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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Role of STAT1, NF-κB, and C/EBPβ in the macrophage transcriptional regulation of hepcidin by mycobacterial infection and IFN-γ
Sow, F. B., Alvarez, G. R., Gross, R. P., Satoskar, A. R., Schlesinger, L. S., Zwilling, B. S., & Lafuse, W. P. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1208719 · Cited by 83
“IFN- induces gene expression by signaling through the JAK-STAT pathway [3, 4], leading to translocation of STAT1 to the nucleus, where it induces expression of IFN- -responsive genes [5].”
Background
Similarities and Differences in Antagonism of Neuron Alpha/Beta Interferon Responses by Venezuelan Equine Encephalitis and Sindbis Alphaviruses
Yin, J., Gardner, C. L., Burke, C., Ryman, K., & Klimstra, W. (2009) · Journal of Virology · doi:10.1128/jvi.01209-09 · Cited by 79
“the noncytolytic clearance of SINV mediated by IFN- (which also signals through the STAT1 pathway [14]) released by T cells (4, 7).”
Background
Interferon-Dependent Engagement of Eukaryotic Initiation Factor 4B via S6 Kinase (S6K)- and Ribosomal Protein S6K-Mediated Signals
Kroczyńska, B., Kaur, S., Katsoulidis, E., Majchrzak-Kita, B., Sassano, A., Kozma, S. C., Fish, E. N., & Platanias, L. C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01537-08 · Cited by 73
Modelling non-stationary gene regulatory processes with a non-homogeneous Bayesian network and the allocation sampler
Grzegorczyk, M., Husmeier, D., Edwards, K., Ghazal, P., & Millar, A. (2008) · Bioinform. · doi:10.1093/bioinformatics/btn367 · Cited by 79
“To assist the elucidation of regulatory network structures, probabilistic machine learning methods based on Bayesian networks can be employed, as proposed in the seminal paper by Friedman et al. (2000). In a nutshell, the idea is to simplify the mathematical description of the biological system by replacing coupled di…”
MethodInfluential
Basal Expression Levels of IFNAR and Jak-STAT Components Are Determinants of Cell-Type-Specific Differences in Cardiac Antiviral Responses
Zurney, J., Howard, K. E., & Sherry, B. (2007) · Journal of Virology · doi:10.1128/jvi.01172-07 · Cited by 68
“ISGF3 complexes translocate to the nucleus and initiate the transcription of many ISGs, including ISG561 and the transcription factor IRF7, leading to the induction of an antiviral state (12).”
Background
Chemotactic Effect of Ciliary Neurotrophic Factor on Macrophages in Retinal Ganglion Cell Survival and Axonal Regeneration
Cen, L., Luo, J.-M., Zhang, C., Fan, Y., Song, Y., So, K., van Rooijen, N., Pang, C. P., Lam, D. S. C., & Cui, Q. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0791 · Cited by 82
The role of protein kinase C δ activation and STAT3 Ser727 phosphorylation in insulin-induced keratinocyte proliferation
Gartsbein, M., Alt, A., Hashimoto, K., Nakajima, K., Kuroki, T., & Tennenbaum, T. (2006) · Journal of Cell Science · doi:10.1242/jcs.02744 · Cited by 81
“Although the role of tyrosine phosphorylation as an essential step for activation of STAT3 is well established (Darnell et al., 1994; Levy and Darnell, 2002), the precise role of a single serine phosphorylation event, such as the one associated with the activation of Ser727 in STAT3, was not known.”
Background
Phosphorylation of TRIM28 Enhances the Expression of IFN-β and Proinflammatory Cytokines During HPAIV Infection of Human Lung Epithelial Cells
Krischuns, T., Günl, F., Henschel, L., Binder, M., Willemsen, J., Schloer, S., Rescher, U., Gerlt, V., Zimmer, G., Nordhoff, C., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02229 · Cited by 83
“Secreted IFNα/β bind to the interferon-α/β receptor on neighboring cells resulting in STAT1/2 phosphorylation by the receptor-associated Jak/Tyk kinases (8).”
