Cited by 6,080Cytokine Signaling Pathways and Interactionsinterferon and immune responsesNF-κB Signaling Pathways

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

Darnell, James E., Kerr, lan M., Stark, George R.·1994·Science

DOI 10.1126/science.8197455

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Abstract

Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.

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Background
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Background
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Background
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Background
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BackgroundInfluential
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Method
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BackgroundMethod
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Background
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Background
Interaction between STAT3 and GLI1/tGLI1 oncogenic transcription factors promotes the aggressiveness of triple-negative breast cancers and HER2-enriched breast cancer
Sirkisoon, S. R., Carpenter, R. L., Rimkus, T., Anderson, A., Harrison, A., Lange, A. M., Jin, G., Watabe, K., & Lo, H.-W. (2018) · Oncogene · doi:10.1038/s41388-018-0132-4 · Cited by 96
“JAK2 phosphorylates STAT3 at Y705 to activate its nuclear import and transcriptional activity [15, 16].”
Background
The crucial regulatory role of type I interferon in inflammatory diseases
Ji, L., Li, T., Chen, H., Yang, Y., Liu, J., Liu, J., Qiao, W., & Chen, H. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01188-z · Cited by 107
“JAK1 and non-receptor tyrosine kinase 2 (TYK2) are phosphorylated and activated by IFNAR [24], subsequently inducing phosphorylation and dimerization of transcription factors STAT1 and STAT2 [49, 50].”
Background
Erythropoietin as a Neuroprotective Molecule: An Overview of Its Therapeutic Potential in Neurodegenerative Diseases
Rey, F., Balsari, A., Giallongo, T., Ottolenghi, S., Giulio, A. M. D., Samaja, M., & Carelli, S. (2019) · ASN NEURO · doi:10.1177/1759091419871420 · Cited by 115
“…activation of the associated Janus tyrosine kinase 2 (JAK2) and secondary signaling molecules, such as the signal transducer and activator of transcription 5 (STAT5), phosphatidylinositol 3-kinase (PI3K), and mitogenactivated protein kinase (MAPK; Darnell et al., 1994; Constantinescu et al., 1999).”
Background
Update on Janus Kinase Antagonists in Inflammatory Bowel Disease
Boland, B. S., Sandborn, W. J., & Chang, J. T. (2014) · Gastroenterology Clinics of North America · doi:10.1016/j.gtc.2014.05.011 · Cited by 95
β-Catenin/TCF pathway upregulates STAT3 expression in human esophageal squamous cell carcinoma
Yan, S., Zhou, C., Zhang, W., Zhang, G., Zhao, X., Yang, S., Wang, Y., Lü, N., Zhu, H., & Xu, N. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.05.035 · Cited by 98
IFN-α and IFN-λ differ in their antiproliferative effects and duration of JAK/STAT signaling activity
Maher, S., Sheikh, F. G., Scarzello, A. J., Romero-Weaver, A. L., Baker, D., Donnelly, R., & Gamero, A. (2008) · Cancer Biology & Therapy · doi:10.4161/cbt.7.7.6192 · Cited by 95
Upregulation of Protein Phosphatase 2Ac by Hepatitis C Virus Modulates NS3 Helicase Activity through Inhibition of Protein Arginine Methyltransferase 1
Duong, F., Christen, V., Berke, J., Penna, S. H., Moradpour, D., & Heim, M. (2005) · Journal of Virology · doi:10.1128/jvi.79.24.15342-15350.2005 · Cited by 95
“Phosphorylated STATs form dimers, translocate into the nucleus, bind to promoter elements of interferonstimulated genes, and activate the transcription of interferonstimulated genes (7).”
