Darnell, J. E. Jr, Kerr, I. M. & Stark, G. R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264, 1415–1421 (1994).
O’Shea, J. J., Gadina, M. & Schreiber, R. D. Cytokine signaling in 2002: new surprises in the Jak/Stat pathway. Cell 109, S121–S131 (2002).
Yu, H. & Jove, R. The STATs of cancer—new molecular targets come of age. Nat. Rev. Cancer 4, 97–105 (2004).
Yu, H., Lee, H., Herrmann, A., Buettner, R. & Jove, R. Revisiting STAT3 signalling in cancer: new and unexpected biological functions. Nat. Rev. Cancer 14, 736–746 (2014).
Guschin, D. et al. A major role for the protein tyrosine kinase JAK1 in the JAK/STAT signal transduction pathway in response to interleukin-6. EMBO J. 14, 1421–1429 (1995).
Heinrich, P. C. et al. Principles of interleukin (IL)-6-type cytokine signalling and its regulation. Biochem. J. 374, 1–20 (2003).
Yu, C. L. et al. Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein. Science 269, 81–83 (1995).
Bromberg, J. F. et al. Stat3 as an oncogene. Cell 98, 295–303 (1999).
Wang, T. et al. Regulation of the innate and adaptive immune responses by Stat-3 signaling in tumor cells. Nat. Med. 10, 48–54 (2004).
Kortylewski, M. et al. Inhibiting Stat3 signaling in the hematopoietic system elicits multicomponent antitumor immunity. Nat. Med. 11, 1314–1321 (2005).
Yu, H., Kortylewski, M. & Pardoll, D. Crosstalk between cancer and immune cells: role of STAT3 in the tumour microenvironment. Nat. Rev. Immunol. 7, 41–51 (2007).
Jones, S. A. & Jenkins, B. J. Recent insights into targeting the IL-6 cytokine family in inflammatory diseases and cancer. Nat. Rev. Immunol. 18, 773–789 (2018).
Kang, S., Tanaka, T., Narazaki, M. & Kishimoto, T. Targeting interleukin-6 signaling in clinic. Immunity 50, 1007–1023 (2019).
Erdogan, F. et al. JAK-STAT core cancer pathway: an integrative cancer interactome analysis. J. Cell Mol. Med. 26, 2049–2062 (2022).
Yu, H., Pardoll, D. & Jove, R. STATs in cancer inflammation and immunity: a leading role for STAT3. Nat. Rev. Cancer 9, 798–809 (2009).
Ghoshal Gupta, S., Baumann, H. & Wetzler, M. Epigenetic regulation of signal transducer and activator of transcription 3 in acute myeloid leukemia. Leuk. Res. 32, 1005–1014 (2008).
Wingelhofer, B. et al. Implications of STAT3 and STAT5 signaling on gene regulation and chromatin remodeling in hematopoietic cancer. Leukemia 32, 1713–1726 (2018).
Maurer, B. et al. High activation of STAT5A drives peripheral T-cell lymphoma and leukemia. Haematologica 105, 435–447 (2020).
Schepers, H., Wierenga, A. T., Vellenga, E. & Schuringa, J. J. STAT5-mediated self-renewal of normal hematopoietic and leukemic stem cells. JAKSTAT 1, 13–22 (2012).
Subramaniam, D. et al. Suppressing STAT5 signaling affects osteosarcoma growth and stemness. Cell Death Dis. 11, 149 (2020).
Chou, P. H. et al. A chemical probe inhibitor targeting STAT1 restricts cancer stem cell traits and angiogenesis in colorectal cancer. J. Biomed. Sci. 29, 20 (2022).
Wang, F., Zhang, L., Liu, J., Zhang, J. & Xu, G. Highly expressed STAT1 contributes to the suppression of stemness properties in human paclitaxel-resistant ovarian cancer cells. Aging 12, 11042–11060 (2020).
Qadir, A. S. et al. CD95/Fas increases stemness in cancer cells by inducing a STAT1-dependent type I interferon response. Cell Rep. 18, 2373–2386 (2017).
Liu, C. et al. STAT1-mediated inhibition of FOXM1 enhances gemcitabine sensitivity in pancreatic cancer. Clin. Sci. 133, 645–663 (2019).