Background
Molecular Mechanisms of Neurodegeneration in Spinal Muscular Atrophy
Ahmad, S., Bhatia, K., Kannan, A., & Gangwani, L. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s33122 · Cited by 78
Roles of unphosphorylated ISGF3 in HCV infection and interferon responsiveness
Sung, P. S., Cheon, H., Cho, C. H., Hong, S.-H., Park, D. Y., Seo, H.-I., Park, S., Yoon, S. K., Stark, G. R., & Shin, E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513341112 · Cited by 84
“This transcription factor, IFN-stimulated gene factor 3 (ISGF3), induces the expression of hundreds of ISGs (18, 19).”
BackgroundSelf-citation
Targeting JAK1/STAT3 Signaling Suppresses Tumor Progression and Metastasis in a Peritoneal Model of Human Ovarian Cancer
Wen, W. X., Liang, W. P., Wu, J., Kowolik, C. M., Buettner, R., Scuto, A., Hsieh, M.-Y., Hong, H., Brown, C. E., Forman, S. J., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0077 · Cited by 88
“STAT3 is predominantly located in the cytoplasm in an inactive form, but is activated by phosphorylation at Tyr705 by the Janus family kinases (JAK) (25).”
Influenza A Virus-Induced Degradation of Eukaryotic Translation Initiation Factor 4B Contributes to Viral Replication by Suppressing IFITM3 Protein Expression
Wang, S., Chi, X., Wei, H., Chen, Y., Chen, Z., Huang, S., & Chen, J. (2014) · Journal of Virology · doi:10.1128/jvi.00126-14 · Cited by 79
“Although it is well recognized that the JAK/STAT pathway plays crucial roles in type I, II, and III IFN-dependent transcription of ISGs (47), the regulation of mRNA translation for these IFN-sensitive genes remains elusive.”
Background
Activation of the Ras/Raf/MEK Pathway Facilitates Hepatitis C Virus Replication via Attenuation of the Interferon-JAK-STAT Pathway
Zhang, Q., Gong, R., Qu, J., Zhou, Y., Liu, W., Chen, M., Liu, Y., Zhu, Y., & Wu, J. (2011) · Journal of Virology · doi:10.1128/jvi.00688-11 · Cited by 74
Role of Interferon α (IFNα)-inducible Schlafen-5 in Regulation of Anchorage-independent Growth and Invasion of Malignant Melanoma Cells
Katsoulidis, E., Mavrommatis, E., Woodard, J., Shields, M. A., Sassano, A., Carayol, N., Sawicki, K. T., Munshi, H. G., & Platanias, L. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.151076 · Cited by 91
Suppression of thymus- and activation-regulated chemokine (TARC/CCL17) production by 1,2,3,4,6-penta-O-galloyl-β-d-glucose via blockade of NF-κB and STAT1 activation in the HaCaT cells
Ju, S. M., Song, H. Y., Lee, S. J., Seo, W. Y., Sin, D. H., Goh, A. R., Kang, Y., Kang, I.-J., Won, M., Yi, J., et al. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.137 · Cited by 75
Non-DNA-binding platinum anticancer agents: Cytotoxic activities of platinum–phosphato complexes towards human ovarian cancer cells
Bose, R., Maurmann, L., Mishur, R. J., Yasui, L., Gupta, S., Grayburn, W. S., Hofstetter, H., & Salley, T. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0803094105 · Cited by 78
Physical and functional interactions between STAT3 and KAP1
Tsuruma, R., Ohbayashi, N., Kamitani, S., Ikeda, O., Sato, N., Muromoto, R., Sekine, Y., Oritani, K., & Matsuda, T. (2007) · Oncogene · doi:10.1038/sj.onc.1210952 · Cited by 77
STAT5 Phosphorylation in Malignant Melanoma Is Important for Survival and Is Mediated Through SRC and JAK1 Kinases
Mirmohammadsadegh, A., Hassan, M., Bardenheuer, W., Marini, A., Gustrau, A., Nambiar, S., Tannapfel, A., Bojar, H., Ruzicka, T., & Hengge, U. R. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700385 · Cited by 72
Novel type I interferon IL-28A suppresses hepatitis C viral RNA replication
Zhu, H.-Z., Butera, M., Nelson, D., & Liu, C. (2005) · Virology Journal · doi:10.1186/1743-422x-2-80 · Cited by 78
“We further analyzed the expression of ISGs using a RTPCR approach.”
