The role of STAT3 in autophagy
Open accessAbstract
Autophagy is an evolutionarily conserved process in eukaryotes that eliminates harmful components and maintains cellular homeostasis in response to a series of extracellular insults. However, these insults may trigger the downstream signaling of another prominent stress responsive pathway, the STAT3 signaling pathway, which has been implicated in multiple aspects of the autophagic process. Recent reports further indicate that different subcellular localization patterns of STAT3 affect autophagy in various ways. For example, nuclear STAT3 fine-tunes autophagy via the transcriptional regulation of several autophagy-related genes such as BCL2 family members, BECN1, PIK3C3, CTSB, CTSL, PIK3R1, HIF1A, BNIP3, and microRNAs with targets of autophagy modulators. Cytoplasmic STAT3 constitutively inhibits autophagy by sequestering EIF2AK2 as well as by interacting with other autophagy-related signaling molecules such as FOXO1 and FOXO3. Additionally, the mitochondrial translocation of STAT3 suppresses autophagy induced by oxidative stress and may effectively preserve mitochondria from being degraded by mitophagy. Understanding the role of STAT3 signaling in the regulation of autophagy may provide insight into the classic autophagy model and also into cancer therapy, especially for the emerging targeted therapy, because a series of targeted agents execute antitumor activities via blocking STAT3 signaling, which inevitably affects the autophagy pathway. Here, we review several of the representative studies and the current understanding in this particular field.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
STAT3 is indispensable for physiologic leptin actions, and STAT3 dysfunction in any direction could cause pathophysiological alterations in mice and humans.
“Overall, STAT3 is indispensable for physiologic leptin actions, and STAT3 dysfunction in any direction could cause pathophysiological alterations in mice and humans”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as You et al., 2015
The Introduction reports that constitutive STAT3 activation is associated with malignant tumors and that disruption of the mouse Stat3 gene causes embryonic lethality. These examples support a narrower claim that altered STAT3 function can have pathological consequences, but the paper does not address whether STAT3 is indispensable for physiological leptin actions or establish the claimed effects of dysfunction in any direction across mice and humans (searched: leptin actions, leptin receptor, pathophysiological alterations). (LLM, conf=0.78)
Experimental — accuracy not yet measuredSTAT3 undergoes post-translational modifications including methylation, acetylation, ubiquitination, ISGylation, and SUMOylation.
“In addition to tyrosine phosphorylation, STAT3 also undergoes a variety of other post-translational modifications, including methylation, acetylation, ubiquitination, IFN-stimulated gene (ISG)-ylation, and small ubiquitin-related modifiers (SUMOs)-conjugation (SUMOylation) (Kojima et al., 2013; You et al., 2015; Zouein et al., 2015; Avalle and Poli, 2018; Hu et al., 2018) with various effects on”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as You et al., 2015
The sections on tyrosine and serine phosphorylation of STAT3 discuss those modifications, but do not address any of the five modifications named in the claim. Searches for methylation, acetylation, ubiquitination, ISGylation, and SUMOylation found no supporting passage in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredAt the molecular level, IL-6 increases the activity of DNMT1 with activating effects on JAK/STAT3, NF-κB and PI3K/AKT/mTOR signaling pathways, affecting regulation of autophagy-related functions required to maintain cellular homeostasis under stress such as a prenatal insult.
“At the molecular level, IL-6 increases the activity of DNA methyltransferases 1 (DNMT1) with activating effects on the JAK/STAT3, NF-κB and PI3K/AKT/mTOR signaling pathways [144–148] affecting the regulation of autophagy-related functions, that are required to maintain cellular homeostasis under stress [149], such as a prenatal insult.”
