Mitochondrial c-Jun N-terminal Kinase (JNK) Signaling Initiates Physiological Changes Resulting in Amplification of Reactive Oxygen Species Generation
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The JNK signaling cascade is critical for cellular responses to a variety of environmental and cellular stimuli. Although gene expression aspects of JNK signal transduction are well studied, there are minimal data on the physiological impact of JNK signaling. To bridge this gap, we investigated how JNK impacted physiology in HeLa cells. We observed that inhibition of JNK activity and JNK silencing with siRNA reduced the level of reactive oxygen species (ROS) generated during anisomycin-induced stress in HeLa cells. Silencing p38 had no significant impact on ROS generation under anisomycin stress. Moreover, JNK signaling mediated amplification of ROS production during stress. Mitochondrial superoxide production was shown to be the source of JNK-induced ROS amplification, as an NADPH oxidase inhibitor demonstrated little impact on JNK-mediated ROS generation. Using mitochondrial isolation from JNK null fibroblasts and targeting the mitochondrial scaffold of JNK, Sab, we demonstrated that mitochondrial JNK signaling was responsible for mitochondrial superoxide amplification. These results suggest that cellular stress altered mitochondria, causing JNK to translocate to the mitochondria and amplify up to 80% of the ROS generated largely by Complex I. This work demonstrates that a sequence of events exist for JNK mitochondrial signaling whereby ROS activates JNK, thereby affecting mitochondrial physiology, which can have effects on cell survival and death.
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Targeting JNK to mitochondria results in a significant increase in oxidants generated by complex I.
“Furthermore, targeting of JNK to the mitochondria resulted in a significant increase in oxidants generated by complex I (67).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [67]
Translocation of JNK to mitochondria is essential for cytochrome c release and apoptosis downstream of other stress activators.
“other studies have shown that translocation of JNK to the mitochondria was essential for cytochrome c release and apoptosis downstream of other stress activators (67, 189).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [67]
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How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Signal integration by JNK and p38 MAPK pathways in cancer development
Wagner, E. F., & Nebreda, Á. R. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2694 · Cited by 2,583 · see citing works
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792 · see citing works
The JNK signal transduction pathway
Weston, C. R. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(01)00258-1 · Cited by 1,545 · see citing works
Dhanasekaran, D. N., & Reddy, E. P. (2008) · Oncogene · doi:10.1038/onc.2008.301 · Cited by 1,529 · see citing works
Evidence that glutamine, not sugar, is the major energy source for cultured HeLa cells.
Reitzer, L. J., Wice, B. M., & Kennell, D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30124-2 · Cited by 1,240 · see citing works
ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
Tobiume, K., Matsuzawa, A., Takahashi, T., Nishitoh, H., Morita, K., Takeda, K., Minowa, O., Miyazono, K., Noda, T., & Ichijo, H. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve046 · Cited by 1,213 · see citing works
The JNK signal transduction pathway
Weston, C. R., & Davis, R. J. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.001 · Cited by 1,021 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
A Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway
Dickens, M., Rogers, J. S., Cavanagh, J., Raitano, A., Xia, Z., Halpern, J. R., Greenberg, M. E., Sawyers, C. L., & Davis, R. J. (1997) · Science · doi:10.1126/science.277.5326.693 · Cited by 675 · see citing works
Stolk, J. N., Hiltermann, T. J. N., Dijkman, J. H., & Verhoeven, A. J. (1994) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.11.1.8018341 · Cited by 650 · see citing works
Shen, H.-M., & Liu, Z.-G. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.056 · Cited by 629 · see citing works