BackgroundInfluential
Immune checkpoint inhibitors in colorectal cancer: limitation and challenges
Yan, S., Wang, W., Feng, Z., Xue, J., Liang, W., Wu, X., Tan, Z., Zhang, X., Zhang, S., Li, X., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1403533 · Cited by 83
The long non-coding RNA LUCAT1 is a negative feedback regulator of interferon responses in humans
Agarwal, S., Vierbuchen, T., Ghosh, S., Chan, J., Jiang, Z., Kandasamy, R. K., Ricci, E. P., & Fitzgerald, K. A. (2020) · Nature Communications · doi:10.1038/s41467-020-20165-5 · Cited by 82
Active vitamin D regulates macrophage M1/M2 phenotypes via the STAT‐1‐TREM‐1 pathway in diabetic nephropathy
Zhang, X., Zhao, Y., Zhu, X., Guo, Y., Yang, Y., Jiang, Y., & Liu, B. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27450 · Cited by 84
“Darnell, Kerr, and Stark (1994) found that IFN‐γ and LPS promote the activation of M1 macrophages, which is mediated by STAT1.”
Background
Aloperine induces G2/M phase cell cycle arrest and apoptosis in HCT116 human colon cancer cells
Zhang, L., ZHENG, Y., Deng, H., Liang, L., & Peng, J. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1718 · Cited by 81
“Stat proteins are involved in the regulation of fundamental cell processes, such as cell growth, differentiation, and survival (30).”
IFNB1/interferon-β-induced autophagy in MCF-7 breast cancer cells counteracts its proapoptotic function
Ambjørn, M., Ejlerskov, P., Liu, Y., Lees, M. J., Jäättelä, M., & Issazadeh‐Navikas, S. (2012) · Autophagy · doi:10.4161/auto.22831 · Cited by 81
TYK2 Kinase Activity Is Required for Functional Type I Interferon Responses In Vivo
Prchal‐Murphy, M., Semper, C., Lassnig, C., Wallner, B., Gausterer, C., Ingeborg, T., Kobolák, J., Müller, S., Kolbe, T., Karaghiosoff, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039141 · Cited by 75
“canonical – JAK-STAT signalling pathway [3].”
Lestaurtinib Inhibition of the JAK/STAT Signaling Pathway in Hodgkin Lymphoma Inhibits Proliferation and Induces Apoptosis
Díaz, T., Navarro, A., Ferrer, G., Gel, B., Gaya, A., Artells, R., Bellosillo, B., García-García, M., Serrano, S., Martínez, A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018856 · Cited by 77
“The JAK2/STAT5 pathway is a common signaling pathway used by many cytokines that regulate target gene expression related to cell survival, proliferation, angiogenesis, and immune evasion [2].”
Background
Implication of TRIMalpha and TRIMCyp in interferon-induced anti-retroviral restriction activities
Carthagéna, L., Parise, M. C., Ringeard, M., Chelbi‐Alix, M. K., Hazan, U., & Nisole, S. (2008) · Retrovirology · doi:10.1186/1742-4690-5-59 · Cited by 70
“In order to verify if non-human primate cells are responsive to human IFN treatment, we looked at Stat1 phosphorylation, which is an early post-receptor signaling element of both type I and type II IFN pathways, and can thus serve as a positive-indicator of IFN signaling [26].”
Background
IFN- γ Therapy of Tuberculosis and Related Infections
Reljić, R. (2007) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2006.0103 · Cited by 72
“Elucidation of the IFN-(cid:2) action led to the discovery of the Jak-Stat signaling pathway, 5 which is used also by numerous other cytokines.”
