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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Jung, J.-S., Kim, D., & Kim, H.-S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.05.117 · Cited by 61
Prolactin regulates ZNT2 expression through the JAK2/STAT5 signaling pathway in mammary cells.
Qian, L.-X., López, V., Seo, Y., & Kelleher, S. (2009) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00589.2008 · Cited by 59
DNA Methylation Represses IFN-γ–Induced and Signal Transducer and Activator of Transcription 1–Mediated IFN Regulatory Factor 8 Activation in Colon Carcinoma Cells
McGough, J. M., Yang, D., Huang, S., Georgi, D. E., Hewitt, S. M., Röcken, C., Tänzer, M., Ebert, M. P., & Liu, K. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0280 · Cited by 61
“The phosphorylated STAT1 (pSTAT1) is translocated to the nucleus as an active transcription factor (15-17) and binds to the IFN-g activation site (GAS) element to activate transcription of the primary IFN-g response genes (13, 18).”
Background
Respiratory Syncytial Virus-Inducible BCL-3 Expression Antagonizes the STAT/IRF and NF-κB Signaling Pathways by Inducing Histone Deacetylase 1 Recruitment to the Interleukin-8 Promoter
Jamaluddin, M., Choudhary, S., Wang, S., Casola, A., Huda, R., Garofalo, R. P., Ray, S., & Brasier, A. R. (2005) · Journal of Virology · doi:10.1128/jvi.79.24.15302-15313.2005 · Cited by 58
“Activated STATs then form homo- or heterodimers through intermolecular SH2 phosphotyrosine interactions and are subsequently translocated into the nucleus in distinct binding complexes dictated by the nature of the stimulus and target promoters (13).”
Background
Malignant JAK-signaling: at the interface of inflammation and malignant transformation
Perner, F., Pahl, H. L., Zeiser, R., & Heidel, F. H. (2025) · Leukemia · doi:10.1038/s41375-025-02569-8 · Cited by 71
“…expression of growth-and in ﬂ ammatory factors is an evolutionarily conserved cellular response mechanism following stimulation of JAK-dependent receptors [39, 40, 167], yet a speci ﬁ c set of key transcriptional targets have been characterized in the presence of the JAK2-V617F mutation [168, 169].”
A Decade of JAK Inhibitors: What Have We Learned and What May Be the Future?
Liu, C., Kieltyka, J., Fleischmann, R., Gadina, M., & O’Shea, J. J. (2021) · Arthritis & Rheumatology · doi:10.1002/art.41906 · Cited by 69
RIOK3 Is an Adaptor Protein Required for IRF3-Mediated Antiviral Type I Interferon Production
Feng, J., Jesus, P. D. D., Su, V., Han, S., Gong, D., Wu, N. C., Tian, Y., Li, X., Wu, T.-T., Chanda, S. K., et al. (2014) · Journal of Virology · doi:10.1128/jvi.00643-14 · Cited by 54
Chemotherapeutic agents for the treatment of hepatocellular carcinoma: efficacy and mode of action
Shaaban, S., Negm, A., Ibrahim, E. E., & Elrazak, A. A. (2014) · Oncology Reviews · doi:10.4081/oncol.2014.246 · Cited by 56
Chicken interferons, their receptors and interferon-stimulated genes
Goossens, K. E., Ward, A. C., Lowenthal, J. W., & Bean, A. G. D. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.05.020 · Cited by 61
Innate Immune Defense Defines Susceptibility of Sarcoma Cells to Measles Vaccine Virus-Based Oncolysis
Berchtold, S., Lampe, J. W., Weiland, T., Smirnow, I., Schleicher, S., Handgretinger, R., Kopp, H., Reiser, J., Stubenrauch, F., Mayer, N., et al. (2013) · Journal of Virology · doi:10.1128/jvi.02106-12 · Cited by 58
“Secreted IFN binds to its cognate receptor, thus activating the Janus kinase signal transducer and activator of transcription (JAK/Stat) signaling pathway (18).”
