Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity
Open accessAbstract
SIRT1 is involved in the pathogenesis of obesity, diabetes, and aging. However, it is not clear how SIRT1 activity is regulated by intracellular kinases in cells. In this study, we investigated SIRT1 phosphorylation and protein degradation in response to JNK1 activation in obese mice. Mouse SIRT1 is phosphorylated by JNK1 at Ser-46 (Ser-47 in human SIRT1), which is one of the four potential residues targeted by JNK1. The phosphorylation induces a brief activation of SIRT1 function and degradation of SIRT1 thereafter by the proteasome. Ubiquitination occurs in SIRT1 protein after the phosphorylation. Mutation of Ser-46 to alanine prevents the phosphorylation, ubiquitination, and degradation. In vivo, SIRT1 undergoes an extensive degradation in hepatocytes in obesity as a consequence of persistent activation of JNK1. The degradation leads to inhibition of SIRT1 function, which contributes to development of hepatic steatosis. The degradation disappears in obesity when JNK1 is inactivated in mice. JNK2 exhibits an opposite activity in the regulation of SIRT1 degradation. The JNK1-SIRT1 pathway provides a new molecular mechanism for the pathogenesis of hepatic steatosis in obesity.
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Persistent activation of JNK and/or p38K is positively associated with various liver diseases such as steatohepatitis and I/R injury.
“Furthermore, persistent activation of JNK and/or p38K is positively associated with various liver diseases such as steatohepatitis and I/R injury [122], [123], [124], [125], suggesting the clinical importance of JNK and p38K in human disease states, as reviewed [126].”
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Cites
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057 · see citing works
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239 · see citing works
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188 · see citing works
Self-citationNutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works
Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · see citing works
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924 · see citing works
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works
Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works
Self-citationMechanism of hepatic insulin resistance in non-alcoholic fatty liver disease
Samuel, V. T., Liu, Z.-X., Qu, X., Elder, B. D., Bilz, S., Befroy, D., Romanelli, A. J., & Shulman, G. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313478200 · Cited by 1,322 · see citing works
Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., & Li, X. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.02.006 · Cited by 1,112 · see citing works
Mechanism of Human SIRT1 Activation by Resveratrol
Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065 · see citing works
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047 · see citing works
Serine Phosphorylation of Insulin Receptor Substrate 1 by Inhibitor κB Kinase Complex
Gao, Z., Hwang, D. H., Bataille, F., Lefevre, M., York, D. A., Quon, M. J., & Ye, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209459200 · Cited by 777 · see citing works
Self-citationSubstrate-specific activation of sirtuins by resveratrol
Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works
SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling
Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.-F., Kwon, H., Yi, S., Mucke, L., & Gan, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509329200 · Cited by 740 · see citing works
Hyperlipidemic Effects of Dietary Saturated Fats Mediated through PGC-1β Coactivation of SREBP
Lin, J. D., Yang, R., Tarr, P. T., Wu, P., Handschin, C., Li, S., Yang, W., Pei, L., Uldry, M., Tontonoz, P., et al. (2005) · Cell · doi:10.1016/j.cell.2004.11.043 · Cited by 618 · see citing works
Chavez, J. A., Knotts, T. A., Wang, L.-P., Li, G., Dobrowsky, R. T., Florant, G. L., & Summers, S. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212307200 · Cited by 617 · see citing works
A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange
Liu, Y., Dentin, R., Chen, D., Hedrick, S. A., Ravnskjær, K., Schenk, S., Milne, J. C., Meyers, D. J., Cole, P., Yates, J. R., et al. (2008) · Nature · doi:10.1038/nature07349 · Cited by 556 · see citing works
Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1
Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 549 · see citing works
JNK1 but not JNK2 promotes the development of steatohepatitis in mice
Schattenberg, J. M., Singh, R., Wang, Y., Lefkowitch, J. H., Rigoli, R. M., Scherer, P. E., & Czaja, M. J. (2006) · Hepatology · doi:10.1002/hep.20999 · Cited by 384 · see citing works
Gao, Z., Zhang, X., Zuberi, A. R., Hwang, D. H., Quon, M. J., Lefevre, M., & Ye, J. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0383 · Cited by 335 · see citing works
Self-citationSIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X. M., Nicosia, S. V., Bhalla, K. N., & Bai, W. (2007) · Nature Cell Biology · doi:10.1038/ncb1645 · Cited by 324 · see citing works
Phosphorylation Regulates SIRT1 Function
Sasaki, T., Maier, B., Koclega, K. D., Chruszcz, M., Gluba, W., Stukenberg, P. T., Minor, W., & Scrable, H. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004020 · Cited by 290 · see citing works
JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity
Nasrin, N., Kaushik, V. K., Fortier, E., Wall, D., Pearson, K. J., de Cabo, R., & Bordone, L. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008414 · Cited by 271 · see citing works
Gao, Z., Zuberi, A. R., Quon, M. J., Dong, Z., & Ye, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300423200 · Cited by 257 · see citing works
Self-citationModulation of the JNK Pathway in Liver Affects Insulin Resistance Status
Nakatani, Y., Kaneto, H., Kawamori, D., Hatazaki, M., Miyatsuka, T., Matsuoka, T., Kajimoto, Y., Matsuhisa, M., Yamasaki, Y., & Hori, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406963200 · Cited by 230 · see citing works
Differential effects of JNK1 and JNK2 inhibition on murine steatohepatitis and insulin resistance†
Singh, R., Wang, Y., Xiang, Y., Tanaka, K. E., Gaarde, W. A., & Czaja, M. J. (2008) · Hepatology · doi:10.1002/hep.22578 · Cited by 224 · see citing works
Xu, F. L., Gao, Z., Zhang, J., Rivera, C. A., Yin, J., Weng, J., & Ye, J. (2010) · Endocrinology · doi:10.1210/en.2009-1013 · Cited by 221 · see citing works
Self-citationInvolvement of mammalian sirtuin 1 in the action of ethanol in the liver
You, M., Liang, X., Ajmo, J. M., & Ness, G. C. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00575.2007 · Cited by 214 · see citing works
Erion, D. M., Yonemitsu, S., Nie, Y., Nagai, Y., Gillum, M. P., Hsiao, J. J., Iwasaki, T., Stark, R., Weismann, D., Yu, X. X., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812931106 · Cited by 181 · see citing works
Prevention of Steatosis by Hepatic JNK1
Sabio, G., Cavanagh, J., Ko, H. J., Jung, D. Y., Gray, S., Jun, J. Y., Barrett, T., Mora, A., Kim, J. K., & Davis, R. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.09.007 · Cited by 148 · see citing works
Self-citationGao, Z., He, Q., Peng, B., Chiao, P. J., & Ye, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507784200 · Cited by 141 · see citing works
Self-citationJNK2-dependent regulation of SIRT1 protein stability
Ford, J. R., Ahmed, S. U., Allison, S. J., Jiang, M., & Milner, J. (2008) · Cell Cycle · doi:10.4161/cc.7.19.6799 · Cited by 124 · see citing works
Role of the hypothalamic–pituitary–thyroid axis in metabolic regulation by JNK1Preprint
Sabio, G., Cavanagh, J., Barrett, T., Jung, D. Y., Ko, H. J., Ong, H., Morel, C., Mora, A., Reilly, J., Kim, J. K., et al. (2010) · Genes & Development · doi:10.1101/gad.1878510 · Cited by 117 · see citing works
Self-citationInhibition of transcriptional activity of c-JUN by SIRT1
Gao, Z., & Ye, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.09.079 · Cited by 96 · see citing works
Self-citationYou, M., Cao, Q., Liang, X., Ajmo, J. M., & Ness, G. C. (2008) · Journal of Nutrition · doi:10.1093/jn/138.3.497 · Cited by 91 · see citing works
Yang, J., Kong, X., dos Santos, M. E. S. M., Alemán, G., Chaco, E., Liu, G. E., Wu, S.-Y., Samols, D. R., Hakimi, P., Chiang, C.-M., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047340 · Cited by 77 · see citing works
Gao, Z., Wang, Z., Zhang, X., Butler, A. A., Zuberi, A. R., Gawrońska‐Kozak, B., Lefevre, M., York, D., Ravussin, É., Berthoud, H., et al. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00178.2006 · Cited by 66 · see citing works
