of Interferon-α/β Signaling
Hida, S., Ogasawara, K., Sato, K., Abe, M., Takayanagi, H., Yokochi, T., Sato, T., Hirose, S., Shirai, T., Taki, S., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)00064-9 · Cited by 251 · see citing works
Stat3: linking inflammation to epithelial cancer - more than a "gut" feeling?
Jarnicki, A., Putoczki, T. L., & Ernst, M. (2010) · Cell Division · doi:10.1186/1747-1028-5-14 · Cited by 240 · see citing works
Suppressor of cytokine signaling (SOCS) 2, a protein with multiple functions
Rico-Bautista, E., Flores‐Morales, A., & Fernández‐Pérez, L. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2006.09.008 · Cited by 208 · see citing works
Tuberculosis in Poorly Controlled Type 2 Diabetes: Altered Cytokine Expression in Peripheral White Blood Cells
Restrepo, B. I., Fisher‐Hoch, S. P., Pino, P. A., Salinas, A., Rahbar, M. H., Mora, F., Cortes-Penfield, N. W., & McCormick, J. B. (2008) · Clinical Infectious Diseases · doi:10.1086/590565 · Cited by 191 · see citing works
Potential therapeutic targets for inflammation in toll-like receptor 4 (TLR4)-mediated signaling pathways
Roy, A., Srivastava, M., Saqib, U., Liu, D., Faisal, S. M., Sugathan, S., Bishnoi, S., & Baig, M. S. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2016.08.026 · Cited by 192 · see citing works
SCFHOS ubiquitin ligase mediates the ligand‐induced down‐regulation of the interferon‐α receptor
Kumar, S., Tang, W., Ravindranath, A. K., Clark, W. A., Croze, E., & Fuchs, S. Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg524 · Cited by 187 · see citing works
SOCS-1/SSI-1-Deficient NKT Cells Participate in Severe Hepatitis through Dysregulated Cross-Talk Inhibition of IFN-γ and IL-4 Signaling In Vivo
Naka, T., Tsutsui, H., Fujimoto, M., Kawazoe, Y., Kohzaki, H., Morita, Y., Nakagawa, Narazaki, M., Adachi, K., Yoshimoto, T., et al. (2001) · Immunity · doi:10.1016/s1074-7613(01)00132-7 · Cited by 186 · see citing works
The many faces of the SOCS box
Piessevaux, J., Lavens, D., Peelman, F., & Tavernier, J. H. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.08.006 · Cited by 176 · see citing works
Biological Evidence That SOCS-2 Can Act Either as an Enhancer or Suppressor of Growth Hormone Signaling
Greenhalgh, C. J., Metcalf, D., Thaus, A. L., Corbin, J. E., Uren, R. T., Morgan, P. O., Fabri, L., Zhang, J., Martin, H. M., Willson, T. A., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200450200 · Cited by 168 · see citing works
Self-citation
Dendritic Cell Maturation Requires STAT1 and Is under Feedback Regulation by Suppressors of Cytokine Signaling
Jackson, S. H., Yu, C., Mahdi, R. M., Ebong, S., & Egwuagu, C. E. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2307 · Cited by 167 · see citing works
Signal transducer and activator of transcription (STAT) signalling and T‐cell lymphomas
Mitchell, T. J., & John, S. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02091.x · Cited by 163 · see citing works
In vivo activation of STAT3 in cutaneous T-cell lymphoma. Evidence for an antiapoptotic function of STAT3
Sommer, V. H., Clemmensen, O. J., Nielsen, O., Wasik, M. A., Lovato, P., Brender, C., Eriksen, K., Woetmann, A., Kæstel, C. G., Nissen, M. H., et al. (2004) · Leukemia · doi:10.1038/sj.leu.2403385 · Cited by 162 · see citing works
STAT‐1: a novel regulator of apoptosis
Stephanou, A., & Latchman, D. S. (2003) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2003.00363.x · Cited by 152 · see citing works
Opposing actions of STAT-1 and STAT-3
Stephanou, A., & Latchman, D. S. (2005) · Growth Factors · doi:10.1080/08977190500178745 · Cited by 153 · see citing works
Leptin-Induced JAK/STAT Signaling and Cancer Growth
Mullen, M., & Gonzalez-Perez, R. R. (2016) · Vaccines · doi:10.3390/vaccines4030026 · Cited by 151 · see citing works
The JAK/STAT Pathway in Skeletal Muscle Pathophysiology
Moresi, V., Adamo, S., & Berghella, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00500 · Cited by 141 · see citing works