From The ASD Living Biology: from cell proliferation to clinical phenotype (2019) · cites this paper as [149]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069 · see citing works
Autophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,441 · see citing works
STATs in cancer inflammation and immunity: a leading role for STAT3
Yu, H., Pardoll, D., & Jove, R. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2734 · Cited by 4,383 · see citing works
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506 · see citing works
STATs: transcriptional control and biological impact
Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201 · see citing works
Bromberg, J. F., Wrzeszczynska, M. H., Devgan, G., Zhao, Y., Pestell, R. G., Albanese, C., & Darnell, J. E. (1999) · Cell · doi:10.1016/s0092-8674(00)81959-5 · Cited by 2,790 · see citing works
Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070 · see citing works
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Bowman, T., Garcia, R., Turkson, J., & Jove, R. (2000) · Oncogene · doi:10.1038/sj.onc.1203527 · Cited by 1,743 · see citing works
Autophagy modulation as a potential therapeutic target for diverse diseases
Rubinsztein, D. C., Codogno, P., & Levine, B. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3802 · Cited by 1,429 · see citing works
Targeted disruption of the mouse <i>Stat3</i> gene leads to early embryonic lethality
Takeda, K., Noguchi, K., Shi, W., Tanaka, T., Matsumoto, M., Yoshida, N., Kishimoto, T., & Akira, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3801 · Cited by 1,323 · see citing works
Akira, S., Nishio, Y., Inoue, M., Wang, X.-J., We, S., Matsusaka, T., Yoshida, K., Sudo, T., Naruto, M., & Kishimoto, T. (1994) · Cell · doi:10.1016/0092-8674(94)90235-6 · Cited by 1,019 · see citing works
Function of Mitochondrial Stat3 in Cellular Respiration
Wegrzyn, J., Potla, R., Chwae, Y.-J., Sepuri, N. B. V., Zhang, Q., Koeck, T., Derecka, M., Szczepanek, K., Szelag, M., Gornicka, A., et al. (2009) · Science · doi:10.1126/science.1164551 · Cited by 1,014 · see citing works
ROS, mitochondria and the regulation of autophagy
Scherz-Shouval, R., & Elazar, Z. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.009 · Cited by 954 · see citing works
Kouroku, Y., Fujita, E., Tanida, I., Ueno, T., Isoai, A., Kumagai, H., Ogawa, S., Kaufman, R. J., Kominami, E., & Momoi, T. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401984 · Cited by 934 · see citing works
Enhanced DNA-Binding Activity of a Stat3-Related Protein in Cells Transformed by the Src Oncoprotein
Yu, C.-L., Meyer, D. J., Campbell, G. S., Larner, A. C., Carter-Su, C., Schwartz, J., & Jove, R. (1995) · Science · doi:10.1126/science.7541555 · Cited by 931 · see citing works
Levy, D., & Lee, C.-K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15650 · Cited by 925 · see citing works
Bromberg, J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15617 · Cited by 846 · see citing works
Autophagy as a target for anticancer therapy
Jankú, F., McConkey, D. J., Hong, D. S., & Kurzrock, R. (2011) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2011.71 · Cited by 803 · see citing works
IL-6R/STAT3/miR-34a feedback loop promotes EMT-mediated colorectal cancer invasion and metastasis
Rokavec, M., Öner, M. G., Li, H., Jackstadt, R., Jiang, L., Lodygin, D., Kaller, M., Horst, D., Ziegler, P. K., Schwitalla, S., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci73531 · Cited by 753 · see citing works
Self-citationLevy, D. E., & Lee, C.-K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215650 · Cited by 734 · see citing works
Regulation of mTORC1 and its impact on gene expression at a glance
Laplante, M., & Sabatini, D. M. (2013) · Journal of Cell Science · doi:10.1242/jcs.125773 · Cited by 665 · see citing works
Fukada, T., Hibi, M., Yamanaka, Y., Takahashi-Tezuka, M., Fujitani, Y., Yamaguchi, T., Nakajima, K., & Hirano, T. (1996) · Immunity · doi:10.1016/s1074-7613(00)80501-4 · Cited by 652 · see citing works
Hypoxia-induced autophagy: cell death or cell survival?
