Calorie restriction alters mitochondrial protein acetylation
Open accessAbstract
Summary: Calorie restriction (CR) increases lifespan in organisms ranging from budding yeast through mammals. Mitochondrial adaptation represents a key component of the response to CR. Molecular mechanisms underlying this adaptation are largely unknown. Here we show that lysine acetylation of mitochondrial proteins is altered during CR in a tissue‐specific fashion. Via large‐scale mass spectrometry screening, we identify 72 candidate proteins involved in a variety of metabolic pathways with altered acetylation during CR. Mitochondrial acetylation changes may play an important role in the pro‐longevity CR response.
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Calorie restriction does not change brain mitochondrial acetylation and decreases skeletal muscle acetylation.
“Metabolic supplier organs such as the liver and kidney demonstrate mitochondrial hyperacetylation under CR, as does the heart (Schwer et al. 2009); brain mitochondrial acetylation was unchanged, however, and skeletal muscle acetylation decreased.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Schwer et al. 2009
Calorie restriction causes mitochondrial hyperacetylation in liver, kidney, and heart.
“Metabolic supplier organs such as the liver and kidney demonstrate mitochondrial hyperacetylation under CR, as does the heart (Schwer et al. 2009); brain mitochondrial acetylation was unchanged, however, and skeletal muscle acetylation decreased.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Schwer et al. 2009
Caloric restriction enhances mitochondrial protein acetylation in diverse tissues, such as liver, heart, and kidney.
“Intriguingly, CR enhances mitochondrial protein acetylation in diverse tissues, such as liver, heart, and kidney (Schwer et al, 2009).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Schwer et al, 2009
Mitochondrial protein acetylation increases upon fasting and caloric restriction in mice.
“Additionally, acetylation is regulated by perturbation of energy metabolism as demonstrated by an increase in mitochondrial protein acetylation upon fasting (Kim et al., 2006) and caloric restriction (Schwer et al., 2009) in mice.”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Schwer et al., 2009
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“In mammals, acute fasting and chronic ethanol ingestion also alter hepatic mitochondrial protein acetylation (Kim et al., 2006; Picklo, 2008), suggesting that changes in acetylation represents an ancient, evolutionarily conserved mechanism for adaptation to metabolic ⁄ nutritional stress.”
BackgroundMammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
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Background
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SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
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“Furthermore, a growing body of mass spectrometry data demonstrates that numerous mitochondrial proteins involved in metabolism and stress are acetylated [35-37], hinting that sirtuins might regulate a broad range of mitochondrial biology, including energy production, signaling, and apoptosis.”
BackgroundCalorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
“…or SIRT3 expression on a subset of potential protein substrates (Fritz et al., 2012; Hirschey et al., 2010; Kendrick et al., 2011; Law et al., 2009; Schwer et al., 2009; Someya et al., 2010); however, to understand the diverse mechanisms of reversible acetylation that modulate mitochondrial…”
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“, 2006), and protein acetylation is increased as described in previous CR studies (Schwer et al., 2009).”
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“(Schwer et al., 2009), the global pattern of lysine acetylation and deacetylation in liver lysates was refractory to CR-mediated protein deacetylation (Figure 4D, Figure S3B), as evidenced by the fact that the ratio of acetylated to total p53 was significantly increased with CR (Figure 4D, Figure S3B).”
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“Under caloric restriction or fasting, SIRT3 mRNA and protein levels are dramatically increased inmice (2, 39, 40).”
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“Interestingly, four of the eleven proteins that make up complex III have been demonstrated to be acetylated (Schwer et al., 2009).”
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BackgroundFatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
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“CR-mediated induction of SIRT3 in BAT could facilitate SDHA deacetylation and activation.”
BackgroundInfluentialRegulation of intermediary metabolism by protein acetylation
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“Of the nearly 2,200 acetylated proteins identified by acetylation proteomic studies in mammalian cells[10-12,15], metabolic enzymes represent a significant portion of acetylated proteins, due in large part to the use of liver tissues in two of the studies.”
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Protein acetylation in metabolism – metabolites and cofactors
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“Metabolic supplier organs such as the liver and kidney demonstrate mitochondrial hyperacetylation under CR, as does the heart (Schwer et al. 2009); brain mitochondrial acetylation was unchanged, however, and skeletal muscle acetylation decreased.”
BackgroundSIRT3 regulation of mitochondrial oxidative stress
Bause, A. S., & Haigis, M. C. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.007 · Cited by 311 · see citing works
Mechanisms and Dynamics of Protein Acetylation in Mitochondria
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“coli [22–24,38,46–49,59–78].”