Paeonol attenuates TNBS-induced colitis by inhibiting NF-κB and STAT1 transactivation
Ishiguro, K., Ando, T., Maeda, O., Hasegawa, M., Kadomatsu, K., Ohmiya, N., Niwa, Y., Xavier, R. J., & Goto, H. (2006) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2006.07.002 · Cited by 74
Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54
Terenzi, F., Pal, S., & Sen, G. C. (2005) · Virology · doi:10.1016/j.virol.2005.06.011 · Cited by 67
“IFN, on the other hand, induces the same genes using the same cis-element, ISRE, but a different transcription factor, ISGF-3, that is composed of IRF-9, STAT1 and STAT2 (Darnell et al., 1994; Stark et al., 1998; Levy and Darnell, 2002).”
Interferon Induces NF-κB-inducing Kinase/Tumor Necrosis Factor Receptor-associated Factor-dependent NF-κB Activation to Promote Cell Survival*
Yang, C.-H., Murti, A., & Pfeffer, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503120200 · Cited by 77
TLR 3 and MDA 5 signalling, although not expression, is impaired in asthmatic epithelial cells in response to rhinovirus infection.
Parsons, K. S., Hsu, A., & Wark, P. A. B. (2013) · Clinical & Experimental Allergy · doi:10.1111/cea.12218 · Cited by 75
Role of Krüppel-Like Factor 4 in Neurogenesis and Radial Neuronal Migration in the Developing Cerebral Cortex
Qin, S., & Zhang, C. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00838-12 · Cited by 78
“To examine this possibility, we used a dominant negative form of STAT3 (dnSTAT3) in which the Y705 residue was mutated to phenylalanine, thereby preventing its phosphorylation and activation (7, 13).”
Method
VEGF receptors on chronic lymphocytic leukemia (CLL) B cells interact with STAT 1 and 3: implication for apoptosis resistance
Lee, Y. K., Shanafelt, T. D., Bone, N. D., Strege, A. K., Jelinek, D. F., & Kay, N. E. (2005) · Leukemia · doi:10.1038/sj.leu.2403667 · Cited by 125
Interferon Regulatory Factor 9 Structure and Regulation
Paul, A., Tang, T., & Ng, S. K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01831 · Cited by 90
“ISGF3 will translocate into the nucleus and binds to the promoter region of interferon-stimulated response element (ISRE) to activate the transcription of ISGs (37).”
Background
The crossroads of breast cancer progression: insights into the modulation of major signaling pathways
Velloso, F. J., Bianco, A. F. R., Farias, J. O., Torres, N., Ferruzo, P. Y. M., Anschau, V., Jesus-Ferreira, H. C., Chang, T., Sogayar, M. C., Zerbini, L. F., et al. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s142154 · Cited by 94
“tutively associated with the receptor), and STATs (latent cytoplasmic transcription factors).(162) JAKs are cytoplasmic TKs”
Effect of the JAK2/STAT3 inhibitor SAR317461 on human glioblastoma tumorspheres
Mukthavaram, R., Ouyang, X., Saklecha, R., Jiang, P., Nomura, N., Pingle, S. C., Guo, F., Makale, M., & Kesari, S. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0627-5 · Cited by 70
“Instead, they found reduced protein expression of another Bcl-2-family protein, Mcl-1 which is known to be modulated by STAT3 [13].”
Targeting the PIAS1 SUMO ligase pathway to control inflammation
Liu, B., & Shuai, K. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.07.008 · Cited by 70
IFP35 Is Involved in the Antiviral Function of Interferon by Association with the Viral Tas Transactivator of Bovine Foamy Virus
Tan, J., Qiao, W., Wang, J., Xu, F.-W., Li, Y., Zhou, J., Chen, Q.-M., & Geng, Y.-Q. (2008) · Journal of Virology · doi:10.1128/jvi.02249-07 · Cited by 75
“Other diverse transcription factor families, including the interferon regulatory factor (IRF) (32), the signal transducer and activator of transcription (STAT) (7), the NF- B (15, 16), and the nuclear factor of activated T cells (NFAT) (6) families, can also respond to the external signals in the same way.”