Mazure, N. M., & Pouysségur, J. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.015 · Cited by 620 · see citing works
Chung, J., Uchida, E., Grammer, T. C., & Blenis, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6508 · Cited by 620 · see citing works
Wei, Y., Zou, Z., Becker, N., Anderson, M., Sumpter, R., Xiao, G., Kinch, L. N., Koduru, P. R. K., Christudass, C. S., Veltri, R. W., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.015 · Cited by 531 · see citing works
Yokogami, K., Wakisaka, S., Avruch, J., & Reeves, S. A. (2000) · Current Biology · doi:10.1016/s0960-9822(99)00268-7 · Cited by 468 · see citing works
Activation of Autophagy Protects Against Acetaminophen–Induced Hepatotoxicity
Ni, H., Bockus, A. B., Boggess, N., Jaeschke, H., & Ding, W. (2011) · Hepatology · doi:10.1002/hep.24690 · Cited by 429 · see citing works
Combined MTOR and autophagy inhibition
Rangwala, R. A., Chang, Y. C., Hu, J., Algazy, K. M., Evans, T. L., Fecher, L. A., Schuchter, L. M., Torigian, D. A., Panosian, J. T., Troxel, A. B., et al. (2014) · Autophagy · doi:10.4161/auto.29119 · Cited by 426 · see citing works
STAT3 is a potential modulator of HIF‐1‐mediated VEGF expression in human renal carcinoma cells
Jung, J. E., Lee, H. S., Cho, I., Chung, D. H., Yoon, S., Yang, Y. M., Lee, S. E., Choi, S., Park, J., Ye, S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3099fje · Cited by 425 · see citing works
Brock, M., Trenkmann, M., Gay, R., Michel, B., Gay, S., Fischler, M., Ulrich, S., Speich, R., & Huber, L. (2009) · Circulation Research · doi:10.1161/circresaha.109.197491 · Cited by 422 · see citing works
Novel roles of unphosphorylated STAT3 in oncogenesis and transcriptional regulation
Yang, J., Chatterjee-Kishore, M., Staugaitis, S. M., Nguyen, H., Schlessinger, K., Levy, D. E., & Stark, G. R. (2005) · Cancer Research · doi:10.1158/0008-5472.939.65.3 · Cited by 405 · see citing works
Combined autophagy and proteasome inhibition
Vogl, D. T., Stadtmauer, E. A., Tan, K.-S., Heitjan, D. F., Davis, L. E., Pontiggia, L., Rangwala, R. A., Piao, S., Chang, Y. C., Scott, E. C., et al. (2014) · Autophagy · doi:10.4161/auto.29264 · Cited by 372 · see citing works
STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3
Liu, L., McBride, K. M., & Reich, N. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501643102 · Cited by 348 · see citing works
Li, L., Yuan, L., Luo, J., Gao, J., Guo, J., & Xie, X. (2012) · Clinical and Experimental Medicine · doi:10.1007/s10238-012-0186-5 · Cited by 314 · see citing works
Mikhaylova, O., Stratton, Y., Hall, D., Kellner, E., Ehmer, B., Drew, A. F., Gallo, C. A., Plas, D. R., Biesiada, J., Meller, J., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.02.019 · Cited by 313 · see citing works
Stat3 controls lysosomal-mediated cell death in vivo
Kreuzaler, P. A., Staniszewska, A. D., Li, W., Omidvar, N., Kedjouar, B., Turkson, J., Poli, V., Flavell, R. A., Clarkson, R. W. E., & Watson, C. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2171 · Cited by 312 · see citing works
Milani, M., Rzymski, T., Mellor, H. R., Pike, L., Bottini, A., Generali, D., & Harris, A. L. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2839 · Cited by 304 · see citing works
Cytoplasmic STAT3 represses autophagy by inhibiting PKR activity
Shen, S., Niso-Santano, M., Adjemian, S., Takehara, T., Malik, S. A., Minoux, H., Souquere, S., Mariño, G., Lachkar, S., Senovilla, L., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.013 · Cited by 285 · see citing works
Molecular Pathways: JAK/STAT Pathway: Mutations, Inhibitors, and Resistance
Quintás‐Cardama, A., & Verstovšek, S. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0284 · Cited by 284 · see citing works
Feng, Y., Ke, C., Tang, Q., Dong, H., Zheng, X., Lin, W., Ke, J.-A., Huang, J., Yeung, S.-C., & Zhang, H. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.59 · Cited by 272 · see citing works
Regulation of autophagy by stress-responsive transcription factors
Pietrocola, F., Izzo, V., Niso‐Santano, M., Vacchelli, E., Galluzzi, L., Maiuri, M. C., & Kroemer, G. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.05.008 · Cited by 270 · see citing works