Hanawa, N., Shinohara, M., Saberi, B., Gaarde, W. A., Han, D., & Kaplowitz, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708916200 · Cited by 527 · see citing works
Mitochondria Are a Major Source of Paraquat-induced Reactive Oxygen Species Production in the Brain
Castello, P. R., Drechsel, D. A., & Patel, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700827200 · Cited by 477 · see citing works
Lei, K., Nimnual, A. S., Zong, W., Kennedy, N. J., Flavell, R. A., Thompson, C. B., Bar‐Sagi, D., & Davis, R. J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4929-4942.2002 · Cited by 463 · see citing works
Translocation of SAPK/JNK to Mitochondria and Interaction with Bcl-xL in Response to DNA Damage
Kharbanda, S., Saxena, S., Yoshida, K., Pandey, P., Kaneki, M., Wang, Q., Cheng, K., Chen, Y.-N., Campbell, A., Sudha, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.322 · Cited by 429 · see citing works
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Role for mitochondrial oxidants as regulators of cellular metabolism
Nemoto, S., Takeda, K., Yu, Z.-X., Ferrans, V. J., & Finkel, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7311-7318.2000 · Cited by 393 · see citing works
Biochemical Assays of Respiratory Chain Complex Activity
Kirby, D. M., Thorburn, D. R., Turnbull, D. M., & Taylor, R. W. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80004-x · Cited by 383 · see citing works
Generation of superoxide by the mitochondrial Complex I
Grivennikova, V. G., & Vinogradov, A. D. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.013 · Cited by 379 · see citing works
Mukhopadhyay, P., Rajesh, M., Haskó, G., Hawkins, B. J., Madesh, M., & Pacher, P. (2007) · Nature Protocols · doi:10.1038/nprot.2007.327 · Cited by 373 · see citing works
Aoki, H., Kang, P. M., Hampe, J., Yoshimura, K., Noma, T., Matsuzaki, M., & Izumo, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112355200 · Cited by 332 · see citing works
Chemical Genetic Analysis of the Time Course of Signal Transduction by JNK
Ventura, J., Hübner, A., Zhang, C., Flavell, R. A., Shokat, K. M., & Davis, R. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.018 · Cited by 323 · see citing works
Ventura, J.-J., Cogswell, P., Flavell, R. A., Baldwin, A. S., & Davis, R. J. (2004) · Genes & Development · doi:10.1101/gad.1223004 · Cited by 303 · see citing works
Trumpower, B. L., & Edwards, C. A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86947-8 · Cited by 235 · see citing works
Isolation and Subfractionation of Mitochondria from Animal Cells and Tissue Culture Lines
Pallotti, F., & Lenaz, G. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80001-4 · Cited by 232 · see citing works
Anuradha, C. D., Kanno, S., & Hirano, S. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00591-3 · Cited by 231 · see citing works
Kinase signaling cascades in the mitochondrion: a matter of life or death
Horbinski, C., & Chu, C. T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.030 · Cited by 225 · see citing works
Mitochondrial modulation: reversible phosphorylation takes center stage?
Pagliarini, D. J., & Dixon, J. E. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.005 · Cited by 223 · see citing works
Glutathionylation of Mitochondrial Proteins
Hurd, T., Costa, N. J., Dahm, C., Beer, S. M., Brown, S. E., Filipovska, A., & Murphy, M. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.999 · Cited by 195 · see citing works
Superoxide Flux in Endothelial Cells via the Chloride Channel-3 Mediates Intracellular Signaling
Hawkins, B. J., Madesh, M., Kirkpatrick, C. J., & Fisher, A. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0830 · Cited by 184 · see citing works
Garcia, J., Han, D., Sancheti, H., Yap, L.-P., Kaplowitz, N., & Cadenas, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.164160 · Cited by 178 · see citing works
Detection and manipulation of mitochondrial reactive oxygen species in mammalian cells
Forkink, M., Smeitink, J. A. M., Brock, R. E., Willems, P. H. G. M., & Koopman, W. J. H. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.022 · Cited by 150 · see citing works
Soberanes, S., Urich, D., Baker, C. M., Burgess, Z., Chiarella, S. E., Bell, E. L., Ghio, A. J., Vizcaya‐Ruíz, A. D., Liu, J., Ridge, K. M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808844200 · Cited by 144 · see citing works