Background
Identification of novel direct Stat3 target genes for control of growth and differentiation
Snyder, M., Huang, X.-Y., & Zhang, J. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706976200 · Cited by 108
Viral infections in humans and mice with genetic deficiencies of the type I IFN response pathway
Meyts, I., & Casanova, J. (2021) · European Journal of Immunology · doi:10.1002/eji.202048793 · Cited by 112
Recent advances in the clinical development of immune checkpoint blockade therapy
Ghahremanloo, A., Soltani, A., Modaresi, S. M. S., & Hashemy, S. I. (2019) · Cellular Oncology · doi:10.1007/s13402-019-00456-w · Cited by 119
Apoptosis-related BCL2-family Members: Key Players in Chemotherapy
Kontos, C. K., Christodoulou, M., & Scorilas, A. (2014) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/18715206113139990091 · Cited by 96
“[302] Darnell, J.”
Background
Interferon‐α and 5‐fluorouracil combination therapy after palliative hepatic resection in patients with advanced hepatocellular carcinoma, portal venous tumor thrombus in the major trunk, and multiple nodules
Nagano, H., Miyamoto, A., Wada, H., Ota, H., Marubashi, S., Takeda, Y., Dono, K., Umeshita, K., Sakon, M., & Monden, M. (2007) · Cancer · doi:10.1002/cncr.23033 · Cited by 94
“membrane type I receptor, IFNAR2.(44) In this regard, we postulated that IFNAR2 expression in HCC tissues may be a useful predictor with which to distinguish between potential responders and nonresponders to IFN/5-FU combination therapy.”
BackgroundInfluential
Flavivirus infection—A review of immunopathogenesis, immunological response, and immunodiagnosis
Chong, H. Y., Leow, C. Y., Majeed, A. B. A., & Leow, C. H. (2019) · Virus Research · doi:10.1016/j.virusres.2019.197770 · Cited by 123
Voluntary exercise protects hippocampal neurons from trimethyltin injury: Possible role of interleukin-6 to modulate tumor necrosis factor receptor-mediated neurotoxicity
Funk, J. A., Gohlke, J. M., Kraft, A. D., McPherson, C. A., Collins, J. B., & Harry, G. J. (2011) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.03.012 · Cited by 95
“STAT3 is activated by cytokine and growth factor binding to cell surface receptors (Darnell et al., 1994; Ihle, 1996).”
Background
Systemic interferon-α regulates interferon-stimulated genes in the central nervous system
Wang, J., Campbell, I. L., & Zhang, H. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002013 · Cited by 99
Anti-inflammatory roles of retinoic acid in rat brain astrocytes: Suppression of interferon-gamma-induced JAK/STAT phosphorylation.
Choi, W.-H., Ji, K.-A., Jeon, S.-B., Yang, M.-S., Kim, H., Min, K.-J., Shong, M., Jou, I., & Joe, E. (2005) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2005.01.110 · Cited by 93
Targeting STAT3 signaling in kidney disease
Pace, J. A., Paladugu, P., Das, B. C., He, C., & Mallipattu, S. K. (2019) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00034.2019 · Cited by 105
SOCS3 revisited: a broad regulator of disease, now ready for therapeutic use?
Mahony, R., Ahmed, S., Diskin, C., & Stevenson, N. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2234-x · Cited by 89
Sorafenib inhibits signal transducer and activator of transcription 3 signaling associated with growth arrest and apoptosis of medulloblastomas
Yang, F., Meter, T. E. V., Buettner, R., Hedvat, M., Liang, W. P., Kowolik, C. M., Mepani, N., Mirosevich, J., Nam, S., Chen, M. Y., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0138 · Cited by 92
“STAT3 proteins have dual roles as cytoplasmic signaling proteins and nuclear transcription factors that activate a diverse set of genes, including some that implicated in malignant progression (9, 10).”