Nguyen, H. T. T., Dalmasso, G., Müller, S. K., Carrière, J., Seibold, F., & Darfeuille–Michaud, A. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.10.021 · Cited by 250 · see citing works
Szczepanek, K., Chen, Q., Derecka, M., Salloum, F. N., Zhang, Q., Szeląg, M., Cichy, J., Kukreja, R. C., Dulak, J., Lesnefsky, E. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226209 · Cited by 222 · see citing works
Tammineni, P., Anugula, C., Mohammed, F., Murari, A., Larner, A. C., & Sepuri, N. B. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.378984 · Cited by 207 · see citing works
Tai, W.-T., Shiau, C.-W., Chen, H.-L., Liu, C.-Y., Lin, C.-S., Cheng, A.-L., Chen, P.-J., & Chen, K.-F. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.18 · Cited by 202 · see citing works
Nuclear export signal located within the DNA‐binding domain of the STAT1transcription factor
McBride, K. M., McDonald, C., & Reich, N. C. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6196 · Cited by 196 · see citing works
Wan, G., Xie, W., Liu, Z., Xu, W., Lao, Y., Huang, N., Cui, K., Liao, M., He, J., Jiang, Y., et al. (2013) · Autophagy · doi:10.4161/auto.26534 · Cited by 188 · see citing works
Maycotte, P., Gearheart, C. M., Barnard, R., Aryal, S., Levy, J. M. M., Fosmire, S. P., Hansen, R. J., Morgan, M. J., Porter, C. C., Gustafson, D. L., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3470 · Cited by 185 · see citing works
Kodama, H., Fukuda, K., Pan, J.-K., Makino, S., Baba, A., Hori, S., & Ogawa, S. (1997) · Circulation Research · doi:10.1161/01.res.81.5.656 · Cited by 168 · see citing works
Chatterjee, A., Chattopadhyay, D., & Chakrabarti, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095716 · Cited by 152 · see citing works
Regulation of Stat3 nuclear export
Bhattacharya, S., & Schindler, C. (2003) · Journal of Clinical Investigation · doi:10.1172/jci15372 · Cited by 146 · see citing works
Narimatsu, M., Maeda, H., Itoh, S., Atsumi, T., Ohtani, T., Nishida, K., Itoh, M., Kamimura, D., Park, S., Mizuno, K., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6615-6625.2001 · Cited by 145 · see citing works
Wu, H., Wang, F., Hu, S., Yin, C., Li, X., Zhao, S., Wang, J., & Yan, Z. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.07.001 · Cited by 142 · see citing works
Bao, W., Wang, H., Tian, F., He, X.-Y., Qiu, M.-T., Wang, J.-Y., Zhang, H.-J., Wang, L.-H., & Wan, X.-P. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-155 · Cited by 135 · see citing works
NF-κB and STAT3 cooperatively induce IL6 in starved cancer cells
Yoon, S., Woo, S., Kang, J.-H., Kim, K., Hj, S., Gwak, H.-S., Park, S., & Chwae, Y.-J. (2011) · Oncogene · doi:10.1038/onc.2011.517 · Cited by 130 · see citing works
STAT3 inhibits the degradation of HIF-1α by pVHL-mediated ubiquitination
Jung, J. E., Kim, H. S., Lee, C. S., Shin, Y., Kim, Y.-N., Kang, G. H., Kim, T.-Y., Juhnn, Y., Kim, S. J., Park, J., et al. (2008) · Experimental & Molecular Medicine · doi:10.3858/emm.2008.40.5.479 · Cited by 122 · see citing works
Szczepanek, K., Chen, Q., Larner, A. C., & Lesnefsky, E. J. (2012) · Mitochondrion · doi:10.1016/j.mito.2011.08.011 · Cited by 117 · see citing works
Oh, H., Yu, C., Dambuza, I. M., Marrero, B., & Egwuagu, C. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359661 · Cited by 113 · see citing works
Multi-Tasking: Nuclear Transcription Factors with Novel Roles in the Mitochondria
Szczepanek, K., Lesnefsky, E., & Larner, A. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.001 · Cited by 113 · see citing works
Inductive microRNA‐21 impairs anti‐mycobacterial responses by targeting IL‐12 and Bcl‐2
Wu, Z., Lu, H., Sheng, J., & Li, L. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.004 · Cited by 110 · see citing works
Yamada, E., Bastie, C. C., Koga, H., Wang, Y., Cuervo, A. M., & Pessin, J. E. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.014 · Cited by 103 · see citing works
Cucurbitacin I Induces Protective Autophagy in Glioblastoma in Vitro and in Vivo
Yuan, G., Yan, S., Xue, H., Zhang, P., Sun, J., & Li, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.528760 · Cited by 88 · see citing works