Positioning mitochondrial plasticity within cellular signaling cascades
Soubannier, V., & McBride, H. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.008 · Cited by 140 · see citing works
The JNK Cascade as a Biochemical Switch in Mammalian Cells
Bagowski, C. P., Besser, J., Frey, C. R., & Ferrell, J. E. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00083-6 · Cited by 139 · see citing works
Zhou, Q., Lam, P. Y., Han, D., & Cadenas, E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04957.x · Cited by 111 · see citing works
A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria
Wiltshire, C. J., Matsushita, M., Tsukada, S., Gillespie, D. A., & May, G. (2002) · Biochemical Journal · doi:10.1042/bj20020553 · Cited by 103 · see citing works
Kang, Y., & Lee, S. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21470 · Cited by 101 · see citing works
Dougherty, C. J., Kubasiak, L. A., Frazier, D. P., Li, H., Xiong, W., Bishopric, N. H., & Webster, K. A. (2004) · The FASEB Journal · doi:10.1096/fj.04-1505com · Cited by 92 · see citing works
Kamenecka, T., Jiang, R., Song, X., Duckett, D. R., Chen, W., Ling, Y. Y., Habel, J. E., Laughlin, J. D., Chambers, J. W., Figuera-Losada, M., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901351f · Cited by 68 · see citing works
Self-citationPrevention of premature senescence requires JNK regulation of Bcl-2 and reactive oxygen species
Lee, J. J., Lee, J. H., Ko, Y. G., Hong, S., & Js, L. (2009) · Oncogene · doi:10.1038/onc.2009.355 · Cited by 66 · see citing works
Mitochondrial targeting of JNK/SAPK in the phorbol ester response of myeloid leukemia cells
Ito, Y., Mishra, N. C., Yoshida, K., Kharbanda, S., Saxena, S., & Kufe, D. (2001) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400886 · Cited by 62 · see citing works
Mkp1Is a c-Jun Target Gene That Antagonizes JNK-Dependent Apoptosis in Sympathetic Neurons
Kristiansen, M., Hughes, R., Patel, P., Jacques, T. S., Clark, A. R., & Ham, J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2824-10.2010 · Cited by 60 · see citing works
Cerebral ischemia provokes a profound exchange of activated JNK isoforms in brain mitochondria
Zhao, Y., & Herdegen, T. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.02.012 · Cited by 51 · see citing works
Kang (1994) · Oncology Reports · doi:10.3892/or_00000053 · Cited by 42 · see citing works
Sab (SH3BP5), a novel mitochondria-localized JNK-interacting protein
Wiltshire, C. J., Gillespie, D. A., & May, G. (2004) · Biochemical Society Transactions · doi:10.1042/bst0321075 · Cited by 36 · see citing works
Effects of 4-hydroxynonenal on mitochondrial 3-hydroxy-3-methylglutaryl (HMG-CoA) synthase
Patel, V. B., Spencer, C. H., Young, T. A., Lively, M. O., & CUNNINGHAM, C. C. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.004 · Cited by 32 · see citing works
Kim, M., Lee, K., & Lee, S. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06363.x · Cited by 24 · see citing works
Amplification loop cascade for increasing caspase activity induced by docetaxel
Cao, D., Qiao, B., Ge, Z., & Yuan, Y. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20563 · Cited by 24 · see citing works
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TNF and ROS crosstalk in inflammation
Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Phosphoinositide 3-Kinase/Akt Signaling and Redox Metabolism in Cancer
Koundouros, N., & Poulogiannis, G. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00160 · Cited by 420 · see citing works
Ruiz-Torres, V., Encinar, J. A., Herranz‐López, M., Pérez-Sánchez, A., Galiano, V., Barrajón‐Catalán, E., & Micol, V. (2017) · Molecules · doi:10.3390/molecules22071037 · Cited by 229 · see citing works
Brand, M. D., Goncalves, R. L. S., Orr, A. L., Vargas, L., Gerencser, A. A., Borch Jensen, M., Wang, Y. T., Melov, S., Turk, C. N., Matzen, J. T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.012 · Cited by 228 · see citing works
Guo, C., Yang, M. G., Li, J., Wang, J., Yu, Y., Li, Y., Duan, J., Zhou, X., Li, Y., & ccmu.edu.cn, Z. Z. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s112030 · Cited by 222 · see citing works
Immune mechanisms in acetaminophen-induced acute liver failure.