Background
STAT3 in immune responses and inflammatory bowel diseases
Fu, X. Y. (2006) · Cell Research · doi:10.1038/sj.cr.7310029 · Cited by 90
JAK‐STAT core cancer pathway: An integrative cancer interactome analysis
Erdogan, F., Radu, T. B., Orlova, A., Qadree, A., de Araujo, E. D., Israelian, J., Valent, P., Mustjoki, S. M., Herling, M., Moriggl, R., et al. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17228 · Cited by 111
EGCG Inhibits Tumor Growth in Melanoma by Targeting JAK-STAT Signaling and Its Downstream PD-L1/PD-L2-PD1 Axis in Tumors and Enhancing Cytotoxic T-Cell Responses
Menon, D. R., Li, Y., Yamauchi, T., Osborne, D. G., Vaddi, P. K., Wempe, M. F., Zhai, Z., & Fujita, M. (2021) · Pharmaceuticals · doi:10.3390/ph14111081 · Cited by 101
“IFN-γ secreted by immune cells activates JAK/STAT signaling [44,45] to induce PDL1 in tumor cells and various immune cells, including macrophages, T cells, B cells and dendritic cells [46,47].”
Background
The emerging role of signal transducer and activator of transcription 3 in cerebral ischemic and hemorrhagic stroke
Liang, Z., Wu, G., Fan, C., Xu, J., Jiang, S., Yan, X., Di, S., Ma, Z., Hu, W., & Yang, Y. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.11.001 · Cited by 92
Synergistic anti-tumor effect of combined inhibition of EGFR and JAK/STAT3 pathways in human ovarian cancer
Wen, W. X., Wu, J., Liu, L., Tian, Y., Buettner, R., Hsieh, M.-Y., Horne, D. A., Dellinger, T. H., Han, E. S., Jove, R., et al. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0366-5 · Cited by 93
Requirement of histone deacetylase1 (HDAC1) in signal transducer and activator of transcription 3 (STAT3) nucleocytoplasmic distribution
Ray, S., Lee, C., Hou, T., Boldogh, I. R., & Brasier, A. R. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn419 · Cited by 105
“Although the mechanism controlling the nuclear import of STAT3 upon cytokine stimulation is known (2,3), the mechanism by which activated STAT3 export from the nucleus is not well defined.”
Background
Cytokine signalling in embryonic stem cells
Kristensen, D. M., Kalisz, M., & Nielsen, J. H. (2005) · Apmis · doi:10.1111/j.1600-0463.2005.apm_391.x · Cited by 81
“(STAT) family first described for the interferon signalling pathway (1).”
Background
The DNA replication factor MCM5 is essential for Stat1-mediated transcriptional activation
Snyder, M., He, W., & Zhang, J. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507479102 · Cited by 94
SOCS-1 inhibits expression of the antiviral proteins 2',5'-OAS and MxA induced by the novel interferon-lambdas IL-28A and IL-29.
Brand, S., Zitzmann, K., Dambacher, J., Beigel, F., Olszak, T., Vlotides, G., Eichhorst, S., Göke, B., Diepolder, H., & Auernhammer, C. (2005) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2005.04.004 · Cited by 91
Phospho-Ser727 of STAT3 regulates STAT3 activity by enhancing dephosphorylation of phospho-Tyr705 largely through TC45
Wakahara, R., Kunimoto, H., Tanino, K., Kojima, H., Inoue, A., Shintaku, H., & Nakajima, K. (2012) · Genes to Cells · doi:10.1111/j.1365-2443.2011.01575.x · Cited by 95
“…through tyrosine phosphorylation of its critical tyrosine residue in the carboxy-terminal region, STAT protein homo- or heterodimerizes, translocates to the nucleus, and binds to the specific DNA sequences to regulate mRNA expression from by its target genes (Darnell et al. 1994; Darnell 1997).”
Background
Role of Cytokine Signaling during Nervous System Development
Mousa, A., & Bakhiet, M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140713931 · Cited by 103
Differential regulation of CD4+ T helper cell responses by curcumin in experimental autoimmune encephalomyelitis
Kanakasabai, S., Casalini, E. D., Walline, C. C., Mo, C., Chearwae, W., & Bright, J. J. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.10.002 · Cited by 88
“The pathogenesis of EAE/MS is a complex process involving the activation of antigen presenting cells (APCs) such as macrophage and microglia, differentiation of neural antigen-specific Th1/Th17 cells and secretion of inflammatory cytokines in the CNS [22].”