Background
Human primary immunodeficiencies of type I interferons
Jouanguy, E., Zhang, S., Chapgier, A. L. A., Sancho‐Shimizu, V., Puel, A., Pïcard, C., Boisson‐Dupuis, S., Abel, L., & Casanova, J. (2007) · Biochimie · doi:10.1016/j.biochi.2007.04.016 · Cited by 69
The Role of Tissue-Resident Macrophages in the Development and Treatment of Inflammatory Bowel Disease
Ma, S., Zhang, J., Liu, H., Li, S., & Wang, Q. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.896591 · Cited by 81
Macrophage polarization: an effective approach to targeted therapy of inflammatory bowel disease
Du, Y., Rong, L., Cong, Y., Shen, L., Zhang, N., & Wang, B. (2021) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2021.1901079 · Cited by 81
“The functional characteristics and special tissue distribution of various subtypes of the JAK family have made JAK a new target in the fields of immunity, inflammation, and cancer [156,157].”
Background
A Review: Phytochemicals Targeting JAK/STAT Signaling and IDO Expression in Cancer
Arumuggam, N., Bhowmick, N. A., & Rupasinghe, H. P. V. (2015) · Phytotherapy Research · doi:10.1002/ptr.5327 · Cited by 79
“The STAT dimer translocates to the nucleus, where it binds to specific DNA sequences containing gamma activated site motif, and activate transcription (Darnell et al., 1994; Schindler and Darnell, 1995; Darnell, 1997).”
BackgroundInfluential
Anti-inflammatory Mechanism of Ginseng Saponin Metabolite Rh3 in Lipopolysaccharide-Stimulated Microglia: Critical Role of 5′-Adenosine Monophosphate-Activated Protein Kinase Signaling Pathway
Lee, Y., Park, J., Lee, E.-J., Lee, S., Kim, D., Kang, J. L., & Kim, H.-S. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf506110y · Cited by 77
IFNγ Restores Breast Cancer Sensitivity to Fulvestrant by Regulating STAT1, IFN Regulatory Factor 1, NF-κB, BCL2 Family Members, and Signaling to Caspase-Dependent Apoptosis
Ning, Y., Riggins, R. B., Mulla, J. E., Chung, H., Zwart, A. L., & Clarke, R. C. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-1169 · Cited by 69
“Once activated by binding IFN, their specific cell membrane receptors activate the Janus-activated kinase–signal transducer and activator of transcription (STAT) pathway, which results in the regulation of IFNstimulated genes, including IRF1 (27, 28).”
Background
A Characteristic Subset of Psoriasis-Associated Genes Is Induced by Oncostatin-M in Reconstituted Epidermis
Gazel, A., Rosdy, M., Bertino, B., Tornier, C., Sahuc, F., & Blumenberg, M. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700461 · Cited by 73
Alternative and Accessory Pathways in the Regulation of IFN-β-Mediated Gene Expression
Rani, M. R. S., & Ransohoff, R. M. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.788 · Cited by 61
“9,10 15 ISGF3 consists of heterooligomers of signal transducers and activators of transcription (Stat)1, Stat2, and the 48-kDa DNA-binding protein, IFN regulatory factor-9 (IRF-9).”
Proteasome-mediated Degradation of STAT1α following Infection of Macrophages with Leishmania donovani
Forget, G., Gregory, D. J., & Olivier, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414126200 · Cited by 71
PSTPIP2 connects DNA methylation to macrophage polarization in CCL4-induced mouse model of hepatic fibrosis
Yang, Y., Wu, X.-Q., Li, W.-X., Huang, H.-M., Li, H.-D., Pan, X.-Y., Li, X.-F., Huang, C., Meng, X.-M., Zhang, L., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0383-0 · Cited by 72
SIRT1 and microRNAs: The role in breast, lung and prostate cancers
Karbasforooshan, H., Roohbakhsh, A., & Karimi, G. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.03.023 · Cited by 82
Salvianolic acids enhance cerebral angiogenesis and neurological recovery by activating JAK 2/ STAT 3 signaling pathway after ischemic stroke in mice
Li, Y., Zhang, X., Cui, L., Chen, R., Zhang, Y., Zhang, C., Zhu, X., He, T., Shen, Z., Dong, L., et al. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14140 · Cited by 76
STAT3 Represses Nitric Oxide Synthesis in Human Macrophages upon Mycobacterium tuberculosis Infection
