Cited by 1,014Mitochondrial Function and PathologyCytokine Signaling Pathways and InteractionsMetabolism, Diabetes, and Cancer

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Function of Mitochondrial Stat3 in Cellular Respiration

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Wegrzyn, Joanna, Potla, Ramesh, Chwae, Yong-Joon, Sepuri, Naresh B. V., Zhang, Qifang, Koeck, Thomas, Derecka, Marta, Szczepanek, Karol, Szelag, Magdalena, Gornicka, Agnieszka, Moh, Akira, Moghaddas, Shadi, Chen, Qun, Bobbili, Santha, Cichy, Joanna, Dulak, Jozef, Baker, Darren P., Wolfman, Alan, Stuehr, Dennis, Hassan, Medhat O., Fu, Xin-Yuan, Avadhani, Narayan, Drake, Jennifer I., Fawcett, Paul, Lesnefsky, Edward J., Larner, Andrew C.·2009·Science

DOI 10.1126/science.1164551PMC PMC2758306

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Abstract

Cytokines such as interleukin-6 induce tyrosine and serine phosphorylation of Stat3 that results in activation of Stat3-responsive genes. We provide evidence that Stat3 is present in the mitochondria of cultured cells and primary tissues, including the liver and heart. In Stat3 â/â cells, the activities of complexes I and II of the electron transport chain (ETC) were significantly decreased. We identified Stat3 mutants that selectively restored the protein's function as a transcription factor or its functions within the ETC. In mice that do not express Stat3 in the heart, there were also selective defects in the activities of complexes I and II of the ETC. These data indicate that Stat3 is required for optimal function of the ETC, which may allow it to orchestrate responses to cellular homeostasis.

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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
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Hilfiker‐Kleiner, D., Kamiński, K. A., Podewski, E. K., Bonda, T. A., Schaefer, A., Sliwa, K. S., Förster, O., Guba‐Quint, A., Landmesser, U., Doerries, C., et al. (2007) · Cell · doi:10.1016/j.cell.2006.12.036 · Cited by 906
A STAT protein domain that determines DNA sequence recognition suggests a novel DNA-binding domain.Preprint
Horvath, C. M., Wen, Z., & Darnell, J. E., Jr. (1995) · Genes & Development · doi:10.1101/gad.9.8.984 · Cited by 537
Cardiomyocyte-restricted knockout of STAT3 results in higher sensitivity to inflammation, cardiac fibrosis, and heart failure with advanced age
Jacoby, J. J., Kalinowski, A., Liu, M.-G., Zhang, S. S.-M., Gao, Q., Chai, G.-X., Ji, L., Iwamoto, Y., Li, E., Schneider, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134694100 · Cited by 357
Self-citation
Hematopoietic cytokine receptor signaling
Baker, S. J., Rane, S. G., & Reddy, E. P. (2007) · Oncogene · doi:10.1038/sj.onc.1210757 · Cited by 256
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Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., & Hirst, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100444200 · Cited by 247
GRIM‐19, a death‐regulatory gene product, suppresses Stat3 activity via functional interaction
Lufei, C., Ma, J., Huang, G., Zhang, T., Novotny‐Diermayr, V., Ong, C. T., & Cao, X. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg135 · Cited by 220
GRIM-19, a Cell Death Regulatory Protein, Is Essential for Assembly and Function of Mitochondrial Complex I
Huang, G., Lu, H., Hao, A., Ng, D. C. H., Ponniah, S., Guo, K., Lufei, C., Zeng, Q., & Cao, X. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8447-8456.2004 · Cited by 202
Identification of GRIM-19, a Novel Cell Death-regulatory Gene Induced by the Interferon-β and Retinoic Acid Combination, Using a Genetic Approach
Angell, J. E., Lindner, D. J., Shapiro, P. S., Hofmann, E. R., & Kalvakolanu, D. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003929200 · Cited by 199
Decreased activities of ubiquinol:ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c:oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria.
Krähenbühl, S., Chang, M., Brass, E. P., & Hoppel, C. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54810-9 · Cited by 172