Influential
The STAT3 NH2-terminal Domain Stabilizes Enhanceosome Assembly by Interacting with the p300 Bromodomain
Hou, T., Ray, S., Lee, C., & Brasier, A. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805941200 · Cited by 91
Therapeutic role of beta-interferons in multiple sclerosis
Javed, A., & Reder, A. T. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.08.011 · Cited by 91
STAT3 signaling in ovarian cancer: a potential therapeutic target
Liang, R., Chen, X., Chen, L., Wan, F., Chen, K.-H., Sun, Y., & Zhu, X. (2019) · Journal of Cancer · doi:10.7150/jca.35011 · Cited by 91
Interactions of host IL-6 and IFN-γ and cancer-derived TGF-β1 on MHC molecule expression during tumor spontaneous regression
Hsiao, Y.-W., Liao, K., Chung, T.-F., Ch, L., Hsu, C.-D., & Chu, R. (2008) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-007-0446-5 · Cited by 92
“Cellular responses to IFN- are largely mediated by STAT1 activation and are rarely associated with STAT3 [ 25 ,43].”
BackgroundInfluential
The RAS/Raf1/MEK/ERK Signaling Pathway Facilitates VSV-mediated Oncolysis: Implication for the Defective Interferon Response in Cancer Cells.
Noser, J. A., Mael, A. A., Sakuma, R., Ohmine, S., Marcato, P., Lee, P. W., & Ikeda, Y. (2007) · Molecular Therapy · doi:10.1038/sj.mt.6300193 · Cited by 89
Arbidol: a broad-spectrum antiviral that inhibits acute and chronic HCV infection
Boriskin, Y. S., Pécheur, E., & Polyak, S. (2006) · Virology Journal · doi:10.1186/1743-422x-3-56 · Cited by 89
“1 cells with ARB did not induce phosphorylation on the conserved tyrosine amino acid at position 701 of the Stat1 protein (Figure 4C), an essential requirement and indicator of IFN signaling through the Jak-Stat pathway [19].”
BackgroundMethod
Negative Regulation of the Alpha Interferon-Induced Antiviral Response by the Ras/Raf/MEK Pathway
Battcock, S. M., Collier, T. W., Zu, D., & Hirasawa, K. (2006) · Journal of Virology · doi:10.1128/jvi.80.9.4422-4430.2006 · Cited by 85
“Once secreted, IFN- and IFN- , binding to their cognate receptors, activate the Jak-1 and Tyk-2 kinases, which leads to the phosphorylation of STAT-1 and STAT-2 proteins (14, 54).”
Background
Down‐regulation of cyclin E1 expression by microrna‐195 accounts for interferon‐β‐induced inhibition of hepatic stellate cell proliferation
Sekiya, Y., Ogawa, T., Iizuka, M., Yoshizato, K., Ikeda, K., & Kawada, N. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22598 · Cited by 88
RA-inducible gene-I induction augments STAT1 activation to inhibit leukemia cell proliferation
Jiang, L., Zhang, N., Ding, F., Li, X.-Y., Chen, L., Zhang, H., Zhang, W., Chen, S., Wang, Z., Li, J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019059108 · Cited by 88
A logic-based diagram of signalling pathways central to macrophage activation
Raza, S., Robertson, K. A., Lacaze, P. A., Page, D. L., Enright, A. J., Ghazal, P., & Freeman, T. C. (2008) · BMC Systems Biology · doi:10.1186/1752-0509-2-36 · Cited by 75
“The IRF family of transcription factors bind specific DNA sequences, as do the STAT proteins, present on the promoter of target genes [12,13].”
S‐adenosylmethionine and betaine correct hepatitis C virus induced inhibition of interferon signaling in vitro†
Duong, F. H. T., Christen, V., Sinnreich, M. F., & Heim, M. H. (2006) · Hepatology · doi:10.1002/hep.21116 · Cited by 82
STAT1 from the cell membrane to the DNA
Lillemeier, B. F., Köster, M., & Kerr, I. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2508 · Cited by 88
Concanavalin A-induced liver injury triggers hepatocyte proliferation.