Croker, B. A., Kiu, H. & Nicholson, S. E. SOCS regulation of the JAK/STAT signalling pathway. Semin. Cell Dev. Biol. 19, 414–422 (2008).
Song, M. M. & Shuai, K. The suppressor of cytokine signaling (SOCS) 1 and SOCS3 but not SOCS2 proteins inhibit interferon-mediated antiviral and antiproliferative activities. J. Biol. Chem. 273, 35056–35062 (1998).
Krebs, D. L. & Hilton, D. J. SOCS proteins: negative regulators of cytokine signaling. Stem Cell 19, 378–387 (2001).
Rani, A. & Murphy, J. J. STAT5 in cancer and immunity. J. Interferon Cytokine Res. 36, 226–237 (2016).
Inghirami, G. et al. New and old functions of STAT3: a pivotal target for individualized treatment of cancer. Cell Cycle 4, 1131–1133 (2005).
Weniger, M. A. et al. Mutations of the tumor suppressor gene SOCS-1 in classical Hodgkin lymphoma are frequent and associated with nuclear phospho-STAT5 accumulation. Oncogene 25, 2679–2684 (2006).
Lennerz, J. K. et al. Suppressor of cytokine signaling 1 gene mutation status as a prognostic biomarker in classical Hodgkin lymphoma. Oncotarget 6, 29097–29110 (2015).
Ogata, H. et al. Loss of SOCS3 in the liver promotes fibrosis by enhancing STAT3-mediated TGF-β1 production. Oncogene 25, 2520–2530 (2006).
He, B. et al. SOCS-3 is frequently silenced by hypermethylation and suppresses cell growth in human lung cancer. Proc. Natl Acad. Sci. USA 100, 14133–14138 (2003).
Warburg, O. On respiratory impairment in cancer cells. Science 124, 269–270 (1956).
Warburg, O., Wind, F. & Negelein, E. The metabolism of tumors in the body. J. Gen. Physiol. 8, 519–530 (1927).
Vander Heiden, M. G., Cantley, L. C. & Thompson, C. B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324, 1029–1033 (2009).
Liberti, M. V. & Locasale, J. W. The Warburg effect: how does it benefit cancer cells. Trends Biochem. Sci. 41, 211–218 (2016).
Evans, K. W. et al. Oxidative phosphorylation is a metabolic vulnerability in chemotherapy-resistant triple-negative breast cancer. Cancer Res. 81, 5572–5581 (2021).
Chandra, D. & Singh, K. K. Genetic insights into OXPHOS defect and its role in cancer. Biochim. Biophys. Acta 1807, 620–625 (2011).
Ashton, T. M., McKenna, W. G., Kunz-Schughart, L. A. & Higgins, G. S. Oxidative phosphorylation as an emerging target in cancer therapy. Clin. Cancer Res. 24, 2482–2490 (2018).
Nayak, A. P., Kapur, A., Barroilhet, L. & Patankar, M. S. Oxidative phosphorylation: a target for novel therapeutic strategies against ovarian cancer. Cancers https://doi.org/10.3390/cancers10090337 (2018).
Molina, J. R. et al. An inhibitor of oxidative phosphorylation exploits cancer vulnerability. Nat. Med. 24, 1036–1046 (2018).
Leone, R. D. & Powell, J. D. Metabolism of immune cells in cancer. Nat. Rev. Cancer 20, 516–531 (2020).
Xu, S. et al. Uptake of oxidized lipids by the scavenger receptor CD36 promotes lipid peroxidation and dysfunction in CD8+ T cells in tumors. Immunity 54, 1561–1577 e1567 (2021).
Mehla, K. & Singh, P. K. Metabolic regulation of macrophage polarization in cancer. Trends Cancer 5, 822–834 (2019).
Poznanski, S. M. et al. Metabolic flexibility determines human NK cell functional fate in the tumor microenvironment. Cell Metab. 33, 1205–1220 e1205 (2021). This article shows that STAT3-mediated metabolic reprogramming of NK cells in the tumour microenvironment can augment their tumour cell-killing activity.
Yao, C. H. et al. Mitochondrial fusion supports increased oxidative phosphorylation during cell proliferation. Elife https://doi.org/10.7554/eLife.41351 (2019).
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