Self-citationAguirre, A. A., López, T., López‐Bayghen, E., & Ortega, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002847200 · Cited by 61 · see citing works
Yang, R., Wilcox, D. M., Haasch, D. L., Jung, P. M., Nguyen, P., Voorbach, M. J., Doktor, S. Z., Brodjian, S. J., Bush, E. N., Lin, E. P.-Y., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700790200 · Cited by 61 · see citing works
Flagged first, then by citations
Research works printed but not linked: 4
- Erion, D. M., Yonemitsu, S., Nie, Y., Nagai, Y., Gillum, M. P., Hsiao, J. J., Iwasaki, T., Stark, R., Weismann, D., Yu, X. X., Murray, S. F., Bhanot, S., Monia, B. P., Horvath, T. L., Gao, Q., Samuel, V. T., and Shulman, G. I. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 11288 -11293
- Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., Pistell, P. J., Poosala, S., Becker, K. G., Boss, O., Gwinn, D., Wang, M., Ramaswamy, S., Fishbein, K. W., Spencer, R. G., Lakatta, E. G., Le Couteur, D., Shaw, R. J., Navas, P., Puigserver, P., Ingram, D. K., de Cabo, R., and Sinclair, D. A. (2006) Nature 444, 337-342
- Rodgers, J. T., and Puigserver, P. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 12861-12866
- Nasrin, N., Kaushik, V. K., Fortier, E., Wall, D., Pearson, K. J., de Cabo, R., and Bordone, L. (2009) PLoS One 4, e8414
Cited by
Sorted by citations
Byrne, C. D., & Targher, G. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2014.12.012 · Cited by 3,082 · see citing works
Regulation of SIRT1 and Its Roles in Inflammation
Yang, Y., Liu, Y., Wang, Y., Chao, Y., Zhang, J., Jia, Y., Tie, J., & Hu, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831168 · Cited by 721 · see citing works
Self-citationJNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships
Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 524 · see citing works
Redox regulation of SIRT1 in inflammation and cellular senescence
Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503 · see citing works
Calorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
Crosstalk between Oxidative Stress and SIRT1: Impact on the Aging Process
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14023834 · Cited by 457 · see citing works
Xiong, H., Ni, Z., He, J., Jiang, S.-W., Li, X., He, J., Gong, W., Zheng, L., Chen, S., Li, B., et al. (2017) · Oncogene · doi:10.1038/onc.2016.521 · Cited by 362 · see citing works
Chalkiadaki, A., & Guarente, L. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.003 · Cited by 352 · see citing works
Castro, R. E., Ferreira, D. M. S., Afonso, M. B., Borralho, P. M., Machado, M. V., Cortez‐Pinto, H., & Rodrigues, C. M. P. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.08.008 · Cited by 351 · see citing works
Regulation of SIRT1 in aging: Roles in mitochondrial function and biogenesis
Yuan, Y., Cruzat, V. F., Newsholme, P., Cheng, J., Chen, Y., & Lu, Y. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.02.003 · Cited by 301 · see citing works
Hong, S., Moreno‐Navarrete, J. M., Wei, X., Kikukawa, Y., Tzameli, I., Prasad, D., Lee, Y., Asara, J. M., Fernández‐Real, J. M., Maratos–Flier, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3882 · Cited by 258 · see citing works
Sorting out functions of sirtuins in cancer
Roth, M., & Chen, W. (2013) · Oncogene · doi:10.1038/onc.2013.120 · Cited by 239 · see citing works
New Insights for Oxidative Stress and Diabetes Mellitus
Maiese, K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/875961 · Cited by 227 · see citing works
Sung, K., Jeong, W. S., Wild, S. H., & Byrne, C. D. (2012) · Diabetes Care · doi:10.2337/dc11-1853 · Cited by 217 · see citing works
Sirtuins' modulation of autophagy
Ng, F., & Tang, B. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24399 · Cited by 194 · see citing works
Resolution of Fatty Liver and Risk of Incident Diabetes
Sung, K., Wild, S. H., & Byrne, C. D. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-1519 · Cited by 169 · see citing works
Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation
Wang, M., & Lin, H. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-082520-125411 · Cited by 171 · see citing works
The ways and means that fine tune Sirt1 activity