Krenkel, O., Mossanen, J. C., & Tacke, F. (2014) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2304-3881.2014.11.01 · Cited by 221 · see citing works
Suppressors of superoxide production from mitochondrial complex III
Orr, A. L., Vargas, L., Turk, C. N., Baaten, J., Matzen, J., Dardov, V. J., Attle, S. J., Li, J., Quackenbush, D., Goncalves, R. L. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1910 · Cited by 207 · see citing works
Kumar, M., & Bansal, N. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02611-7 · Cited by 204 · see citing works
Kim, K. H., An, D. R., Song, J. S., Yoon, J., Kim, H. S., Yoon, H. J., Im, H. N., Kim, J., Kim, D., Lee, S. J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120251109 · Cited by 203 · see citing works
Win, S., Than, T. A., Han, D., Petrovic, L. M., & Kaplowitz, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276089 · Cited by 197 · see citing works
Han, D., Dara, L., Win, S., Than, T. A., Yuan, L., Abbasi, S. Q., Liu, Z., & Kaplowitz, N. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.01.009 · Cited by 197 · see citing works
Win, S., Than, T. A., Min, R. W. M., Aghajan, M., & Kaplowitz, N. (2016) · Hepatology · doi:10.1002/hep.28486 · Cited by 187 · see citing works
Win, S., Than, T. A., Fernández-Checa, J. C., & Kaplowitz, N. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.522 · Cited by 174 · see citing works
Win, S., Than, T. A., Zhang, J., Oo, C., Min, R. W. M., & Kaplowitz, N. (2017) · Hepatology · doi:10.1002/hep.29689 · Cited by 171 · see citing works
Javadov, S. A., Jang, S., & Agostini, B. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.05.013 · Cited by 157 · see citing works
Meng, M., Huo, R., Wang, Y., Ma, N., Shi, X., Shen, X., & Chang, G. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.024 · Cited by 155 · see citing works
Nuclear-Mitochondrial Interactions
Walker, B. R., & Moraes, C. T. (2022) · Biomolecules · doi:10.3390/biom12030427 · Cited by 136 · see citing works
Critical Role for Mixed-Lineage Kinase 3 in Acetaminophen-Induced Hepatotoxicity
Sharma, M., Gadang, V., & Jaeschke, A. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.079863 · Cited by 118 · see citing works
Dixit, D., Ghildiyal, R., Anto, N. P., & Sen, E. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.179 · Cited by 101 · see citing works
In vivo genetic dissection of tumor growth and the Warburg effect
Wang, C., Purkayastha, A., Jones, K. T., Thaker, S. K., & Banerjee, U. K. (2016) · eLife · doi:10.7554/elife.18126 · Cited by 90 · see citing works
Heslop, K. A., Rovini, A. M. F., Hunt, E. G., Fang, D., Morris, M. E., Christie, C. F., Gooz, M. B., DeHart, D. N., Dang, Y., Lemasters, J. J., et al. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113728 · Cited by 91 · see citing works
Cell death in drug-induced liver injury
Iorga, A., & Dara, L. (2019) · Advances in pharmacology · doi:10.1016/bs.apha.2019.01.006 · Cited by 87 · see citing works
Redox signaling pathways in unilateral ureteral obstruction (UUO)-induced renal fibrosis
Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Aparicio‐Trejo, O. E., Ortega-Lozano, A. J., & Pedraza‐Chaverrí, J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.034 · Cited by 87 · see citing works
Li, W., Jiang, B., Cao, X., Xie, Y., & Huang, T. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.11.021 · Cited by 86 · see citing works
Transcriptional Regulation of Energy Metabolism in Cancer Cells
Rodríguez‐Enríquez, S., Marín‐Hernández, Á., Gallardo‐Pérez, J. C., Pacheco-Velázquez, S. C., Belmont-Díaz, J., Robledo‐Cadena, D. X., Vargas-Navarro, J. L., de la Peña, N. A. C., Saavedra, E., & Moreno‐Sánchez, R. (2019) · Cells · doi:10.3390/cells8101225 · Cited by 86 · see citing works
Rehfeldt, S. C. H., Laufer, S., & Goettert, M. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073701 · Cited by 85 · see citing works
Xu, J., Qin, X., Cai, X., Yang, L., Xing, Y., Li, J., Zhang, L., Tang, Y., Liu, J., Zhang, X., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.012 · Cited by 84 · see citing works
Loss of PDK4 switches the hepatic NF‐κB/TNF pathway from pro‐survival to pro‐apoptosis
Wu, J., Zhao, Y., Park, Y., Lee, J., Gao, L., Zhao, J., & Wang, L. (2018) · Hepatology · doi:10.1002/hep.29902 · Cited by 83 · see citing works
Chambers, J. W., Pachori, A. S., Howard, S., Iqbal, S., & LoGrasso, P. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.406777 · Cited by 81 · see citing works
Self-citationWin, S., Than, T. A., & Kaplowitz, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113657 · Cited by 80 · see citing works
Sun, X., Jia, H., Xu, Q., Zhao, C., & Xu, C. (2019) · Food & Function · doi:10.1039/c9fo01922g · Cited by 77 · see citing works
Nijboer, C. H. A., Bonestroo, H. J. C., Zijlstra, J., Kavelaars, A., & Heijnen, C. J. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.017 · Cited by 75 · see citing works
Paul, M., Hemshekhar, M., Thushara, R. M., Sundaram, M. S., NaveenKumar, S. K., Naveen, S., Sannaningaiah, D., Somyajit, K., West, R., Basappa, B., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127558 · Cited by 73 · see citing works
Chambers, J. W., Howard, S., & LoGrasso, P. V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.421354 · Cited by 72 · see citing works
Self-citationZheng, K., Iqbal, S., Hernandez, P., Park, H., LoGrasso, P. V., & Feng, Y. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501256y · Cited by 71 · see citing works
Self-citationApoptosis Signal-regulating Kinase 1 promotes Ochratoxin A-induced renal cytotoxicity
Liang, R., Shen, X. L., Zhang, B., Li, Y., Xu, W., Zhao, C., Luo, Y., & Huang, K. (2015) · Scientific Reports · doi:10.1038/srep08078 · Cited by 64 · see citing works
Chen, R., Hollborn, M., Grosche, A., Reichenbach, A., Wiedemann, P., Bringmann, A., & Kohen, L. (2014) · Europe PMC (PubMed Central) · Cited by 61 · see citing works
Endoplasmic reticulum stress sensor IRE1α propels neutrophil hyperactivity in lupus.