Dendritic Cells Transduced with SOCS-3 Exhibit a Tolerogenic/DC2 Phenotype That Directs Type 2 Th Cell Differentiation In Vitro and In Vivo
Li, Y., Chu, N., Rostami, A. M., & Zhang, G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1679 · Cited by 141 · see citing works
The Role of the JAK/STAT Signaling Pathway in the Pathogenesis of Alzheimer’s Disease: New Potential Treatment Target
Rusek, M., Smith, J., El-Khatib, K., Aikins, K., Czuczwar, S. J., & Pluta, R. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010864 · Cited by 145 · see citing works
Protein Tyrosine Phosphatase 1B Attenuates Growth Hormone-Mediated JAK2-STAT Signaling
Gu, F., Dubé, N., Kim, J. W., Cheng, A., Ibarra-Sánchez, M. D. J., Tremblay, M. L., & Boisclair, Y. R. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.11.3753-3762.2003 · Cited by 136 · see citing works
Impaired IFN-γ-Dependent Inflammatory Responses in Human Keratinocytes Overexpressing the Suppressor of Cytokine Signaling 1
Federici, M., Giustizieri, M. L., Scarponi, C., Girolomoni, G., & Albanesi, C. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.1.434 · Cited by 136 · see citing works
Targeting the JAK/STAT pathway in solid tumors
Qureshy, Z., Johnson, D. E., & Grandis, J. R. (2020) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2020.58 · Cited by 134 · see citing works
Negative Regulators of JAK/STAT Signaling in Rheumatoid Arthritis and Osteoarthritis
Malemud, C. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030484 · Cited by 122 · see citing works
The role of IL-11 in immunity and cancer
Xu, D. H., Zhu, Z., Wakefield, M. R., Xiao, H., Bai, Q., & Fang, Y. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.01.004 · Cited by 134 · see citing works
Defective macrophage function in neonates and its impact on unresponsiveness of neonates to polysaccharide antigens
Chelvarajan, R. L., Collins, S. M., Doubinskaia, I. E., Goes, S. W., Willigen, J. V., Flanagan, D. L., de Villiers, W. J. S., Bryson, J. S., & Bondada, S. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0403179 · Cited by 118 · see citing works
In silico identification of the key components and steps in IFN‐γ induced JAK‐STAT signaling pathway
Zi, Z., Cho, K., Sung, M., Xia, X., Zheng, J., & Sun, Z. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.009 · Cited by 117 · see citing works
A Point Mutation in Suppressor of Cytokine Signalling 2 (Socs2) Increases the Susceptibility to Inflammation of the Mammary Gland while Associated with Higher Body Weight and Size and Higher Milk Production in a Sheep Model
Rupp, R., Senin, P., Sarry, J., Allain, C., Tasca, C., Ligat, L., Portes, D., Woloszyn, F., Bouchez, O., Tabouret, G., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005629 · Cited by 113 · see citing works
JAK/STAT/SOCS SIGNALING CIRCUITS AND ASSOCIATED CYTOKINE-MEDIATED INFLAMMATION AND HYPERTROPHY IN THE HEART
Terrell, A. M., Crisostomo, P. R., Wairiuko, G. M., Wang, M., Morrell, E. D., & Meldrum, D. R. (2006) · Shock · doi:10.1097/01.shk.0000226341.32786.b9 · Cited by 114 · see citing works
Role of STAT‐1 and STAT‐3 in ischaemia/reperfusion injury
Stephanou, A. (2004) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2004.tb00476.x · Cited by 110 · see citing works
Mast cell homeostasis and the JAK–STAT pathway
Morales, J. K., Falanga, Y. T., Depcrynski, A., Fernando, J. F. A., & Ryan, J. J. (2010) · Genes and Immunity · doi:10.1038/gene.2010.35 · Cited by 109 · see citing works
MDA5 and PTPN2, two candidate genes for type 1 diabetes, modify pancreatic β-cell responses to the viral by-product double-stranded RNA
Colli, M. L., Moore, F., Gurzov, E. N., Ortis, F., & Eizirik, D. L. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp474 · Cited by 103 · see citing works
T‐cell protein tyrosine phosphatase is a key regulator in immune cell signaling: lessons from the knockout mouse model and implications in human disease
Doody, K. M., Bourdeau, A., & Tremblay, M. L. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00743.x · Cited by 101 · see citing works