Revollo, J. R., & Li, X. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.12.004 · Cited by 161 · see citing works
Cellular Stresses and Stress Responses in the Pathogenesis of Insulin Resistance
Onyango, A. N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4321714 · Cited by 160 · see citing works
Shen, B., Zhao, C., Wang, Y., Peng, Y., Cheng, J., Li, Z., Wu, L., Jin, M., & Feng, H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14293 · Cited by 157 · see citing works
Salmonella Typhimurium disrupts Sirt1/AMPK checkpoint control of mTOR to impair autophagy
Ganesan, R., Hos, N. J., Gutiérrez, S., Fischer, J., Stepek, J. M., Daglidu, E., Krönke, M., & Robinson, N. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006227 · Cited by 139 · see citing works
Mechanisms of intrahepatic triglyceride accumulation
Ress, C. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i4.1664 · Cited by 133 · see citing works
García‐Rodríguez, J. L., Barbier‐Torres, L., Fernández-Álvarez, S., Juan, V. G., Monte, M. J., Halilbasic, E., Herranz, D., Álvarez, L., Aspichueta, P., Marı́n, J. J. G., et al. (2013) · Hepatology · doi:10.1002/hep.26971 · Cited by 128 · see citing works
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123 · see citing works
“A recent study also showed that sustained JNK activation led to phosphorylation at Ser-46 of sirtuin 1, NADþ-dependent deacetylase in cytosol (described later), followed by ubiquitin-dependent degradation, contributing to fat accumulation in obese mice [124].”
BackgroundmIGF‐1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart
Vinciguerra, M., Santini, M. P., Martínez, C., Pazienza, V., Claycomb, W. C., Giuliani, A., & Rosenthal, N. A. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00766.x · Cited by 122 · see citing works
O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress
Han, C., Gu, Y., Shan, H., Mi, W., Sun, J., Shi, M., Zhang, X., Lu, X., Han, F., Gong, Q., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01654-6 · Cited by 120 · see citing works
Nin, V., Escande, C., Chini, C. C. S., Giri, S., Camacho-Pereira, J., Matalonga, J., Lou, Z., & Chini, E. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365874 · Cited by 119 · see citing works
Non-alcoholic fatty liver disease: An update with special focus on the role of gut microbiota
Doulberis, M., Kotronis, G., Gialamprinou, D., Kountouras, J., & Katsinelos, P. (2017) · Metabolism · doi:10.1016/j.metabol.2017.03.013 · Cited by 113 · see citing works
Huang, C.-Y., Kuo, W.-W., Yeh, Y.-L., Ho, T.-J., Lin, J.-Y., Dy, L., Chu, C.-H., Tsai, F.-J., Tsai, C.-H., & Huang, C.-Y. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.46 · Cited by 107 · see citing works
Amphetamines promote mitochondrial dysfunction and DNA damage in pulmonary hypertension
Chen, P.-I., Cao, A., Miyagawa, K., Tojais, N. F., Hennigs, J. K., Li, C. G., Sweeney, N. M., Inglis, A. S., Wang, L., Li, D., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.90427 · Cited by 106 · see citing works
WISP1: Clinical Insights for a Proliferative and Restorative Member of the CCN Family
Maiese, K. (2014) · Current Neurovascular Research · doi:10.2174/1567202611666140912115107 · Cited by 103 · see citing works
Neuroprotective effects of dietary restriction: Evidence and mechanisms
Pani, G. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.03.004 · Cited by 103 · see citing works
Moschen, A. R., Wieser, V. E., Gerner, R. R., Bichler, A., Enrich, B., Moser, P. L., Ebenbichler, C. F., Kaser, S., & Tilg, H. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.07.027 · Cited by 103 · see citing works
Kanwal, A., Pillai, V. B., Samant, S. A., Gupta, M., & Gupta, M. P. (2019) · The FASEB Journal · doi:10.1096/fj.201900767r · Cited by 103 · see citing works
Liu, L., Liu, C., Zhang, Q., Shen, J., Zhang, H., Shan, J., Duan, G., Guo, D., Chen, X., Cheng, J., et al. (2016) · Hepatology · doi:10.1002/hep.28690 · Cited by 102 · see citing works
Free radicals and sprint exercise in humans
Morales‐Álamo, D., & Calbet, J. A. L. (2013) · Free Radical Research · doi:10.3109/10715762.2013.825043 · Cited by 88 · see citing works
Targher, G., Marchesini, G., & Byrne, C. D. (2016) · Diabetes & Metabolism · doi:10.1016/j.diabet.2016.04.002 · Cited by 87 · see citing works
SIRT1 phosphorylation by AMP-activated protein kinase regulates p53 acetylation.