Queval, C. J., Song, O., Deboosère, N., Delorme, V., Debrie, A., Iantomasi, R., Veyron‐Churlet, R., Jouny, S., Redhage, K. R., Deloison, G., et al. (2016) · Scientific Reports · doi:10.1038/srep29297 · Cited by 82
Current perspectives of molecular pathways involved in chronic inflammation-mediated breast cancer
Suman, S., Sharma, P. K., Rai, G., Mishra, S., Arora, D., Gupta, P., & Shukla, Y. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.133 · Cited by 73
Regulation of Janus kinases by SOCS proteins
Kershaw, N. J., Murphy, J. M., Lucet, I. S., Nicola, N. A., & Babon, J. J. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130077 · Cited by 75
The role of the Janus kinase family/signal transducer and activator of transcription signaling pathway in fibrotic renal disease
Matsui, F., & Meldrum, K. K. (2012) · Journal of Surgical Research · doi:10.1016/j.jss.2012.06.050 · Cited by 70
Nanoparticle delivery of a peptide targeting EGFR signaling
Kim, S. K., & Huang, L. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.08.014 · Cited by 75
A Novel Role for IFN-Stimulated Gene Factor 3II in IFN-γ Signaling and Induction of Antiviral Activity in Human Cells
Morrow, A., Schmeisser, H., Tsuno, T., & Zoon, K. C. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001359 · Cited by 67
Transmembrane helix-helix interactions involved in ErbB receptor signaling
Cymer, F., & Schneider, D. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.2.11191 · Cited by 81
“Structurally, the receptor consists of an extracellular Epo-binding domain, a single TM helix and an intracellular domain,(20) which is associated with a Janus kinase that mediates downstream signal transduction via the Jak-STAT pathway.(21) Although only the structure of the extracellular EpoR domain with a bound Epo…”
Background
HIV-1 Tat Co-Operates with IFN-γ and TNF-α to Increase CXCL10 in Human Astrocytes
Williams, R., Yao, H.-H., Dhillon, N., & Buch, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005709 · Cited by 73
“CXCL10 promoter [44,45,58], however, resulted in abrogation of luciferase expression, thus underscoring the role of each of these”
Background
Curcumin regulates signal transducer and activator of transcription (STAT) expression in K562 cells
Blasius, R., Reuter, S., Henry, E., Dicato, M. A., & Diederich, M. F. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.07.029 · Cited by 81
“STAT (signal transducers and activators of transcription) proteins are a family of transcription factors activated by extra-cellular signaling proteins such as cytokines, hormones and growth factors [1–6].”
Background
Clinical and pathologic significance of activation of signal transducer and activator of transcription 3 in prostate cancer
Horinaga, M., Okita, H., Nakashima, J., Kanao, K., Sakamoto, M., & Murai, M. (2005) · Urology · doi:10.1016/j.urology.2005.03.066 · Cited by 73
Induction of suppressor of cytokine signaling-3 by herpes simplex virus type 1 confers efficient viral replication
Yokota, S., Yokosawa, N., Okabayashi, T., Suzutani, T., & Fujii, N. (2005) · Virology · doi:10.1016/j.virol.2005.04.028 · Cited by 67
IFN consensus sequence binding protein potentiates STAT1-dependent activation of IFNγ-responsive promoters in macrophages
Contursi, C., Wang, I.-M., Gabriele, L., Gadina, M., O'Shea, J., Morse, H. C., & Ozato, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.91 · Cited by 72
JAK/STAT3 signaling in cardiac fibrosis: a promising therapeutic target
Jiang, H., Yang, J., Li, T., Wang, X., Fan, Z., Ye, Q., & Du, Y. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1336102 · Cited by 68
STAT3 and Its Targeting Inhibitors in Oral Squamous Cell Carcinoma
Jiang, M., & Li, B. (2022) · Cells · doi:10.3390/cells11193131 · Cited by 78
“The signal transducer and activators of transcription (STAT) family are potential cytoplasmic transcription factors, including STAT1, STAT2, STAT3, STAT4, STAT5a, STAT5b, and STAT6, which can be activated in response to cytokine and growth factor stimulation to mediate multiple intracellular signaling pathways [16].”
