The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Open accessAbstract
In lower organisms, increased expression of the NAD-dependent deacetylase Sir2 augments lifespan. The mechanism through which this life extension is mediated remains incompletely understood. Here we have examined the cellular effects of overexpression of SIRT1, the closest mammalian ortholog of Sir2. In PC12 cells, increased expression of the NAD-dependent deacetylase SIRT1 reduces cellular oxygen consumption by approximately 25%. We further demonstrate that SIRT1 expression can alter the transcriptional activity of the mitochondrial biogenesis coactivator PGC-1alpha. In addition, SIRT1 and PGC-1alpha directly interact and can be co-immunoprecipitated as a molecular complex. A single amino acid mutation in the putative ADP-ribosyltransferase domain of SIRT1 inhibits the interaction of SIRT1 with PGC-1alpha but does not effect the interaction of SIRT1 with either p53 or Foxo3a. We further show that PGC-1alpha is acetylated in vivo. This acetylation is augmented by treatment with the SIRT1 inhibitor nicotinamide or by expression of the transcriptional coactivator p300. Finally we demonstrate that SIRT1 catalyzes PGC-1alpha deacetylation both in vitro and in vivo. These results provide a direct link between the sirtuins, a family of proteins linked to lifespan determination and PGC-1alpha, a coactivator that regulates cellular metabolism.
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In the citing paper
“SIRT-1 is a key regulatory factor in muscle metabolism.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [51]
In the citing paper
“In apparent contrast with its role in promoting mitochondrial biogenesis through peroxisome proliferator-activated receptor-γ co-activator 1α deacetylation19–21, SIRT1 has also been implicated in turnover of defective mitochondria by mitophagy22,23.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [20]
In the citing paper
“The interaction between PGC-1α and SIRT1 also suggests a role for SIRT1 in exercise-induced mitochondrial biogenesis [89].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [89]
In the citing paper
“Activity of PGC-1α is regulated through inhibitory acetylation by GCN5 [59] and stimulatory deacetlyation by SIRT1 [60-62].”
From PGC-1α in aging and anti-aging interventions (2009) · cites this paper as [60]
In the citing paper
“AMPK and SIRT1, two major metabolic sensors in cells, modulate directly PGC1α activity through phosphorylation and deacetylation respectively”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Nemoto et al., 2005
In the citing paper
“AMPK and SIRT1, the two mainmajor metabolic sensors in cells, modulate directly are direct modulators of PGC1α activity through phosphorylation and deacetylation respectively (Jager et al., 2007; Nemoto et al., 2005).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Nemoto et al., 2005
Citations
Cites
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413
Self-citationWu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
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
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
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076
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
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Wang, C., Tian, L., Popov, V. M., & Pestell, R. G. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.003 · Cited by 71
Khalek, W. A., Cortade, F., Ollendorff, V., Lapasset, L., Tintignac, L. A. J., Chabi, B., & Wrutniak‐Cabello, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114388 · Cited by 69
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Ren, R., Wang, Z., Wu, M., & Wang, H. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.49535 · Cited by 67
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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
SirT1 in muscle physiology and disease: lessons from mouse models
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McBurney, M. W., Clark-Knowles, K. V., Caron, A. Z., & Gray, D. A. (2013) · Genes & Cancer · doi:10.1177/1947601912474893 · Cited by 69
The role of SIRT3 in mitochondrial homeostasis and cardiac adaptation to hypertrophy and aging
Sack, M. N. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.11.004 · Cited by 66
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Chabi, B., Adhihetty, P. J., O′Leary, M. F. N., Menzies, K. J., & Hood, D. A. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91451.2008 · Cited by 64
Role of sirtuins in ischemia-reperfusion injury
Pantazi, E. D. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i43.7594 · Cited by 68
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Mantel, C., & Broxmeyer, H. E. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3283043819 · Cited by 65
Pearen, M. A., Goode, J. M., Fitzsimmons, R. L., Eriksson, N. A., Thomas, G. P., Cowin, G., Wang, S.-C., Tuong, Z. K., & Muscat, G. E. O. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1205 · Cited by 63
Warren, J. S., Oka, S., Zablocki, D., & Sadoshima, J. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00103.2017 · Cited by 64
Zullo, A., Simone, E., Grimaldi, M., Musto, V., & Mancini, F. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040928 · Cited by 67