Lau, A. W., Liu, P., Inuzuka, H., & Gao, D. (2014) · PubMed Central · Cited by 86 · see citing works
The REGγ Proteasome Regulates Hepatic Lipid Metabolism through Inhibition of Autophagy
Dong, S., Jia, C., Zhang, S., Fan, G., Li, Y., Shan, P., Sun, L., Xiao, W., Li, L., Zheng, Y., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.08.012 · Cited by 85 · see citing works
SIRT1 Regulation in Ageing and Obesity
Pardo, P. S., & Boriek, A. M. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111249 · Cited by 90 · see citing works
Bahl, S., & Seto, E. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03599-4 · Cited by 82 · see citing works
Emerging Roles of SIRT1 in Cancer Drug Resistance
Wang, Z., & Chen, W. (2013) · Genes & Cancer · doi:10.1177/1947601912473826 · Cited by 84 · see citing works
Sarne, Y., Toledano, R., Rachmany, L., Sasson, E., & Doron, R. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.025 · Cited by 81 · see citing works
Morales‐Álamo, D., Ponce‐González, J. G., Guadalupe‐Grau, A., Rodríguez‐García, L., Santana, A., Cussó, M. R., Guerrero, M., Guerra, B., Dorado, C., & Calbet, J. A. L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00415.2012 · Cited by 78 · see citing works
3,5-Diiodo-l-thyronine ameliorates diabetic nephropathy in streptozotocin-induced diabetic rats
Shang, G., Gao, P., Zhao, Z., Chen, Q., Jiang, T., Zhang, N., & Li, H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.01.023 · Cited by 79 · see citing works
Nelson, L. E., Valentine, R. J., Cacicedo, J. M., Gauthier, M., Ido, Y., & Ruderman, N. B. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00296.2011 · Cited by 79 · see citing works
Zeng, Y., Guo, M., Wu, Q., Tan, X., Jiang, C., Teng, F., Chen, J., Zhang, F., Ma, X., Li, X., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.08.018 · Cited by 78 · see citing works
Ginsenoside Rb1 Prevents H2O2-Induced HUVEC Senescence by Stimulating Sirtuin-1 Pathway
Song, Z., Liu, Y., Hao, B., Yu, S., Zhang, H., Liu, D., Zhou, B., Wu, L., Wang, M., Xiong, Z., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112699 · Cited by 76 · see citing works
Role of Sirtuins in Regulating Pathophysiology of the Heart
Bindu, S., Pillai, V. B., & Gupta, M. P. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.04.015 · Cited by 73 · see citing works
Ham, M., Choe, S. S., Shin, K. C., Choi, G., Kim, J., Noh, J., Kim, Y., Ryu, J.-W., Yoon, K., Lee, C., et al. (2016) · Diabetes · doi:10.2337/db16-0060 · Cited by 73 · see citing works
AMPK signaling in skeletal muscle during exercise: Role of reactive oxygen and nitrogen species
Morales-Alamo, D., & Calbet, J. A. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.012 · Cited by 72 · see citing works
Xie, X., Cao, Y., Dai, L., & Zhou, D. (2023) · Molecular Medicine · doi:10.1186/s10020-022-00595-1 · Cited by 71 · see citing works
Ferreira, D. M. S., Afonso, M. B., Rodrigues, P. M., Simão, A. L., Pereira, D. M., Borralho, P. M., Rodrigues, C. M. P., & Castro, R. E. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00420-13 · Cited by 70 · see citing works
Panes-Fernández, J., Godoy, P. A., Silva-Grecchi, T., Celis, M. T., Ramírez-Molina, O., Gavilán, J., Muñoz-Montesino, C., Castro, P. A., Moraga‐Cid, G., Yévenes, G. E., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00709 · Cited by 71 · see citing works
Huang, K., Chen, C., Hao, J., Huang, J., Liu, P., & Huang, H. (2014) · Endocrinology · doi:10.1210/en.2014-1381 · Cited by 69 · see citing works
Kang, H., & Kim, B. (2023) · Foods · doi:10.3390/foods12050925 · Cited by 71 · see citing works