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Peralta, S., Wang, X., & Moraes, C. T. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.11.001 · Cited by 60
SIRT5 and post-translational protein modifications: A potential therapeutic target for myocardial ischemia-reperfusion injury with regard to mitochondrial dynamics and oxidative metabolism
Zou, R., Shi, W., Tao, J., Li, H., Lin, X., Yang, S., & Hua, P. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.11.005 · Cited by 61
STAT3 can serve as a hit in the process of malignant transformation of primary cells
Demaria, M., Misale, S., Giorgi, C., Miano, V., Camporeale, A., Campisi, J., Pinton, P., & Poli, V. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.20 · Cited by 60
Glucose Modulates Respiratory Complex I Activity in Response to Acute Mitochondrial Dysfunction
Cannino, G., El‐Khoury, R., Pirinen, M., Hutz, B., Rustin, P., Jacobs, H. T., & Dufour, É. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.386060 · Cited by 62
Extramyocellular interleukin‐6 influences skeletal muscle mitochondrial physiology through canonical JAK/STAT signaling pathways
Abid, H., Ryan, Z. C., Delmotte, P. F., Sieck, G. C., & Lanza, I. R. (2020) · The FASEB Journal · doi:10.1096/fj.202000965rr · Cited by 60
Nongenomic STAT5-dependent effects on Golgi apparatus and endoplasmic reticulum structure and function
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The Stat3 paradox: A killer and an oncogene
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Nuclear localization of pyruvate dehydrogenase complex-E2 (PDC-E2), a mitochondrial enzyme, and its role in signal transducer and activator of transcription 5 (STAT5)-dependent gene transcription
Chueh, F., Leong, K.-F., Cronk, R. J., Venkitachalam, S., Pabich, S., & Yu, C. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.03.004 · Cited by 58
Catecholamines suppress fatty acid re-esterification and increase oxidation in white adipocytes via STAT3
Reilly, S. M., Hung, C., Ahmadian, M., Zhao, P., Keinan, O., Gomez, A. V., DeLuca, J. H., Dadpey, B., Lu, D., Zaid, J., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0217-6 · Cited by 58
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Boengler, K., Heusch, G., & Schulz, R. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3309 · Cited by 58
STAT3 supports experimental K-RasG12D–induced murine myeloproliferative neoplasms dependent on serine phosphorylation
Gough, D. J., Marié, I. J., Lobry, C., Aifantis, I., & Levy, D. E. (2014) · Blood · doi:10.1182/blood-2013-02-484196 · Cited by 58
High-Density Lipoprotein Regulation of Mitochondrial Function
White, C. R., Datta, G., & Giordano, S. S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_22 · Cited by 59
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Weinhouse, C. (2017) · Toxicology · doi:10.1016/j.tox.2017.08.008 · Cited by 59
A first-in-human phase I study of OPB-111077, a small-molecule STAT3 and oxidative phosphorylation inhibitor, in patients with advanced cancers
Tolcher, A., Flaherty, K., Shapiro, G. I., Berlin, J., Witzig, T., Habermann, T., Bullock, A., Rock, E., Elekes, A., Lin, C., et al. (2018) · The Oncologist · doi:10.1634/theoncologist.2017-0325 · Cited by 57
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Zheng, Z.-Y., Yang, P.-L., Li, R.-Y., Liu, L.-X., Xu, X., Liao, L., Li, X., Chu, M.-Y., Liu, P., Huang, Q., et al. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.09.035 · Cited by 57
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Ishii, I., Harada, Y., & Kasahara, T. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00137 · Cited by 57
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Majoros, A., Platanitis, E., Szappanos, D., Cheon, H., Vogl, C., Shukla, P., Stark, G. R., Sexl, V., Schreiber, R. D., Schindler, C., et al. (2016) · EMBO Reports · doi:10.15252/embr.201540726 · Cited by 55
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Pei, H., Yang, Y., Zhao, H., Li, X., Yang, D., Li, D., & Yang, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5470457 · Cited by 56
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Hou, D., Wang, B., You, R., Wang, X., Liu, J., Zhan, W., Chen, P., Qin, T., Zhang, X., & Huang, H. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-3191 · Cited by 59
Metabolic control of DNA methylation in naive pluripotent cells
Betto, R. M., Diamante, L., Perrera, V., Audano, M., Rapelli, S., Lauria, A., Incarnato, D., Arboit, M., Pedretti, S., Rigoni, G., et al. (2021) · Nature Genetics · doi:10.1038/s41588-020-00770-2 · Cited by 55
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Huang, C., Chen, L., Chen, G. L., Chao, T., & Wang, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911092 · Cited by 54
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Prêle, C. M., Yao, E., O’Donoghue, R. J. J., Mutsaers, S. E., & Knight, D. A. (2012) · Proceedings of the American Thoracic Society · doi:10.1513/pats.201201-007aw · Cited by 54
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Reich, N. C. (2009) · Science Signaling · doi:10.1126/scisignal.290pe61 · Cited by 56