Trautwein, C., Rakemann, T., Malek, N. P., Plümpe, J., Tiegs, G., & Manns, M. P. (1998) · Journal of Clinical Investigation · doi:10.1172/jci504 · Cited by 87
IFIT5 potentiates anti-viral response through enhancing innate immune signaling pathways
Zhang, B., Liu, X., Chen, W., & Chen, L. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt088 · Cited by 87
Astrocytes in injury states rapidly produce anti‐inflammatory factors and attenuate microglial inflammatory responses
Kim, J.-H., Min, K., Seol, W., Jou, I., & Joe, E.-H. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07004.x · Cited by 92
Control of specificity and magnitude of NF-κB and STAT1-mediated gene activation through PIASy and PIAS1 cooperation
Tahk, S., Liu, B., Chernishof, V., Wong, K. A., Wu, H., & Shuai, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701877104 · Cited by 84
SUMO wrestling with type 1 diabetes
Li, M., Guo, D., Isales, C. M., Eizirik, D. L., Atkinson, M. A., She, J., & Wang, C. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0645-5 · Cited by 89
“Signaling through the STAT transcription factors is utilized by a large number of cytokines, growth factors and hormones [34–36].”
Next generation of tumor-activating type I IFN enhances anti-tumor immune responses to overcome therapy resistance
Cao, X., Liang, Y., Hu, Z., Li, H., Yang, J., Hsu, E. J., Zhu, J., Zhou, J., & Fu, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-26112-2 · Cited by 106
“(5) ProIFN can increase CD8+ T cells in the tumor microenvironment, and thus can potentially be used in cold tumors.”
Background
Dual Regulatory Roles of the Phosphatidylinositol 3-Kinase In Interferon Signaling
Kaur, S., Sassano, A., Joseph, A., Majchrzak-Kita, B., Eklund, E., Verma, A., Brachmann, S., Fish, E., & Platanias, L. (2008) · Journal of Immunology · doi:10.4049/jimmunol.181.10.7316 · Cited by 86
Targeting signaling pathways in multiple myeloma: Pathogenesis and implication for treatments
Hu, J., & Hu, W.-X. (2018) · Cancer Letters · doi:10.1016/j.canlet.2017.11.020 · Cited by 84
SnapShot: Jak-STAT Signaling II
Villarino, A. V., Gadina, M., O’Shea, J. J., & Kanno, Y. (2020) · Cell · doi:10.1016/j.cell.2020.04.052 · Cited by 85
The interferon regulatory factors and oncogenesis
Tanaka, N., & Taniguchi, T. (2000) · Seminars in Cancer Biology · doi:10.1006/scbi.2000.0310 · Cited by 85
PaintOmics 4: new tools for the integrative analysis of multi-omics datasets supported by multiple pathway databases
Liu, T., Salguero, P., Petek, M., Martínez-Mira, C., Balzano‐Nogueira, L., Ramšak, Ž., McIntyre, L. M., Gruden, K., Tarazona, S., & Conesa, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac352 · Cited by 105
“STAT4 is a key TF of the immune cell lineage (36), and mir-1883p has been reported to regulate cell proliferation (37).”