Sule, G., Abuaita, B. H., Steffes, P. A., Fernandes, A. T., Estes, S., Dobry, C., Pandian, D., Gudjonsson, J., Kahlenberg, J., O'Riordan, M., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci137866 · Cited by 53 · see citing works
Aluminum Induces Osteoblast Apoptosis Through the Oxidative Stress-Mediated JNK Signaling Pathway
Li, X., Han, Y., Guan, Y., Zhang, L. N., Bai, C., & Li, Y. (2012) · Biological Trace Element Research · doi:10.1007/s12011-012-9523-5 · Cited by 60 · see citing works
The deafness gene DFNA5 induces programmed cell death through mitochondria and MAPK-related pathways
Rossom, S. V., de Beeck, K. O., Hristovska, V., Winderickx, J., & Camp, G. V. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00231 · Cited by 59 · see citing works
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Benn, C., & Dawson, L. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00242 · Cited by 57 · see citing works
Phosphoregulation on mitochondria: Integration of cell and organelle responses
Lucero, M., Suarez, A. E., & Chambers, J. W. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13141 · Cited by 58 · see citing works
Self-citationUntangling the effect of insulin action on brain mitochondria and metabolism
Schell, M., Wardelmann, K., & Kleinridders, A. (2021) · Journal of Neuroendocrinology · doi:10.1111/jne.12932 · Cited by 56 · see citing works
Network Motifs in JNK Signaling
Sehgal, V., & Ram, P. T. (2013) · Genes & Cancer · doi:10.1177/1947601913507577 · Cited by 57 · see citing works
Li, Z., Mbah, N. E., Overmeyer, J. H., Sarver, J. G., George, S., Trabbic, C. J., Erhardt, P., & Maltese, W. A. (2019) · BMC Cancer · doi:10.1186/s12885-019-5288-y · Cited by 56 · see citing works
Ali, I., Li, C., Kuang, M., Shah, A. U., Shafiq, M., Ahmad, M. A., Abdalmegeed, D., Li, L., & Wang, G. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2022.05.121 · Cited by 54 · see citing works
Chen, T., Zhao, L., Chen, S., Zheng, B., Chen, H., Zeng, T., Sun, H., Zhong, S.-J., Wu, W., Lin, X., et al. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111131 · Cited by 53 · see citing works
Huo, Y., Win, S., Than, T. A., Yin, S., Ye, M., Hu, H., & Kaplowitz, N. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6833 · Cited by 53 · see citing works
Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases
Laughlin, J. D., Nwachukwu, J. C., Figuera-Losada, M., Cherry, L., Nettles, K. W., & LoGrasso, P. V. (2012) · Structure · doi:10.1016/j.str.2012.09.021 · Cited by 50 · see citing works
“SAB is a more recently identified scaffold protein localized to the mitochondria, accounting for JNK-mediated ROS generation (Chambers and LoGrasso, 2011), and acetaminophen-induced liver injury (Win et al., 2011), and is also a JNK substrate.”