Role of growth hormone, insulin-like growth factor-I, and insulin-like growth factor binding proteins in the catabolic response to injury and infection
Lang, C. H., & Frost, R. A. (2002) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200205000-00006 · Cited by 99 · see citing works
Augmented Expression of Cardiotrophin-1 in Failing Human Hearts Is Accompanied by Diminished Glycoprotein 130 Receptor Protein Abundance
Zolk, O., Ng, L. L., O’Brien, R. J., Weyand, M., & Thomas Eschenhagen, A. (2002) · Circulation · doi:10.1161/01.cir.0000033117.39335.df · Cited by 94 · see citing works
Protective effect of curcumin on TNBS-induced intestinal inflammation is mediated through the JAK/STAT pathway
Zhang, X., Wu, J., Ye, B., Wang, Q., Xie, X., & Shen, H. (2016) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-016-1273-z · Cited by 93 · see citing works
STAT3: A Novel Molecular Mediator of Resistance to Chemoradiotherapy
Spitzner, M., Ebner, R., Wolff, H. A., Ghadimi, Β. M., Wienands, J., & Grade, M. (2014) · Cancers · doi:10.3390/cancers6041986 · Cited by 91 · see citing works
Two Drosophila suppressors of cytokine signaling (SOCS) differentially regulate JAK and EGFR pathway activities
Rawlings, J. S., Rennebeck, G., Harrison, S. M. W., Xi, R., & Harrison, D. A. (2004) · BMC Cell Biology · doi:10.1186/1471-2121-5-38 · Cited by 90 · see citing works
Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin
Hafizi, S., Alindri, F., Karlsson, R., & Dahlbäck, B. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02718-3 · Cited by 88 · see citing works
Infection-induced IL-10 and JAK-STAT
Carey, A. J., Tan, C. K., & Ulett, G. C. (2012) · JAK-STAT · doi:10.4161/jkst.19918 · Cited by 86 · see citing works
Human Parvovirus B19 NS1 Protein Modulates Inflammatory Signaling by Activation of STAT3/PIAS3 in Human Endothelial Cells
Duechting, A., Tschöpe, C., Kaiser, H., Lamkemeyer, T., Tanaka, N., Aberle, S., Lang, F. J. W., Torresi, J., Kandolf, R., & Bock, C. –. (2008) · Journal of Virology · doi:10.1128/jvi.00891-08 · Cited by 85 · see citing works
STAT Signaling in Glioma Cells
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SOCS2 Induces Neurite Outgrowth by Regulation of Epidermal Growth Factor Receptor Activation
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Authors: Greenhalgh, C. J., & Hilton, D. J.
Affiliations: Walter and Eliza Hall Institute of Medical Research (AU)
Corresponding author: Greenhalgh, Christopher J
ORCID: Hilton, Douglas J
Venue: Journal of Leukocyte Biology
Publisher: Oxford University Press (OUP)
Published: 2001-09-01
Volume: 70
Issue: 3
Pages: 348-356
ISSN: 0741-5400 (ISSN-L)
1938-3673
DOI: 10.1189/jlb.70.3.348
OpenAlex: W2107469094
Cited by: 258
References: 93
Citations by year: 2026: 1 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 4 · 2017: 11 · 2016: 14 · 2015: 9 · 2014: 13 · 2013: 11 · 2012: 13
FWCI: 10.00
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: Journal of Leukocyte Biology (publishedVersion)
PubMed (publishedVersion)
Funders: Anti-Cancer Council of Victoria, Melbourne, Australia
National Health and Medical Research Council, Canberra, Australia
National Institutes of Health (CA-22556)
Australian Federal Government Cooperative Research Centers Program
Topics: Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: cytokine signaling, negative regulation, suppressor of cytokine signaling, STAT proteins, negative feedback loop, signal attenuation, protein phosphatase, transcriptional repression, DNA-binding activity
MeSH terms: Suppressor of Cytokine Signaling 1 Protein, Suppressor of Cytokine Signaling 3 Protein, Animals, Carrier Proteins, DNA-Binding Proteins, Models, Biological, Proteins, Repressor Proteins, Transcription Factors, Signal Transduction, Trans-Activators, Cytokines, Protein Tyrosine Phosphatases, Intracellular Signaling Peptides and Proteins, Suppressor of Cytokine Signaling Proteins, Protein Inhibitors of Activated STAT, Mice

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