Background
Cellular and molecular mechanisms of liver regeneration: Proliferation, growth, death and protection of hepatocytes
Ozaki, M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.10.007 · Cited by 103
Porcine Epidemic Diarrhea Virus Infection Inhibits Interferon Signaling by Targeted Degradation of STAT1
Guo, L., Luo, X., Ren, L., Xu, Y., Zhang, J., Ge, J., Bu, Z., Feng, L., & Wang, Y. (2016) · Journal of Virology · doi:10.1128/jvi.01091-16 · Cited by 87
Hemagglutinin of Influenza A Virus Antagonizes Type I Interferon (IFN) Responses by Inducing Degradation of Type I IFN Receptor 1
Xia, C., Vijayan, M., Pritzl, C. J., Fuchs, S. Y., McDermott, A. B., & Hahm, B. (2015) · Journal of Virology · doi:10.1128/jvi.02749-15 · Cited by 93
p42/p44 MAPK-mediated Stat3Ser727 phosphorylation is required for progestin-induced full activation of Stat3 and breast cancer growth
Tkach, M., Rosemblit, C., Rivas, M. A., Proietti, C. J., Flaqué, M. C. D., Mercogliano, M. F., Béguelin, W., Maronna, E., Guzmán, P., Gercovich, F. G., et al. (2013) · Endocrine Related Cancer · doi:10.1530/erc-12-0194 · Cited by 93
Resveratrol down-regulates interferon-γ-inducible inflammatory genes in macrophages: molecular mechanism via decreased STAT-1 activation
Chung, E. Y., Kim, B. H., Hong, J. T., Lee, C., Ahn, B., Nam, S.-Y., Han, S., & Kim, Y. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.07.012 · Cited by 80
“Upon tyrosine phosphorylation, STAT-1 is released from the receptor, forms a homodimer to function as a transcription factor [15,16] and enters into the nucleus [17,18], where it specifically binds to the IFN-γ-activated sequence (GAS)”
Background
Cancer-Associated Myeloproliferation: Old Association, New Therapeutic Target
Wilcox, R. A. (2010) · Mayo Clinic Proceedings · doi:10.4065/mcp.2010.0077 · Cited by 74
IL-9: Basic Biology, Signaling Pathways in CD4+ T Cells and Implications for Autoimmunity
Li, H., & Rostami, A. M. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9186-y · Cited by 78
JAK2-STAT3 signaling pathway mediates thrombin-induced proinflammatory actions of microglia in vitro
Huang, C., Ma, R., Sun, S., Wei, G., Fang, Y., Liu, R., & Li, G. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.07.004 · Cited by 85
Innate immune response to viral infection of the lungs
See, H. V., & Wark, P. A. B. (2008) · Paediatric Respiratory Reviews · doi:10.1016/j.prrv.2008.04.001 · Cited by 70
MicroRNA-155 Implication in M1 Polarization and the Impact in Inflammatory Diseases
Paşca, S., Jurj, A. M., Petrushev, B., Tomuleasa, C., & Matei, D. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00625 · Cited by 85
“IFNγ acts on the IFNγR, which further recruits JAK1/2 leading to the formation STAT1/STAT2 heterodimers, which act as a transcription factor for NOS2, MHC2 and IL12 (7, 8).”
BackgroundInfluential
Type I Interferon Responses by HIV-1 Infection: Association with Disease Progression and Control
Soper, A., Kimura, I., Nagaoka, S., Konno, Y., Yamamoto, K., Koyanagi, Y., & Sato, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01823 · Cited by 102
“After the entry of ISGF3 complex into the nucleus, this complex binds to the IFN-stimulated response element located in the promoter region of ISGs and initiates their transcription (Figure 2) (15).”
Background
TheDrosophilaJAK-STAT pathway in blood cell formation and immunity
Morin-Poulard, I., Vincent, A., & Crozatier, M. (2013) · JAK-STAT · doi:10.4161/jkst.25700 · Cited by 86
“The Janus kinase-signal transducer and activator of transcription (JAK-STAT) signaling pathway was discovered from studies on the role of interferon in the control of immune responses in mammals.(1) This pathway, which is highly conserved throughout evolution, transduces the activity of a variety of cytokines and grow…”
Method
Cadmium blocks receptor-mediated Jak/STAT signaling in neurons by oxidative stress
Monroe, R. K., & Halvorsen, S. W. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.04.023 · Cited by 83
Role of janus kinase inhibitors in the treatment of alopecia areata
Triyangkulsri, K., & Suchonwanit, P. (2018) · Drug Design, Development and Therapy · doi:10.2147/dddt.s172638 · Cited by 83
“17–19 Subsequently, a large number of cytokines, particularly γ c cytokines, have been found to activate the JAK-STAT pathway, leading to a myriad of gene expression.”
The Complex Role of STAT3 in Viral Infections
Kuchipudi, S. V. (2015) · Journal of Immunology Research · doi:10.1155/2015/272359 · Cited by 88
“Cytokine receptors on plasma membrane do not usually possess intrinsic tyrosine kinase activity and their engagement activates receptor-associated tyrosine kinases, prominent of which are Janus kinase (JAK) family kinases (JAK1, JAK2, JAK3, and TYK2) [3, 4, [8] [9] [10] .”