Background
Molecular and Cellular Mechanisms of Hexavalent Chromium-Induced Lung Cancer: An Updated Perspective
Urbano, A. M., Ferreira, L. M. R., & Alpoim, M. C. (2012) · Current Drug Metabolism · doi:10.2174/138920012799320464 · Cited by 59
“ing [297] and is required to induce innate immune antiviral and antiproliferative responses [298,299].”
Background
The potential role of JAK2/STAT3 pathway on the anti-apoptotic effect of recombinant human erythropoietin (rhEPO) after experimental traumatic brain injury of rats
Zhao, J., Li, G., Zhang, Y., Su, X., & Hang, C. (2011) · Cytokine · doi:10.1016/j.cyto.2011.07.018 · Cited by 60
“The janus kinase/signal transducer and activator of transcription (JAK/STAT) is an important pathway responding to cytokines by transducing signals from cell surface to the nucleus [12].”
Background
AIP1 prevents graft arteriosclerosis by inhibiting IFN-γ-dependent smooth muscle cell proliferation and intimal expansion
Yu, L., Qin, L.-F., Zhang, H.-F., He, Y., Chen, H., Pober, J., Tellides, G., & Min, W. (2011) · Circulation Research · doi:10.1161/circresaha.111.248245 · Cited by 58
Hyperglycaemic conditions hamper keratinocyte locomotion via sequential inhibition of distinct pathways: new insights on poor wound closure in patients with diabetes
Lan, C., Wu, C.-S., Kuo, H. ‐., Huang, S.-H., & Chen, G.-S. (2009) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2009.09089.x · Cited by 58
Interleukin‐6 induces proliferation in adult spinal cord‐derived neural progenitors via the JAK2/STAT3 pathway with EGF‐induced MAPK phosphorylation
Kang, M.-S., & Kang, S. K. (2008) · Cell Proliferation · doi:10.1111/j.1365-2184.2008.00537.x · Cited by 52
JAK/STAT Signaling and Cervical Cancer: From the Cell Surface to the Nucleus
Valle‐Mendiola, A., Gutiérrez‐Hoya, A., & Soto‐Cruz, I. (2023) · Genes · doi:10.3390/genes14061141 · Cited by 63
“Three cytokine-receptor families activate JAK1: Cytokine receptors with the γ common (γc) receptor subunit (also known as IL-2 family receptors) such as IL-2R, IL-4R, IL-7R, IL-9R, and IL-15R receptors; class II cytokine receptors, which include the IFNα/βR, IFN-γR, and IL-10 family cytokine receptors; and cell membra…”
BackgroundInfluential
HIF‐1, the Warburg Effect, and Macrophage/Microglia Polarization Potential Role in COVID‐19 Pathogenesis
Ferraro, E., Germanò, M., Mollace, R., Mollace, V., & Malara, N. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8841911 · Cited by 62
M2-like polarization of THP-1 monocyte-derived macrophages under chronic iron overload
Kao, J., Wang, S., Ho, L.-W., Huang, S., Lee, C., Lee, M.-S., Yang, R., & Shieh, J. (2020) · Annals of Hematology · doi:10.1007/s00277-020-03916-8 · Cited by 61
Hydrogen Sulfide Prevents Elastin Loss and Attenuates Calcification Induced by High Glucose in Smooth Muscle Cells through Suppression of Stat3/Cathepsin S Signaling Pathway
Zhou, Y.-B., Zhou, H., Li, L., Kang, Y., Cao, X., Wu, Z., Ding, L., Sethi, G., & Bian, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174202 · Cited by 57
“Stat3, an inducible monomeric transcription factor, dimerizes upon phosphorylation, and then translocates to the nucleus for exerting its functions on cell proliferation, angiogenesis, apoptotic resistance, and tumor evasion [37,38].”