BackgroundSelf-citationJang, S., Yu, L., Abdelmegeed, M. A., Gao, Y., Banerjee, A., & Song, B. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.040 · Cited by 50 · see citing works
Wang, C., Nie, X., Zhang, Y., Li, T., Mao, J., Liu, X., Gu, Y., Shi, J., Xiao, J., Wan, C., et al. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.06.012 · Cited by 50 · see citing works
Nelson, K. J., Bolduc, J. A., Wu, H., Collins, J. A., Burke, E. A., Reisz, J. A., Klomsiri, C., Wood, S. T., Yammani, R. R., Poole, L. B., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004613 · Cited by 49 · see citing works
Ou, Z., Chen, J., Dai, W.-P., Liu, X., Yang, Y., Li, Y., Lin, Z., Wang, T.-T., Wu, Y., Su, D.-H., et al. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00218.2016 · Cited by 48 · see citing works
Khan, I., Paul, S., Jakhar, R., Bhardwaj, M., Han, J., & Kang, S. C. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.09.094 · Cited by 48 · see citing works
Tempol, a superoxide dismutase mimetic agent, reduces cisplatin-induced nephrotoxicity in rats
Ewees, M. G., Messiha, B. A. S., Abdel‐Bakky, M. S., Bayoumi, A. M. A., & Abo‐Saif, A. A. (2018) · Drug and Chemical Toxicology · doi:10.1080/01480545.2018.1485688 · Cited by 48 · see citing works
Activation of endothelial TRPM2 exacerbates blood–brain barrier degradation in ischemic stroke
Zong, P., Feng, J., Li, C. X., Jellison, E. R., Yue, Z., Miller, B. A., & Yue, L. (2023) · Cardiovascular Research · doi:10.1093/cvr/cvad126 · Cited by 47 · see citing works
Win, S., Min, R. W. M., Chen, C. Q., Zhang, J., Chen, Y., Li, M., Suzuki, A., Abdelmalek, M. F., Wang, Y., Aghajan, M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci128289 · Cited by 42 · see citing works
Weng, C., Yu, C.-C., Kuo, M., Chen, B.-C., & Lin, C. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.030 · Cited by 44 · see citing works
Chen, J., Chen, B., Zou, Z., Li, W., Zhang, Y., Xie, J., & Liu, C. (2017) · Oncotarget · doi:10.18632/oncotarget.22592 · Cited by 42 · see citing works
Hirata, Y., Inoue, A., Suzuki, S., Takahashi, M., Matsui, R., Kono, N., Noguchi, T., & Matsuzawa, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-59636-6 · Cited by 40 · see citing works
Bavachinin Induces Oxidative Damage in HepaRG Cells through p38/JNK MAPK Pathways
Wang, S., Wang, M., Wang, M., Tian, Y., Sun, X. Y., Sun, G., & Sun, X. (2018) · Toxins · doi:10.3390/toxins10040154 · Cited by 40 · see citing works
ROS-mediated JNK pathway critically contributes to PFOS-triggered apoptosis in SH-SY5Y cells
Sun, P., Gu, L., Luo, J., Qin, Y., Sun, L., & Jiang, S. (2019) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2019.106821 · Cited by 39 · see citing works
Jang, S., & Javadov, S. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113526 · Cited by 38 · see citing works
Sab mediates mitochondrial dysfunction involved in imatinib mesylate-induced cardiotoxicity
Chambers, T. P., Santiesteban, L., Gomez, D. F., & Chambers, J. W. (2017) · Toxicology · doi:10.1016/j.tox.2017.03.006 · Cited by 38 · see citing works
Self-citationWin, S., Min, R. W. M., Zhang, J., Kanel, G. C., Wanken, B., Chen, Y., Li, M., Wang, Y., Suzuki, A., Aung, F. W. M., et al. (2021) · Hepatology · doi:10.1002/hep.32083 · Cited by 38 · see citing works
cJun N-terminal kinase (JNK) phosphorylation of serine 36 is critical for p66Shc activation
Khalid, S., Drasche, A., Thurner, M., Hermann, M., Ashraf, M., Fresser, F., Baier, G., Kremser, L., Lindner, H. H., & Troppmair, J. (2016) · Scientific Reports · doi:10.1038/srep20930 · Cited by 37 · see citing works
Prem, P. N., Sivakumar, B., Boovarahan, S. R., & Kurian, G. A. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154123 · Cited by 36 · see citing works