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Ganguly, D., Fan, M., Yang, C. H., Zbytek, B., Finkelstein, D., Roussel, M. F., & Pfeffer, L. M. (2018) · Oncotarget · doi:10.18632/oncotarget.25188 · Cited by 57
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Peron, M., Meneghetti, G., Meneghetti, G., Martorano, L., Betto, R. M., Facchinello, N., Tesoriere, A., Tiso, N., Martello, G., & Argenton, F. (2021) · Development · doi:10.1242/dev.199477 · Cited by 55
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Role of macrophage AHR/TLR4/STAT3 signaling axis in the colitis induced by non-canonical AHR ligand aflatoxin B1
Zhang, L., Cheng, D., Zhang, J., Tang, H., Li, F., Peng, Y., Duan, X., Meng, E., Zhang, C., Zeng, T., et al. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.131262 · Cited by 53
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Gobelli, D., Serrano‐Lorenzo, P., Esteban-Amo, M. J., Serna, J., Pérez-García, M. T., Orduña, A., Jourdain, A. A., Martín, M. A., de la Fuente, M. Á., & Simarro, M. (2023) · iScience · doi:10.1016/j.isci.2023.107473 · Cited by 57
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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
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Shi, H., Chen, S., & Chi, H. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.03.010 · Cited by 58
HDL protects against ischemia reperfusion injury by preserving mitochondrial integrity
Frias, M. A., Pedretti, S., Hacking, D., Somers, S., Lacerda, L., Opie, L. H., James, R. W., & Lecour, S. (2013) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2013.02.003 · Cited by 52
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Kitajima, S., Yoshida, A., Kohno, S., Li, F., Suzuki, S., Nagatani, N., Nishimoto, Y., Sasaki, N., Muranaka, H., Wan, Y., et al. (2017) · Oncogene · doi:10.1038/onc.2017.124 · Cited by 52
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Dard, L., Bellancé, N., Lacombe, D., & Rossignol, R. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.003 · Cited by 56
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Penna, C. R. R., Perrelli, M. G., Tullio, F., Angotti, C., Camporeale, A., Poli, V., & Pagliaro, P. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0371-z · Cited by 51
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Fujio, Y., Maeda, M., Mohri, T., Obana, M., Iwakura, T., Hayama, A., Yamashita, T., Nakayama, H., & Azuma, J. (2011) · Journal of Pharmacological Sciences · doi:10.1254/jphs.11r05cr · Cited by 50
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Nagata, N., Matsuo, K., Bettaieb, A., Bakke, J., Matsuo, I., Graham, J. L., Xi, Y., Liu, S., Tomilov, A. A., Tomilova, N. B., et al. (2012) · Endocrinology · doi:10.1210/en.2012-1406 · Cited by 51
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Authors: Wegrzyn, J., Potla, R., Chwae, Y.-J., Sepuri, N. B. V., Zhang, Q., Koeck, T., Derecka, M., Szczepanek, K., Szelag, M., Gornicka, A., Moh, A., Moghaddas, S., Chen, Q., Bobbili, S., Cichy, J., Dulak, J., Baker, D. P., Wolfman, A., Stuehr, D., Hassan, M. O., Fu, X.-Y., Avadhani, N., Drake, J. I., Fawcett, P., Lesnefsky, E. J., & Larner, A. C.
Affiliations: Department of Biochemistry and Molecular Biology and Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA.
Cleveland State University (US)
Corresponding author: Potla, Ramesh
Larner, Andrew C.
ORCID: Chwae, Yong-Joon
Sepuri, Naresh B. V.
Zhang, Qifang
Koeck, Thomas
Derecka, Marta
Szczepanek, Karol
Chen, Qun
Cichy, Joanna
Stuehr, Dennis
Fu, Xin-Yuan
Avadhani, Narayan
Drake, Jennifer I.
Lesnefsky, Edward J.
Larner, Andrew C.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2009-02-06
Volume: 323
Issue: 5915
Pages: 793-797
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1164551
PMC: PMC2758306
OpenAlex: W2042503285
Cited by: 1,014
References: 14
Citations by year: 2026: 41 · 2025: 37 · 2024: 44 · 2023: 66 · 2022: 65 · 2021: 78 · 2020: 57 · 2019: 62 · 2018: 58 · 2017: 60 · 2016: 54 · 2015: 57 · 2014: 61 · 2013: 62 · 2012: 82
FWCI: 28.42
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
AJOU Open Repository (Ajou University) (submittedVersion)
Jagiellonian University Repository (Jagiellonian University) (submittedVersion, cc-by-nc-nd)
IUScholarWorks (Indiana University) (submittedVersion)
Funders: National Institute on Aging (P01-AG15885, P01AG015885)
National Cancer Institute (R01CA098924, CA098924)
National Institute of Allergy and Infectious Diseases (R01AI059710)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: STAT3, mitochondrial STAT3, cellular respiration, electron transport chain, complex I, complex II, heart, liver, interleukin-6, cytokine signaling, transcription factors
MeSH terms: Animals, Cells, Cultured, Homeostasis, Mitochondria, Mitochondria, Heart, Mitochondria, Liver, NADH, NADPH Oxidoreductases, Oxidative Phosphorylation, Phosphorylation, Serine, Signal Transduction, Cell Respiration, Electron Transport Complex II, Electron Transport Complex I, STAT3 Transcription Factor, Mitochondrial Membranes, Mice, Precursor Cells, B-Lymphoid

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Function of Mitochondrial Stat3 in Cellular Respiration

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