Background
Characterization of the Mollusc RIG-I/MAVS Pathway Reveals an Archaic Antiviral Signalling Framework in Invertebrates
Huang, B., Zhang, L., Du, Y., Xu, F., Li, L., & Zhang, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-08566-x · Cited by 64
ADAR1 , inosine and the immune sensing system: distinguishing self from non‐self
Liddicoat, B., Chalk, A. M., & Walkley, C. R. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1322 · Cited by 58
IRF-1 responsiveness to IFN-γ predicts different cancer immune phenotypes
Murtas, D., Maric, D., Giorgi, V. D., Reinboth, J., Worschech, A., Fetsch, P. A., Filie, A. C., Ascierto, M. L., Bedognetti, D., Liu, Q., et al. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.335 · Cited by 59
Inhibitory effects of melatonin on the lipopolysaccharide‐induced CC chemokine expression in BV2 murine microglial cells are mediated by suppression of Akt‐induced NF‐κB and STAT/GAS activity
Min, K., Jang, J., & Kwon, T. K. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00943.x · Cited by 53
“Nuclear STAT dimer binds the specific DNA elements, such as interferon-gamma-activated sequence and interferon-sensitive response element [51].”
Background
IRF8 Governs Expression of Genes Involved in Innate and Adaptive Immunity in Human and Mouse Germinal Center B Cells
Shin, D., Lee, C., & Morse, H. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027384 · Cited by 59
An Integrated Pipeline for the Genome-Wide Analysis of Transcription Factor Binding Sites from ChIP-Seq
Mercier, E., Droit, A., Li, L., Robertson, G., Zhang, X., & Gottardo, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016432 · Cited by 47
“Subsequently, STAT proteins translocate to the nucleus and bind to conserved genomic regulatory sequences to rapidly activate gene transcription [42,43].”
Background
Alkylation of Cysteine 468 in Stat3 Defines a Novel Site for Therapeutic Development
Buettner, R., Corzano, R., Rashid, R., Lin, J., Senthil, M., Hedvat, M., Schroeder, A., Mao, A., Herrmann, A., Yim, J. H., et al. (2011) · ACS Chemical Biology · doi:10.1021/cb100253e · Cited by 58
Negative Feedback Regulation of IFN-γ Pathway by IFN Regulatory Factor 2 in Esophageal Cancers
Wang, Y., Liu, D., Chen, P., Koeffler, H. P., Tong, X., & Xie, D. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5021 · Cited by 52
“Thereby, we firstly measured the phosphorylation of STAT-1 after IFN-g treatment, which is the marker of IFN-g pathway (26, 27).”
Method
Characterization of a hypoxia-responsive leptin receptor (omLepR(L)) cDNA from the marine medaka (Oryzias melastigma).
Wong, M., Yu, R., Ng, P., Law, S. H. L., Tsang, A. S. L., & Kong, R. (2007) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2007.01.025 · Cited by 57
Stat5 constitutive activation rescues defects in spinal muscular atrophy
Ting, C.-H., Lin, C.-W., Wen, S.-L., Hsieh-Li, H.-M., & Li, H. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddl482 · Cited by 58
“Stat proteins form homo- or heterodimers that recognize IRE or GAS elements (g-IFN-activated sequence) in the promoter region (48).”
Background
Human tyk2 kinase deficiency: another primary immunodeficiency syndrome.
Watford, W. T., & O'Shea, J. (2006) · Immunity · doi:10.1016/j.immuni.2006.10.007 · Cited by 57
NSD2 promotes tumor angiogenesis through methylating and activating STAT3 protein
Song, D., Lan, J., Chen, Y., Liu, A., Wu, Q., Zhao, C., Feng, Y., Wang, J., Luo, X., Cao, Z., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01747-z · Cited by 70
“Both EZH2 and SET9 are reported to have the ability to methylate STAT3 at different amino residues upon IL-6 stimulation [15, 16].”
BackgroundInfluential
Regulation of Epigenetic Modifiers, Including KDM6B, by Interferon-γ and Interleukin-4 in Human Macrophages
Yıldırım-Buharalıoğlu, G., Bond, M., Sala‐Newby, G. B., Hindmarch, C. C. T., & Newby, A. C. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00092 · Cited by 38
“Biochim Biophys Acta (2014) 1839(8):627–43.”