Background
Induction of type I interferons by a novel porcine reproductive and respiratory syndrome virus isolate
Nan, Y.-C., Wang, R., Shen, M., Faaberg, K., Samal, S., & Zhang, Y.-J. (2012) · Virology · doi:10.1016/j.virol.2012.05.015 · Cited by 72
Hepatitis C virus core protein genotype 3a increases SOCS-7 expression through PPAR- in Huh-7 cells
Pazienza, V., Vinciguerra, M., Andriulli, A., & Mangia, A. (2010) · Journal of General Virology · doi:10.1099/vir.0.020644-0 · Cited by 69
A Novel c-Jun-dependent Signal Transduction Pathway Necessary for the Transcriptional Activation of Interferon γ Response Genes
Gough, D. J., Sabapathy, K., Ko, E. Y.-N., Arthur, H. A., Schreiber, R. D., Trapani, J. A., Clarke, C. J. P., & Johnstone, R. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607674200 · Cited by 62
NF-κB activation contributes to indoleamine dioxygenase transcriptional synergy induced by IFN-γ and tumor necrosis factor-α
Robinson, C. M., Hale, P. T., & Carlin, J. M. (2006) · Cytokine · doi:10.1016/j.cyto.2006.07.007 · Cited by 73
“Although latent STAT-1 is activated by tyrosine phosphorylation following binding of IFN-c or TNF-a to their respective receptors, IRF-1 must be synthesized de novo [14–17,25].”
Background
A novel functional activator of the Drosophila JAK/STAT pathway, unpaired2, is revealed by an in vivo reporter of pathway activation
Gilbert‐Ross, M., Weaver, B. K., Gergen, J. P., & Reich, N. C. (2005) · Mechanisms of Development · doi:10.1016/j.mod.2005.03.004 · Cited by 68
Role of STAT3 in skin fibrosis and transforming growth factor beta signalling
Pedroza, M., To, S., Assassi, S., Wu, M., Tweardy, D. J., & Agarwal, S. K. (2017) · Rheumatology · doi:10.1093/rheumatology/kex347 · Cited by 71
Tocotrienols: the unsaturated sidekick shifting new paradigms in vitamin E therapeutics
Kanchi, M. M., Shanmugam, M. K., Rane, G., Sethi, G., & Kumar, A. P. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.08.001 · Cited by 76
IRF9 is a key factor for eliciting the antiproliferative activity of IFN-α
Tsuno, T., Mejido, J., Zhao, T., Schmeisser, H., Morrow, A., & Zoon, K. (2009) · Journal of immunotherapy · doi:10.1097/cji.0b013e3181ad4092 · Cited by 71
“It has been reported that ISREs in most IFN-a response genes are usually located within 200-bp upstream of the TSSs.(19) However, it is also reported that at least 52% of human genes based on reference sequence (National Center for Biotechnology Information) were subject to regulation by putative alternative promoters…”
Background
Type I interferon (IFN)-dependent activation of Mnk1 and its role in the generation of growth inhibitory responses
Joshi, S., Kaur, S., Redig, A., Goldsborough, K., David, K. A., Ueda, T., Watanabe‐Fukunaga, R., Baker, D., Fish, E., Fukunaga, R., et al. (2009) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0900562106 · Cited by 71
“Notably, the original discovery of Jak-Stat pathways resulted from work focused on IFN signaling (4, 6, 7) and provided important clues and insights on how IFNs and other cytokines regulate transcription of target genes.”
Background
Tissue-Specific and Inducer-Specific Differential Induction of ISG56 and ISG54 in Mice
Terenzi, F., White, C. L., Pal, S., Williams, B. R. G., & Sen, G. C. (2007) · Journal of Virology · doi:10.1128/jvi.00322-07 · Cited by 65
“The binding of type I IFNs, IFN- and IFN-, to their cell surface receptor (IFNAR) leads to Jak1- and Tyk2-mediated tyrosine phosphorylation of STAT1 and STAT2, which heterodimerize, bind to IFN regulatory factor 9 (IRF-9, or p48) to form the IFNstimulated gene factor 3 (ISGF3) and translocate to the nucleus ( 8 , 30).”
Background

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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