Background
Inhibiting signal transducer and activator of transcription 3: rationality and rationale design of inhibitors
Mankan, A. K., & Greten, F. R. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.601739 · Cited by 77
“1 Signal transducers and activators of transcription Signal transducer and activator of transcription (STAT) proteins are a group of transcription factors activated in response to various ligands such as cytokines, growth factors and hormones and transduce extracellular and intracellular signals by translocating to th…”
Background
Reactive oxygen species and erectile dysfunction: possible role of NADPH oxidase
Jeremy, J. Y., Jones, R. A., Koupparis, A. J., Hotston, M. R., Persad, R. A., Angelini, G. D., & Shukla, N. (2006) · International Journal of Impotence Research · doi:10.1038/sj.ijir.3901523 · Cited by 86
Up-Regulation of the JAK/STAT1 Signal Pathway during Chlamydia trachomatis Infection
Lad, S. P., Fukuda, E. Y., Li, J., de la Maza, L. M., & Li, E. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.11.7186 · Cited by 75
“STAT1 protein was originally identified as an IFN-induced transcriptional factor (21, 37).”
Background
The Resistance Mechanisms of Lung Cancer Immunotherapy
Wang, F., Wang, S., & Zhou, Q. H. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.568059 · Cited by 90
“Tumors neutralize the impact of IFN-γ by mutating or down-regulating the molecules involved in the IFN-γ signaling pathway, including IFN-γ receptor chains, regulatory factors, JAK1/2, and STATs upon continuous IFN-γ exposure (73, 83).”
Background
Autophagic and Apoptotic Pathways as Targets for Chemotherapy in Glioblastoma
Trejo‐Solís, C., Serrano‐García, N., Escamilla-Ramírez, Á., Castillo‐Rodríguez, R. A., Jiménez‐Farfán, D., Palencia, G., Calvillo, M., Lemus, M. A. A., Flores‐Nájera, A., Cruz-Salgado, A., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123773 · Cited by 87
“JAK phosphorylates receptors with tyrosine kinase activity, which in turn activate the kinases ERK and AKT via the Ras signaling [342].”
Background
The role of the JAK-STAT pathway in neural stem cells, neural progenitor cells and reactive astrocytes after spinal cord injury
Wang, T., Yuan, W., Liu, Y., Zhang, Y., Wang, Z., Zhou, X., Ning, G., Zhang, L., YAO, L., Feng, S., et al. (2014) · Biomedical Reports · doi:10.3892/br.2014.401 · Cited by 84
“The authors also considered JAK-STATs to be crucial in enhancing cell survival in CNS.”

Authors: Darnell, J. E., Kerr, L. M., & Stark, G. R.
Affiliations: Rockefeller University (US)
Case Comprehensive Cancer Center (US)
ORCID: Stark, George R.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-06-03
Volume: 264
Issue: 5164
Pages: 1415-1421
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8197455
OpenAlex: W2029275361
Cited by: 6,080
References: 85
Citations by year: 2026: 84 · 2025: 139 · 2024: 175 · 2023: 170 · 2022: 183 · 2021: 177 · 2020: 162 · 2019: 155 · 2018: 121 · 2017: 166 · 2016: 148 · 2015: 152 · 2014: 160 · 2013: 207 · 2012: 188
FWCI: 28.59
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: JAK/STAT signaling, interferon-alpha, interferon-gamma, signal transduction, STAT proteins, transcriptional activation, JAK kinases, interferon receptor, nuclear translocation, DNA binding
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA-Binding Proteins, Genes, Genetic Complementation Test, Humans, Interferon-gamma, Molecular Sequence Data, Mutation, Protein-Tyrosine Kinases, Regulatory Sequences, Nucleic Acid, Transcription Factors, Signal Transduction, Transcriptional Activation, Interferon-alpha, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

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