STAT3 upregulation in pituitary somatotroph adenomas induces growth hormone hypersecretion
Zhou, C., Jiao, Y., Wang, R., Ren, S.-G., Wawrowsky, K., & Melmed, S. K. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78173 · Cited by 61
“STAT3, a member of the STAT family, participates in cellular responses to cytokines and growth factors (9).”
Bioactive sesquiterpene lactones and other compounds isolated from Vernonia cinerea
Youn, U. J., Miklóssy, G., Chai, X., Wongwiwatthananukit, S., Toyama, O., Songsak, T., Turkson, J., & Chang, L. C. (2013) · Fitoterapia · doi:10.1016/j.fitote.2013.12.013 · Cited by 59
“However, the functions of NF-κB and STAT3 extend far beyond the cancer cell and both transcriptional factors are important regulators of immune and inflammatory functions [9,10].”
Background
Intercellular Signalling in the Mammary Gland
Wilde, C., Peaker, M., & Knight, C. (2012) · Springer US · doi:10.1007/978-1-4615-1973-7 · Cited by 56
New mimetic peptides of the kinase-inhibitory region (KIR) of SOCS1 through focused peptide libraries
Doti, N., Scognamiglio, P. L., Madonna, S., Scarponi, C., Ruvo, M., Perretta, G., Albanesi, C., & Marasco, D. (2011) · Biochemical Journal · doi:10.1042/bj20111647 · Cited by 63
Inhibitor of κB Kinase ϵ (IKKϵ), STAT1, and IFIT2 Proteins Define Novel Innate Immune Effector Pathway against West Nile Virus Infection
Perwitasari, O., Cho, H., Diamond, M., & Gale, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.285205 · Cited by 70
Hepatitis B Virus X Protein Impairs Hepatic Insulin Signaling Through Degradation of IRS1 and Induction of SOCS3
Kim, K., Kim, K. H., & Cheong, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008649 · Cited by 62
“However, dominant negative (DN, Tyr705 mutated with Phe) STAT3 significantly decreased the HBx-induced STAT3 (WT or CA) activation (Figure 5D).”
BackgroundInfluential
Type I Interferons and Interferon Regulatory Factors Regulate TNF-Related Apoptosis-Inducing Ligand (TRAIL) in HIV-1-Infected Macrophages
Huang, Y., Walstrom, A., Zhang, L., Zhao, Y. L., Cui, M., Ye, L., & Zheng, J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005397 · Cited by 53
“Tyr701 is obligatory for STAT1 activation, while Ser727 may be required for the maximal induction of STAT1-mediated gene activation [26,66].”
Background
Unraveling Viral Interleukin-6 Binding to gp130 and Activation of STAT-Signaling Pathways Independently of the Interleukin-6 Receptor
Adam, N., Rabe, B., Suthaus, J., Grötzinger, J., Rose‐John, S., & Scheller, J. (2009) · Journal of Virology · doi:10.1128/jvi.01601-08 · Cited by 57
“Dimerization of gp130 with itself or with the appropriate -receptor leads to activation of members of the JAK family of kinases and the STAT1 and STAT3 transcriptional activators (9, 38).”
Background
Gene structures and promoter characteristics of interferon regulatory factor 1 (IRF-1), IRF-2 and IRF-7 from snakehead Channa argus
Jia, W., & Guo, Q. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2007.11.011 · Cited by 59
Urokinase-induced activation of the gp130/Tyk2/Stat3 pathway mediates a pro-inflammatory effect in human mesangial cells via expression of the anaphylatoxin C5a receptor
Shushakova, N., Tkachuk, N., Dangers, M., Tkachuk, S., Park, J.-K., Hashimoto, K., Haller, H., & Dumler, I. (2005) · Journal of Cell Science · doi:10.1242/jcs.02409 · Cited by 56
“Signal transducers and activators of transcription of the Stat family play important roles in regulating immediate-early biological effects initiated by a variety of extracellular ligands including cytokines, chemokines and growth factors (Darnell et al., 1994; Schindler, 1999).”