Zou, Z., Liu, B., Zeng, L., Yang, X., Huang, R., Wu, C., Zhu, H., Gao, Y., Yuan, D., & Yu, J. (2019) · Mediators of Inflammation · doi:10.1155/2019/7854389 · Cited by 66 · see citing works
Genealogy of an ancient protein family: the Sirtuins, a family of disordered members
Costantini, S., Sharma, A., Raucci, R., Costantini, M., Autiero, I., & Colonna, G. (2013) · BMC Evolutionary Biology · doi:10.1186/1471-2148-13-60 · Cited by 66 · see citing works
Peng, L., Yuan, Z., Li, Y., Ling, H., Izumi, V., Fang, B., Fukasawa, K., Koomen, J. M., Chen, J., & Seto, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612796 · Cited by 65 · see citing works
A Redox-resistant Sirtuin-1 Mutant Protects against Hepatic Metabolic and Oxidant Stress
Shao, D., Fry, J., Han, J., Hou, X., Pimentel, D. R., Matsui, R., Cohen, R. A., & Bachschmid, M. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520403 · Cited by 66 · see citing works
SIRT1 and stem cells: In the forefront with cardiovascular disease, neurodegeneration and cancer
Maiese, K. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i2.235 · Cited by 66 · see citing works
Zhao, X., Liu, Y., Zhu, G., Liang, Y.-Y., Liu, B., Wu, Y., Han, M., Sun, W., Han, Y. K., Chen, G., et al. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.07.363 · Cited by 63 · see citing works
CERKL regulates autophagy via the NAD-dependent deacetylase SIRT1
Hu, X., Lu, Z., Yu, S., Reilly, J., Liu, F., Jia, D., Qin, Y., Han, S., Liu, X., Qu, Z., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1520548 · Cited by 63 · see citing works
Armour, S. M., Bennett, E. J., Braun, C. R., Zhang, X., McMahon, S. B., Gygi, S. P., Harper, J. W., & Sinclair, D. A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00971-12 · Cited by 62 · see citing works
SIRT1 in the Development and Treatment of Hepatocellular Carcinoma
Farcas, M. F., Andrei-Alexandru, G., Gulei, D., Ionescu, C., Irimie, A., Cătană, C.-S., & Berindan‐Neagoe, I. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00148 · Cited by 60 · see citing works
Li, Z., Bridges, B., Olson, J. C., & Weinman, S. A. (2016) · Oncogene · doi:10.1038/onc.2016.359 · Cited by 59 · see citing works
Kim, T. H., Yang, Y. M., Han, C. Y., Koo, J. H., Oh, H., Kim, S. S., You, B. H., Choi, Y. H., Park, T., Lee, C. H., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci97831 · Cited by 59 · see citing works
Wang, S., Zhong Chong, Z., Chen Shang, Y., & Maiese, K. (2013) · Current Neurovascular Research · doi:10.2174/156720213804805945 · Cited by 58 · see citing works
Repositioning antipsychotic chlorpromazine for treating colorectal cancer by inhibiting sirtuin 1
Lee, W., Lee, W.-T., Cheng, C., Chen, K., Chou, C., Chung, C., Sun, M.-S., Cheng, H., Ho, M.-N., & Lin, C. (2015) · Oncotarget · doi:10.18632/oncotarget.4768 · Cited by 58 · see citing works
Regeneration in the nervous system with erythropoietin
Maiese, K. (2015) · Frontiers in bioscience · doi:10.2741/4408 · Cited by 55 · see citing works
Tong, X., Zhang, D., Arthurs, B., Li, P., Durudogan, L., Gupta, N., & Yin, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130047 · Cited by 54 · see citing works
Fusco, S., Maulucci, G., & Pani, G. (2012) · Cell Cycle · doi:10.4161/cc.22074 · Cited by 54 · see citing works
Yang, H., Yan, B., Liao, D., Huang, S., & Qiu, Y. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.106 · Cited by 52 · see citing works
RelB acts as a molecular switch driving chronic inflammation in glioblastoma multiforme