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Ma, J.-M., Yin, G., Lu, Z., Xie, P., Zhou, H., Liu, J., & Yu, L. (2018) · Phytotherapy Research · doi:10.1002/ptr.6108 · Cited by 63
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Yang, C., Yang, W., He, Z., Guo, J., Yang, X., Wang, R., & Li, H. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.624402 · Cited by 63
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Yeo, D., Kang, C., & Ji, L. L. (2020) · GeroScience · doi:10.1007/s11357-020-00171-7 · Cited by 63
Szekeres, Z., Nagy, A., Jahner, K., & Szabados, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158214 · Cited by 67
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Thomas, B., & Beal, M. F. (2010) · Movement Disorders · doi:10.1002/mds.22781 · Cited by 62
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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 64
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Tan, M., Tang, C., Zhang, Y., Cheng, Y., Cai, L., Chen, X., Gao, Y., Deng, Y., & Pan, M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1016020 · Cited by 61
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Liu, S., Li, D., Zeng, H.-Y., Kan, L.-Y., Zou, W., Zhang, P., Gu, H., & Tang, X. (2017) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyx030 · Cited by 58
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Li, M., Ding, J., Tang, Q., Hao, M., Wang, B., Wu, J., Yu, L., Jiao, M., Luo, B., Xie, M., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.12.017 · Cited by 57
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Forini, F., Nicolini, G., & Iervasi, G. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16036312 · Cited by 57
Wen, F., An, C., Wu, X., Yang, Y., Xu, J., Liu, Y., Wang, C., Nie, L., Fang, H., & Yang, Z. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.11.008 · Cited by 57
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Marton, O., Koltai, E., Takeda, M., Koch, L. G., Britton, S. L., Davies, K. J. A., Boldogh, I. R., & Radak, Z. O. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1554-7 · Cited by 53
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McMeekin, L. J., Fox, S. N., Boas, S. M., & Cowell, R. M. (2021) · Cells · doi:10.3390/cells10020352 · Cited by 53
Maynard, S., Hall, A., Galanos, P., Rizza, S., Yamamoto, T., Gram, H. H., Munk, S. H. N., Shoaib, M., Sørensen, C. S., Bohr, V. A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac741 · Cited by 56
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Choupani, J., Derakhshan, S. M., Bayat, S., Alivand, M. R., & Khaniani, M. S. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26302 · Cited by 47
Zhang, T., Du, X., Zhao, L., He, M., Lin, L., Guo, C., Zhang, X., Han, J., Yan, H., Huang, K., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900782r · Cited by 51
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Ji, L. L., Yeo, D., Kang, C., & Zhang, T. (2020) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2020.01.001 · Cited by 51
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Huhtiniemi, T., Wittekindt, C., Laitinen, T., Leppänen, J., Salminen, A., Poso, A., & Lahtela-Kakkonen, M. K. (2006) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-006-9084-9 · Cited by 52
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Barhwal, K. K., Das, S. K., Kumar, A., Hota, S. K., & Srivastava, R. B. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13225 · Cited by 50
RetractedBecerril, S., Rodrı́guez, A., Catalán, V., Sáinź, N., Ramírez, B., Collantes, M., Peñuelas, I., Gómez‐Ambrosi, J., & Frühbeck, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010962 · Cited by 50
Puthanveetil, P., Wang, Y., Zhang, D., Wang, F., Kim, M. S., Innis, S. M., Pulinilkunnil, T., Abrahani, A., & Rodrigues, B. B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.009 · Cited by 50
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Metadata
- Authors
- Nemoto, S., Fergusson, M. M., & Finkel, T.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Finkel, Toren
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 280
- Issue
- 16
- Pages
- 16456-16460
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2058768220
- Cited by
- 1,047
- References
- 35
- Citations by year
- 2026: 29 · 2025: 28 · 2024: 41 · 2023: 35 · 2022: 48 · 2021: 54 · 2020: 62 · 2019: 55 · 2018: 49 · 2017: 61 · 2016: 59 · 2015: 62 · 2014: 67 · 2013: 73 · 2012: 59
- FWCI
- 17.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- SIRT1, PGC-1α, Sir2, NAD+-dependent deacetylase, ADP-ribosyltransferase, protein-protein interaction, mitochondrial biogenesis, oxygen consumption, cellular metabolism, lifespan extension, nicotinamide, P300, p53, FOXO3, sirtuins
- MeSH terms
- Forkhead Box Protein O1, Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Acetylation, Animals, DNA-Binding Proteins, HeLa Cells, Humans, NAD, Nerve Tissue Proteins, Niacinamide, Nuclear Proteins, Oxygen Consumption, Transcription Factors, Trans-Activators, Tumor Suppressor Protein p53, RNA-Binding Proteins, PC12 Cells, Sirtuins, E1A-Associated p300 Protein, Rats, Forkhead Transcription Factors, Sirtuin 1
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