Sorafenib exerts anti-glioma activity in vitro and in vivo
Siegelin, M. D., Raskett, C. M., Gilbert, C. A., et al. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.05.009 · Cited by 85 · see citing works
Khanim, F. L., Merrick, B., Giles, H. V., Jankute, M., JACKSON, J. B., Giles, L., Birtwistle, J., Bunce, C. M., & Drayson, M. T. (2011) · Blood Cancer Journal · doi:10.1038/bcj.2011.38 · Cited by 84 · see citing works
Pratt, J., & Annabi, B. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.01.012 · Cited by 83 · see citing works
Kim, D. J., Tremblay, M. L., & DiGiovanni, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010290 · Cited by 83 · see citing works
Hevehan, D. L., Miller, W. M., & Papoutsakis, E. T. (2002) · Blood · doi:10.1182/blood.v99.5.1627 · Cited by 79 · see citing works
Zhou, X., Ren, Y., Liu, A., Han, L., Zhang, K., Li, S., Li, P., Li, P., Kang, C., Wang, X., et al. (2014) · Oncology Reports · doi:10.3892/or.2014.3114 · Cited by 76 · see citing works
Granulocyte colony-stimulating factor activates a 72-kDa isoform of STAT3 in human neutrophils
Chakraborty, A., & Tweardy, D. J. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.64.5.675 · Cited by 67 · see citing works
STAT3 down regulates LC3 to inhibit autophagy and pancreatic cancer cell growth
Gong, J., Muñoz, A. R., Chan, D. C. F., Ghosh, R., & Kumar, A. P. (2014) · Oncotarget · doi:10.18632/oncotarget.1810 · Cited by 63 · see citing works
Stat3 inhibits Beclin 1 expression through recruitment of HDAC3 in nonsmall cell lung cancer cells
Miao, L.-J., Huang, F.-X., Sun, Z.-T., Zhang, R.-X., Huang, S.-F., & Wang, J. (2014) · Tumor Biology · doi:10.1007/s13277-014-1961-6 · Cited by 62 · see citing works
Spaccarotella, E., Pellegrino, E., Ferracin, M., et al. (2013) · Haematologica · doi:10.3324/haematol.2013.088286 · Cited by 56 · see citing works
STAT3-dependent transactivation of miRNA genes following Toxoplasma gondii infection in macrophage
Cai, Y., Chen, H., Jin, L., You, Y., & Shen, J. (2013) · Parasites & Vectors · doi:10.1186/1756-3305-6-356 · Cited by 54 · see citing works
Roles of mTOR and STAT3 in Autophagy Induced by Telomere 3' Overhang-Specific DNA Oligonucleotides
Yokoyama, T., Kondo, Y., & Kondo, S. (2007) · Autophagy · doi:10.4161/auto.4602 · Cited by 48 · see citing works
Khatib, H., Huang, W., Mikheil, D. M., et al. (2009) · Journal of Dairy Science · doi:10.3168/jds.2009-2439 · Cited by 48 · see citing works
Yuan, X., Du, J., Song, H., et al. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.09.006 · Cited by 47 · see citing works
Lian, J., Ni, Z., Dai, X., Su, C., Smith, A. R., Xu, L., & He, F. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0559 · Cited by 47 · see citing works
Glioblastoma stem cells: a new target for metformin and arsenic trioxide.
Carmignani, M., Volpe, A. R., Aldea, M. D., et al. (2014) · PubMed · Cited by 46 · see citing works
Proteolytic Conversion of STAT3α to STAT3γ in Human Neutrophils
Kato, T., Sakamoto, E., Kutsuna, H., Eto-Kimura, A., Hato, F., & Kitagawa, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400637200 · Cited by 39 · see citing works
Choy, M., Movassagh, M., Siggens, L., Vujić, A., Goddard, M. J., Sanchez, A. M., Perkins, N. D., Figg, N. L., Bennett, M. R., Carroll, J. S., et al. (2010) · Genome Medicine · doi:10.1186/gm158 · Cited by 35 · see citing works
Ouyang, D., Zhang, Y.-T. Y., Xu, L., Li, J., Zha, Q., & He, X. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr032 · Cited by 31 · see citing works
Pensa, S., Lloyd‐Lewis, B., Sargeant, T. J., Resemann, H. K., Kahn, C. R., & Watson, C. J. (2014) · The FEBS Journal · doi:10.1111/febs.13035 · Cited by 28 · see citing works
Hamedani, F. S., Cinar, M., Mo, Z., et al. (2014) · Leukemia Research · doi:10.1016/j.leukres.2013.12.027 · Cited by 27 · see citing works
Su, J.-C., Tseng, P., Hsu, C.-Y., Tai, W., Huang, J., Ko, C.-H., Lin, M.-W., Liu, C., Chen, K., & Shiau, C. (2014) · Oncotarget · doi:10.18632/oncotarget.2054 · Cited by 26 · see citing works
Toit, A. D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3472 · Cited by 13 · see citing works