Waters, M. R., Gupta, A. S., Mockenhaupt, K., Brown, L. N., Biswas, D. D., & Kordula, T. (2019) · Oncogenesis · doi:10.1038/s41389-019-0146-y · Cited by 52 · see citing works
Waller-Evans, H., Hue, C., Fearnside, J. F., Rothwell, A. R., Lockstone, H., Calderari, S., Wilder, S. P., Cazier, J., Scott, J., & Gauguier, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082825 · Cited by 46 · see citing works
Chattopadhyay, T., Maniyadath, B., Bagul, H. P., Chakraborty, A., Shukla, N., Budnar, S., Rajendran, A., Shukla, A., Kamat, S. S., & Kolthur‐Seetharam, U. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909943117 · Cited by 50 · see citing works
Yang, F., Wang, X., Yang, D., Lu, Y., Wei, G., Yu, W., Liu, X., Zheng, Q., Ying, J., & Hua, F. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.738686 · Cited by 50 · see citing works
Proteasome‐mediated proteostasis: Novel medicinal and pharmacological strategies for diseases
Mishra, R., Upadhyay, A., Prajapati, V. K., & Mishra, A. (2018) · Medicinal Research Reviews · doi:10.1002/med.21502 · Cited by 50 · see citing works
Zhao, X., Wu, Y., Li, J., Li, D., Yang, J., Zhu, P., Liu, Y., Zhuang, Y., Yu, S., Cao, W., et al. (2019) · Toxicology · doi:10.1016/j.tox.2019.05.003 · Cited by 50 · see citing works
Song, B., Akbar, M. D., Jo, I., Hardwick, J. P., & Abdelmegeed, M. A. (2015) · Advances in pharmacology · doi:10.1016/bs.apha.2015.04.002 · Cited by 49 · see citing works
Liu, L., Yasen, M., Tang, D., Ye, J., Aisa, H. A., & Xin, X. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.01.143 · Cited by 48 · see citing works
Self-citationNon-Alcoholic Steatohepatitis and Hepatocellular Carcinoma: Implications for Lycopene Intervention
Ip, B. C., & Wang, X. (2013) · Nutrients · doi:10.3390/nu6010124 · Cited by 47 · see citing works
Reverting p53 activation after recovery of cellular stress to resume with cell cycle progression
Lazo, P. A. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.005 · Cited by 46 · see citing works
Inhibition of ATG3 ameliorates liver steatosis by increasing mitochondrial function
Lima, N. D. S., Fondevila, M. F., Nóvoa, E., Buqué, X., Mercado-Gómez, M., Gallet, S., Gonzalez-Rellan, M. J., Fernandez, U., Loyens, A., García-Vence, M., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.09.008 · Cited by 46 · see citing works
Senthil, K. K. J., Gokila, V. M., Mau, J., Lin, C.-C., Chu, F., Wei, C., Liao, V. H., & Wang, S. (2016) · Oncotarget · doi:10.18632/oncotarget.11229 · Cited by 46 · see citing works
Choi, S., Kwon, S., Seok, S., Xiao, Z., Lee, K. W., KANG, Y. Y., Li, X., Shinoda, K., Kajimura, S., KEMPER, B. W., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00006-17 · Cited by 46 · see citing works
Harnessing the Power of SIRT1 and Non-coding RNAs in Vascular Disease
Maiese, K. (2016) · Current Neurovascular Research · doi:10.2174/1567202613666161129112822 · Cited by 44 · see citing works
Elumalai, S., Karunakaran, U., Moon, J. S., & Won, K. C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.030 · Cited by 44 · see citing works
Programming Apoptosis and Autophagy with Novel Approaches for Diabetes Mellitus
Maiese, K. (2015) · Current Neurovascular Research · doi:10.2174/1567202612666150305110929 · Cited by 43 · see citing works
Lee, I. C. J., Ho, X. Y., George, S. E., Goh, C. W., Sundaram, J. R., Pang, K. K. L., Luo, W., Yusoff, P., Sze, N. S. K., & Shenolikar, S. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.152 · Cited by 43 · see citing works