Background
Immune evasion of SARS-CoV-2 from interferon antiviral system
Min, Y., Huang, M., Sun, X., Dèng, F., Wáng, H., & Ning, Y. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.023 · Cited by 65
“The activated kinases immediately phosphorylate and activate signal transducer and activator of transcription proteins (STAT1 and STAT2) which then combine with IRF9 to form a heterotrimeric transcription factor complex called IFN-stimulated gene factor 3 (ISGF3) [14,25,26].”
The role of Th17 cells in viral infections
Aghbash, P. S., Hemmat, N., Nahand, J. S., Shamekh, A., Memar, M. Y., Babaei, A., & Baghi, H. B. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107331 · Cited by 66
Urinary biomarkers in lupus nephritis
Aragón, C. C., Tafúr, R.-A., Suárez-Avellaneda, A., Martínez, M. T., Salas, A. S.-D. L., & Tobón, G. J. (2020) · Journal of Translational Autoimmunity · doi:10.1016/j.jtauto.2020.100042 · Cited by 91
“The CXCR3 receptor is a chemokine receptor that is located chiefly in CD4⁺ T cells (producer of IFN-ɣ) and has been identified as one of the key receptors for general leukocytic infiltrate in LN. P. Enghard et al. evaluated, using immunohistochemistry and immunofluorescence, the leukocytic infiltrate of 18 patients wi…”
BackgroundInfluential
Role of STAT3 in Genesis and Progression of Human Malignant Gliomas
Ouedraogo, Z. G., Biau, J., Kémény, J., Morel, L., Verrelle, P., & Chautard, E. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0103-0 · Cited by 63
“They therefore induce transcription of specific target genes [16, 17] (Fig.”
Background
Caffeic acid phenethyl ester protects the brain against hexavalent chromium toxicity by enhancing endogenous antioxidants and modulating the JAK/STAT signaling pathway
Mahmoud, A. M., & El-Twab, S. M. A. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.04.073 · Cited by 61
“These dimers translocate into the nucleus, bind to specific cis-elements, and activate transcription of target genes [17,18].”
An Alternative STAT Signaling Pathway Acts in Viral Immunity in Caenorhabditis elegans
Tanguy, M., Véron, L., Stempor, P. A., Ahringer, J., Sarkies, P., & Miska, E. (2017) · mBio · doi:10.1128/mbio.00924-17 · Cited by 55
“Importantly, we recovered an enriched motif that was nearly identical to the motif predicted from our gene expression analysis (Fig 1B) and matching the mammalian IRF and STAT motifs in the JASPAR core database and the consensus core interferon sensitive response element (ISRE) TTCNNTTT (Fig 3E, 3F) [22].”
ISG15 inhibits cancer cell growth and promotes apoptosis
Zhou, M., Chen, F.-Z., Chen, H., Wan, X.-X., Zhou, X., Fang, Q., & Zhang, D. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2845 · Cited by 64
Understanding STAT3 signaling in cardiac ischemia
O’Sullivan, K. E., Breen, E. P., Gallagher, H. C., Buggy, D. J., & Hurley, J. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0543-8 · Cited by 53
“[16] J Mol Cell Cardiol 2012 Mouse Rapamycin induces cardioprotection in ischemia/reperfusion via activation of ERK, STAT3, eNOS, and GSK-3b”
Background
Signal transducers and activators of transcription—from cytokine signalling to cancer biology
Santos, C. I., & Costa‐Pereira, A. P. (2011) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2011.03.003 · Cited by 59
Potential role of NADPH oxidase-mediated activation of Jak2/Stat3 and mitogen-activated protein kinases and expression of TGF-β1 in the pathophysiology of acute pancreatitis
Ju, K. D., Lim, J., Kim, K. H., & Kim, H. (2011) · Inflammation Research · doi:10.1007/s00011-011-0335-4 · Cited by 55
Modulation of SOCS protein expression influences the interferon responsiveness of human melanoma cells
Lesinski, G. B., Zimmerer, J. M., Kreiner, M., Trefry, J. C., Bill, M. A., Young, G. S., Becknell, B., & Carson, W. E. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-142 · Cited by 59
“Janus kinase-signal transducer and activator of transcription (Jak-STAT) pathway (Reviewed in [16,17].”