The Toxicity of Aluminum Chloride on Kidney of Rats
Liu, J., Wang, Q., Sun, X., Yang, X., Zhuang, C., Xu, F., Cao, Z., & Li, Y. (2016) · Biological Trace Element Research · doi:10.1007/s12011-016-0648-9 · Cited by 35 · see citing works
Bradfield, C. J., Liang, J. J., Ernst, O., John, S. P., Sun, J., Ganesan, S., de Jesus, A. A., Bryant, C. E., Goldbach-Mansky, R., & Fraser, I. D. C. (2023) · Cell Death & Differentiation · doi:10.1038/s41418-022-01106-9 · Cited by 33 · see citing works
Blood Brothers: Hemodynamics and Cell–Matrix Interactions in Endothelial Function
Yurdagul, A., & Orr, A. W. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6525 · Cited by 32 · see citing works
MicroRNA‐133 suppresses ZFHX3‐dependent atrial remodelling and arrhythmia
Cheng, T.-Y., Kao, Y., Chao, T., Lin, Y., Chen, S., & Chen, Y. (2019) · Acta Physiologica · doi:10.1111/apha.13322 · Cited by 32 · see citing works
Pasqua, L. G. D., Cagna, M., Berardo, C., Vairetti, M., & Ferrigno, A. (2022) · Biomedicines · doi:10.3390/biomedicines10010194 · Cited by 32 · see citing works
Alcohol induces mitochondrial derangements in alveolar macrophages by upregulating NADPH oxidase 4
Morris, N. L., Harris, F. L., Brown, L. A. S., & Yeligar, S. M. (2020) · Alcohol · doi:10.1016/j.alcohol.2020.11.004 · Cited by 29 · see citing works
Chaanine, A. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910579 · Cited by 30 · see citing works
Liu, R., Pulliam, D. A., Liu, Y., & Salmon, A. B. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.014 · Cited by 29 · see citing works
Rani, R., Kumar, S., Sharma, A., Mohanty, S. K., Donnelly, B., Tiao, G. M., & Gandhi, C. R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005583 · Cited by 29 · see citing works
Wang, Z., Shen, J., Sun, W. Y., Zhang, T., Zuo, D., Wang, H., Wang, G., Xu, J., Yin, F., Mao, M., et al. (2019) · Cancer Science · doi:10.1111/cas.14008 · Cited by 28 · see citing works
Role of c-Jun N-Terminal Kinases (JNKs) in Epilepsy and Metabolic Cognitive Impairment
Busquets, O., Ettcheto, M., Cano, A. C., Manzine, P. R., Sánchez‐López, E., Espinosa-Jiménez, T., Verdaguer, E., Castro-Torres, R. D., Beas‐Zárate, C., Sureda, F. X., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010255 · Cited by 28 · see citing works
Ma, Y., Ma, X., An, Y., Sun, Y., Dou, W., Li, M., Bao, H., & Zhang, C. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.804241 · Cited by 28 · see citing works
Guillonneau, M., Paris, F., Dutoit, S., Estéphan, H., Bénéteau, E., Huot, J., & Corre, I. (2016) · The FASEB Journal · doi:10.1096/fj.201500194r · Cited by 27 · see citing works
Enhancement of the antimycobacterial activity of macrophages by ajoene
Choi, J.-A., Cho, S., Lim, Y.-J., Lee, J., Go, D., Kim, S.-H., & Song, C. (2017) · Innate Immunity · doi:10.1177/1753425917747975 · Cited by 27 · see citing works
Kosić, M., Paunović, V., Ristic, B. Z., Mirčić, A., Bošnjak, M., Stevanović, D., Kravic‐Stevovic, T., Trajković, V., & Harhaji-Trajkovic, L. M. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.06.003 · Cited by 27 · see citing works
Karthivashan, G., Arulselvan, P., & Fakurazi, S. (2015) · RSC Advances · doi:10.1039/c5ra07838e · Cited by 26 · see citing works
Li, G., Wang, M., Hao, L., Loo, W. T.-Y., Jin, L., Cheung, M., Chow, L. W. C., & Ng, E. L. Y. (2014) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2014.02.015 · Cited by 26 · see citing works
Sahai, R., Bhattacharjee, A., Shukla, V. N., Yadav, P., Hasanain, M., Sarkar, J., Narender, T., & Mitra, K. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01605-5 · Cited by 26 · see citing works
Nunes, G. D., Wilson, E. R., Hurley, E. L., He, B., O’Malley, B. W., Poitelon, Y., Wrabetz, L. G., & Feltri, M. L. (2021) · eLife · doi:10.7554/elife.66278 · Cited by 24 · see citing works