Cordeiro, A., Souza, L. L., Oliveira, L. S. D., Faustino, L. C., Santiago, L. A., Bloise, F. F., Ortiga-Carvalho, T. M., Almeida, N. A. D. S., & Pazos-Moura, C. C. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0420 · Cited by 43 · see citing works
HDAC 4 stabilizes SIRT 1 via sumoylation SIRT 1 to delay cellular senescence
Han, X., Niu, J., Zhao, Y., Kong, Q., Tong, T., & Han, L. (2015) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12496 · Cited by 42 · see citing works
Evaluation of Sirtuin Role in Neuroprotection of Retinal Ganglion Cells in Hypoxia
Balaiya, S., Ferguson, L. R., & Chalam, K. V. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-9259 · Cited by 41 · see citing works
JAK1-mediated Sirt1 phosphorylation functions as a negative feedback of the JAK1-STAT3 pathway
Wang, W., Li, F. R., Xu, Y., Wei, J., Zhang, Y., Yang, H., Gao, B., Yu, G., & Fang, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001387 · Cited by 41 · see citing works
Developmental Programming of Pediatric Non-Alcoholic Fatty Liver Disease: Redefining the ‘First-Hit’
Stewart, M. S., Heerwagen, M. J. R., & Friedman, J. (2013) · Clinical obstetrics and gynecology · doi:10.1097/grf.0b013e3182a09760 · Cited by 47 · see citing works
Yin, Z., Geng, X., Zhang, Z., Wang, Y., & Gao, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.746711 · Cited by 40 · see citing works
Metformin and insulin-resistant related diseases: Emphasis on the role of microRNAs
Alimoradi, N., Firouzabadi, N., & Fatehi, R. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111662 · Cited by 38 · see citing works
Endothelial SIRT1 as a Target for the Prevention of Arterial Aging: Promises and Challenges
Begum, M. K., Konja, D., Singh, S., Chłopicki, S., & Wang, Y. (2021) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001154 · Cited by 40 · see citing works
Zhao, P., & Malik, S. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00821-7 · Cited by 37 · see citing works
Deng, Y., Pan, M., Nie, H., Zheng, C., Tang, K., Zhang, Y., & Yang, Q. (2019) · Molecules · doi:10.3390/molecules24213943 · Cited by 36 · see citing works
- Authors
- Gao, Z., Zhang, J., Kheterpal, I., Kennedy, N., Davis, R. J., & Ye, J.
- Affiliations
- Pennington Biomedical Research Center (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Ye, Jianping
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-06
- Volume
- 286
- Issue
- 25
- Pages
- 22227-22234
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3121368
- OpenAlex
- W2001428385
- Cited by
- 187
- References
- 46
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 7 · 2023: 5 · 2022: 6 · 2021: 15 · 2020: 12 · 2019: 15 · 2018: 16 · 2017: 16 · 2016: 17 · 2015: 20 · 2014: 13 · 2013: 21 · 2012: 13
- FWCI
- 7.31
- 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)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- National Institutes of Health (DK085495)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-085495, R56DK068036, R01DK085495, R01DK068036, DK068036, P30DK072476)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Epidemiology › Liver Disease Diagnosis and Treatment
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Keywords
- SIRT1, JNK1, JNK2, protein degradation, ubiquitination, proteasome, hepatic steatosis, obesity, hepatocytes
- MeSH terms
- Animals, Cell Line, Dietary Fats, Enzyme Activation, Fatty Liver, Histone Deacetylases, Humans, Male, Mice, Inbred C57BL, Obesity, Phosphorylation, Mitogen-Activated Protein Kinase 8, Mice, Rats, Ubiquitination, Gene Knockout Techniques, Sirtuin 1
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