Background
Src family kinases promote AML cell survival through activation of signal transducers and activators of transcription (STAT)
Ozawa, Y., Williams, A. H., Estes, M. L., Matsushita, N., Boschelli, F., Jove, R., & List, A. F. (2008) · Leukemia Research · doi:10.1016/j.leukres.2007.11.032 · Cited by 57
“signal ransducers and activators of transcription (STATs) are latent ytoplasmic transcription factors, which are activated folowing phosphorylation by both receptor and non-receptor yrosine kinases [1].”
Background
Macrophages in diabetic gastroparesis – the missing link?
Neshatian, L., Gibbons, S. J., & Farrugia, G. (2015) · Neurogastroenterology & Motility · doi:10.1111/nmo.12418 · Cited by 55
Heterogeneity of atherosclerotic plaque macrophage origin, phenotype and functions: Implications for treatment
Nagenborg, J., Goossens, P., Biessen, E. A. L., & Donners, M. M. P. C. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.10.005 · Cited by 50
Interferon Family Cytokines in Obesity and Insulin Sensitivity
Huang, L.-Y., Chiu, C.-J., Hsing, C., & Hsu, Y. (2022) · Cells · doi:10.3390/cells11244041 · Cited by 59
“Signal transduction is dependent on IFN-γ interacting with the IFN-γ α/β receptor and activating the downstream JAK-STAT signaling pathway [60].”
Background
Molecular Structure and Function of Janus Kinases: Implications for the Development of Inhibitors
Garrido-Trigo, A., & Salas, A. (2019) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjz206 · Cited by 63
Downregulation of Interferon-β and Inhibition of TLR3 Expression are associated with Fatal Outcome of Severe Fever with Thrombocytopenia Syndrome
Song, P., Zheng, N., Zhang, L., Liu, Y., Chen, T., Bao, C.-J., Li, Z.-F., Yong, W., Zhang, Y.-Y., Wu, C., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06921-6 · Cited by 54
Combination of IAP antagonist and IFNγ activates novel caspase-10- and RIPK1-dependent cell death pathways
Tanzer, M. C., Khan, N. R., Rickard, J. A., Etemadi, N., Lalaoui, N., Spall, S. K., Hildebrand, J. M., Segal, D., Miasari, M., Chau, D., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2016.147 · Cited by 53
Pretreatment with Fucoidan from Fucus vesiculosus Protected against ConA-Induced Acute Liver Injury by Inhibiting Both Intrinsic and Extrinsic Apoptosis
Li, J., Chen, K., Li, S., Liu, T., Wang, F., Xia, Y., Lu, J., Zhou, Y., & Guo, C. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152570 · Cited by 54
“Gambin and colleagues reported that IFN-γ produced by macrophages combined with membrane receptors to activate JAK1 and JAK2 which recruited STAT1 [47 – 48].”