Xu, S., Xu, Z., Liu, B., Sun, Q., Yang, L., Wang, J., Wang, Y., & Liu, H. (2014) · Leukemia Research · doi:10.1016/j.leukres.2014.07.004 · Cited by 11 · see citing works
Second-Line Treatment for Pancreatic Cancer
Kaddis, N., & Saif, M. W. (2014) · PubMed · doi:10.6092/1590-8577/2691 · Cited by 8 · see citing works
Su, J., Liu, C., Tai, W., et al. (2013) · Cancer Research · doi:10.1158/1538-7445.am2013-3447 · Cited by 1 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [83]Pratt J, Annabi B. Induction of autophagy biomarker BNIP3 requires a JAK2/STAT3 and MT1-MMP signaling interplay in Concanavalin-A-activated U87 glioblastoma cells. Cellular Signal 2014; 26: 917- 24; PMID:24462646; http://dx.doi.org/ 10.1016/j.cellsig.2014.01.012 24462646 · DOI
Cited by
Sorted by citations
Bharath, L. P., Agrawal, M., McCambridge, G., Nicholas, D. A., Hasturk, H., Liu, J., Jiang, K., Liu, R., Guo, Z., Deeney, J., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.015 · Cited by 614 · see citing works
The ASD Living Biology: from cell proliferation to clinical phenotype
Courchesne, E., Pramparo, T., Gazestani, V. H., Lombardo, M. V., Pierce, K., & Lewis, N. E. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0056-y · Cited by 333 · see citing works
Bharadwaj, U., Kasembeli, M. M., Robinson, P., & Tweardy, D. J. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018440 · Cited by 314 · see citing works
“In addition to tyrosine phosphorylation, STAT3also undergoes a variety of other post-translational modifications, including methylation, acetylation, ubiquitination, IFN-stimulated gene (ISG)-ylation, and small ubiquitin-related modifiers (SUMOs)-conjugation (SUMOylation) (Kojima et al., 2013; You et al., 2015; Zouein…”
BackgroundIL-6 regulates autophagy and chemotherapy resistance by promoting BECN1 phosphorylation
Hu, F., Song, D., Yan, Y., Huang, C., Shen, C., Lan, J., Chen, Y., Liu, A., Wu, Q., Sun, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23923-1 · Cited by 235 · see citing works
The complex STATes of astrocyte reactivity: How are they controlled by the JAK-STAT3 pathway?
Ceyzériat, K., Abjean, L., Carrillo-de Sauvage, M.-A., Ben Haim, L., & Escartin, C. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.05.043 · Cited by 185 · see citing works
Oh, Y. M., Lee, S. W., Kim, W. K., Chen, S., Church, V. A., Cates, K., Li, T., Zhang, B., Dolle, R. E., Dahiya, S., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01185-4 · Cited by 100 · see citing works
Drug resistance in colorectal cancer: An epigenetic overview
Luo, M., Yang, X., Chen, H.-N., Nice, E. C., & Huang, C. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188623 · Cited by 94 · see citing works
Wang, P., Feng, Y.-B., Wang, L., Li, Y., Fan, C., Song, Q., & Yu, S. Y. (2019) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2019.08.002 · Cited by 38 · see citing works
Tian, Y.-T., Ma, L.-P., Ding, C.-Y., Liu, M.-M., Wang, S.-N., Tian, M., Gao, L., & Liu, Q.-J. (2022) · International Journal of Radiation Biology · doi:10.1080/09553002.2022.2055799 · Cited by 10 · see citing works
- Authors
- You, L., Wang, Z., Li, H., Shou, J., Jing, Z., Xie, J., Sui, X., Pan, H., & Han, W.
- Affiliations
- Sir Run Run Shaw Hospital (CN)
- Zhejiang University (CN)
- Corresponding author
- Pan, Hongming
- Han, Weidong
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2015-05-04
- Volume
- 11
- Issue
- 5
- Pages
- 729-739
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC4509450
- OpenAlex
- W1853894947
- Cited by
- 515
- References
- 91
- Citations by year
- 2026: 29 · 2025: 57 · 2024: 69 · 2023: 47 · 2022: 85 · 2021: 68 · 2020: 55 · 2019: 36 · 2018: 25 · 2017: 24 · 2016: 15 · 2015: 4
- FWCI
- 2.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Autophagy (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- STAT3, STAT3 signaling, PKR, FOXO1, FOXO3, mitophagy, oxidative stress, HIF1A, Bcl-2 family proteins, PIK3C3, Beclin-1, PIK3R1, microRNA, cancer therapy, targeted therapy
- MeSH terms
- Animals, Autophagy, Humans, Mitochondria, Models, Biological, Neoplasms, Subcellular Fractions, STAT3 Transcription Factor
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review