GKN2 promotes oxidative stress-induced gastric cancer cell apoptosis via the Hsc70 pathway
Zhang, Z., Xue, H., Dong, Y., Zhang, J., Pan, Y., Shi, L., Xiong, P., Zhu, J., Li, W., Zheng, W., et al. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1336-3 · Cited by 25 · see citing works
Kim, D. H., Lee, D. H., Jo, M. R., Son, D. J., Park, M. H., Hwang, C. J., Park, J. H., Yuk, D. Y., Yoon, D. Y., Jung, Y., et al. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39284 · Cited by 24 · see citing works
Novel Insights into the PKCβ-dependent Regulation of the Oxidoreductase p66Shc
Haller, M., Khalid, S., Kremser, L., Fresser, F., Furlan, T., Hermann, M., Guenther, J., Drasche, A., Leitges, M., Giorgio, M., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.752766 · Cited by 24 · see citing works
Neutrophil biology within hepatic environment
Alvarenga, D. M., Mattos, M. S., de Araujo, A., Antunes, M. M., & Menezes, G. B. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2722-9 · Cited by 22 · see citing works
Lee, M., Yang, C., Song, G., & Lim, W. (2021) · Antioxidants · doi:10.3390/antiox10060957 · Cited by 22 · see citing works
Min, R. W. M., Aung, F. W. M., Liu, B., Arya, A., & Win, S. (2022) · Biomedicines · doi:10.3390/biomedicines10082035 · Cited by 22 · see citing works
Silicon nitride as a biomaterial
Pezzotti, G. (2023) · Journal of the Ceramic Society of Japan · doi:10.2109/jcersj2.23057 · Cited by 23 · see citing works
Chandrasekaran, S., & Caparon, M. G. (2016) · mBio · doi:10.1128/mbio.02215-15 · Cited by 22 · see citing works
Jung, K. I., Ko, D.-H., Shin, N., Pyo, C.-W., & Choi, S.-Y. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.03.021 · Cited by 22 · see citing works
Sulfatide Inhibits HMGB1 Secretion by Hindering Toll-Like Receptor 4 Localization Within Lipid Rafts
Kim, H. S., Han, M., Park, I. H., Park, C. H., Kwak, M. S., & Shin, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01305 · Cited by 22 · see citing works
Latham, S. L., O’Donnell, Y. E. I., & Croucher, D. R. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220808 · Cited by 21 · see citing works
A Small Molecule Bidentate-Binding Dual Inhibitor Probe of the LRRK2 and JNK Kinases
Feng, Y., Chambers, J. W., Iqbal, S., Koenig, M., Park, H., Cherry, L., Hernandez, P., Figuera-Losada, M., & LoGrasso, P. V. (2013) · ACS Chemical Biology · doi:10.1021/cb3006165 · Cited by 21 · see citing works
Self-citationChen, C., Hsieh, T., Lin, Y., Liu, Y., Liou, J., & Yen, Y. (2019) · Cancers · doi:10.3390/cancers11091345 · Cited by 21 · see citing works
- Authors
- Chambers, J. W., & LoGrasso, P. V.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- LoGrasso, Philip V.
- ORCID
- Chambers, Jeremy W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-05
- Volume
- 286
- Issue
- 18
- Pages
- 16052-16062
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3091214
- OpenAlex
- W2032947455
- Cited by
- 194
- References
- 50
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 16 · 2023: 7 · 2022: 11 · 2021: 14 · 2020: 14 · 2019: 22 · 2018: 15 · 2017: 14 · 2016: 14 · 2015: 13 · 2014: 14 · 2013: 10 · 2012: 7
- FWCI
- 4.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (U01NS057153)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- JNK signaling, reactive oxygen species, mitochondrial superoxide, p38 MAPK, mitochondrial complex I, mitochondrial translocation, NADPH oxidase, HeLa cells, cell survival and death
- MeSH terms
- Animals, Anisomycin, Fibroblasts, Humans, Protein Synthesis Inhibitors, Signal Transduction, Reactive Oxygen Species, Mice, Knockout, NADPH Oxidases, Mitochondrial Proteins, Electron Transport Complex I, JNK Mitogen-Activated Protein Kinases, Mice
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