Ginkgetin inhibits the growth of DU −145 prostate cancer cells through inhibition of signal transducer and activator of transcription 3 activity
Jeon, Y. J., Jung, S., Yun, J., Lee, C. W., Choi, J., Lee, Y., Han, D. C., & Kwon, B. (2015) · Cancer Science · doi:10.1111/cas.12608 · Cited by 60
Protein Tyrosine Phosphatase 1B Is a Regulator of the Interleukin-10–Induced Transcriptional Program in Macrophages
Pike, K. A., Hutchins, A. P., Vinette, V., Théberge, J.-F., Sabbagh, L., Tremblay, M. L., & Miranda‐Saavedra, D. (2014) · Science Signaling · doi:10.1126/scisignal.2005020 · Cited by 57
Inducible STAT3 NH2 terminal mono-ubiquitination promotes BRD4 complex formation to regulate apoptosis
Ray, S., Zhao, Y., Jamaluddin, M., Edeh, C. B., Lee, C., & Brasier, A. R. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.03.007 · Cited by 56
Recent developments on dry eye disease treatment compounds
Colligris, B., Alkozi, H. A., & Pintor, J. J. (2013) · Saudi Journal of Ophthalmology · doi:10.1016/j.sjopt.2013.12.003 · Cited by 55
“After the discovery of JAK’s it was identified as the STAT family of transcription factors (STAT1-5a, 5b and 6).(19) The activation of the cytokine receptor JAK signaling complex leads to the stimulation of JAK kinases resulting in the phosphorylation of receptor chains, creating docking sites for STAT transcription f…”
Background
Risk Factors and Therapeutic Targets in Pancreatic Cancer
Wörmann, S. M., & Algül, H. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00282 · Cited by 51
“The classical STAT tyrosine phosphorylation is mediated by the Janus kinase (JAK) family of tyrosine kinases, which in turn is activated by cytokine and growth factor receptors (189, 190).”
Background
Therapy targets in glioblastoma and cancer stem cells: lessons from haematopoietic neoplasms
Cruceru, M. L., Neagu, M. T., Demoulin, J., & Constantinescu, S. N. (2013) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12122 · Cited by 49
The enigma of the role of Protein inhibitor of Activated STAT3 (PIAS3) in the immune response
Yagil, Z., Nechushtan, H., Kay, G., Yang, C. M., Kemeny, D. M., & Razin, E. (2010) · Trends in Immunology · doi:10.1016/j.it.2010.01.005 · Cited by 52
Targeting of Jak/STAT Pathway in Antigen Presenting Cells in Cancer
Nefedova, Y., & Gabrilovich, D. I. (2007) · Current Cancer Drug Targets · doi:10.2174/156800907780006887 · Cited by 54
HKDC1 promotes tumor immune evasion in hepatocellular carcinoma by coupling cytoskeleton to STAT1 activation and PD-L1 expression
Zhang, Y., Wang, M., Ye, L., Shen, S., Zhang, Y., Qian, X., Zhang, T., Yuan, M., Ye, Z., Cai, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45712-2 · Cited by 53
“Since phosphorylation of STAT1 residue Y701 is essential for its nuclear translocation and transcriptional regulatory activity 25 , we performed WB analysis to examine its phosphorylation levels under HKDC1 KD or loss of hex-okinase activity (i.e., in the HKDC1 S602A variant).”
JAK inhibitors for the treatment of vitiligo
Inoue, S., Suzuki, T., Sano, S., & Katayama, I. (2024) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2023.12.008 · Cited by 62
Feline Infectious Peritonitis Virus Nsp5 Inhibits Type I Interferon Production by Cleaving NEMO at Multiple Sites
Chen, S., Tian, J., Li, Z.-J., Kang, H., Zhang, J., Huang, J., Yin, H., Hu, X.-L., & Qu, L.-D. (2019) · Viruses · doi:10.3390/v12010043 · Cited by 53
“The type I interferons activate the JAK–STAT pathway to stimulate the expression of interferon-stimulated genes (ISGs), which collectively inhibit viral replication and assembly [28].”
Background
Porcine Reproductive and Respiratory Syndrome Virus nsp11 Antagonizes Type I Interferon Signaling by Targeting IRF9
Wang, D., Chen, J.-Y., Yu, C., Zhu, X.-Y., Xu, S.-G., Fang, L.-R., & Xiao, S.-B. (2019) · Journal of Virology · doi:10.1128/jvi.00623-19 · Cited by 53
“Subsequently, the Janus kinase/signal transduction and transcription activator (JAK/STAT) pathway is activated by type I IFNs (9, 10).”
BackgroundInfluential

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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