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“A large proportion of the mitochondrial proteins are regulated by reversible acetylation and deacetylation, and the level of acetylation is sensitive to metabolic states and dietary conditions such as high-fat diet,75 fasting76 and CR.77 Three sirtuins, Sirt3, Sirt4 and Sirt5, are located in mammalian mitochondria.78…”
BackgroundSirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation
Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283 · see citing works
Sirtuins: guardians of mammalian healthspan
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Self-citationThe sirtuins, oxidative stress and aging: an emerging link
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“It is noteworthy that during caloric restriction, global mitochondrial protein acetylation increases in metabolically active tissue such as liver [51].”
BackgroundMitochondrial sirtuins: regulators of protein acylation and metabolism
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works
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SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
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SENP1-Sirt3 Signaling Controls Mitochondrial Protein Acetylation and Metabolism
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Self-citationMitochondrial protein acetylation regulates metabolism
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“Mice fed a calorierestricted diet also show increases in mitochondrial protein acetylation [28], similar to the acetylation patterns observed during fasting.”
BackgroundMethodProtein acylation: mechanisms, biological functions and therapeutic targets
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“Mitochondrial adaptation is also crucial for the response to calorie restriction.(318) In calorie-restricted mice, dramatic changes in acetylation were observed in liver mitochondria, with the majority changes of acetylation increasing.”
BackgroundSoftic, S., Meyer, J. G., Wang, G.-X., Gupta, M. K., Batista, T. M., Lauritzen, H. P. M. M., Fujisaka, S., Serra, D., Herrero, L., Willoughby, J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.003 · Cited by 227 · see citing works
“HADHA is known to be hyperacetylated by caloric restriction (Schwer et al., 2009), a condition that increases FAO.”
BackgroundMitochondrial Metabolism, Sirtuins, and AgingPreprint
Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 237 · see citing works
“2006), caloric restriction (Schwer et al. 2009), and caloric excess (Hirschey et al.”
BackgroundThe sirtuin family’s role in aging and age-associated pathologies
Hall, J. A., Dominy, J. E., Lee, Y., & Puigserver, P. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64094 · Cited by 235 · see citing works
“In contrast to SIRT3, hepatic SIRT4 expression declines slightly during CR and increases in genetic models of diabetes (9, 55, 67).”
BackgroundHuang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231 · see citing works
Acyl-coenzyme A synthetases in metabolic control
Ellis, J. M., Frahm, J. L., Li, L. O., & Coleman, R. (2010) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32833884bb · Cited by 228 · see citing works
Dichloroacetate and cancer: New home for an orphan drug?
Kankotia, S., & Stacpoole, P. W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.08.005 · Cited by 212 · see citing works
Chowdhury, S. R., Smith, D. R., Saleh, A. J., Schapansky, J., Marquez, A. M., Gomes, S., Akude, E., Morrow, D., Calcutt, N. A., & Fernyhough, P. (2012) · Brain · doi:10.1093/brain/aws097 · Cited by 215 · see citing works
“Therefore, enhanced sorbitol oxidation within the DRG could lead to a diminished NAD +/NADH ratio, as measured in nerve (Obrosova et al., 1999; Stevens et al., 2000), lowering available NAD + levels resulting in reduced SIRT1 or SIRT3 activity (Guarente, 2006; Schwer et al., 2009).”
BackgroundNewman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 207 · see citing works
“Intriguingly and unlike SIRT3, SIRT4 expression is reduced during calorie restriction and is increased in mouse models of diabetes (72, 80).”
BackgroundZhou, X., Chen, M., Zeng, X., Yang, J., Deng, H., Yi, L., & Mt, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.530 · Cited by 208 · see citing works
“A similar positive effect on the ATP/ROS ratio was detected in adult flies, in which mitochondrial uncoupling in neurons was increased, and the life span extended.(37) Interventions that maintain a beneficial mitochondrial ATP/ROS ratio could provide therapeutic opportunities for extending healthy life span and preven…”
BackgroundSirtuins, Aging, and MetabolismPreprint
Guarente, L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010629 · Cited by 205 · see citing works
VDAC1: from structure to cancer therapy
Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 193 · see citing works
“Among the other post-translation modifications VDAC1 undergoes are phosphorylation of serine, threonine, and tyrosine residues (Distler et al., 2007; Kerner et al., 2012) and acetylation of lysines (Kim et al., 2006; Schwer et al., 2009; Zhao et al., 2010; Yang et al., 2011).”
BackgroundHentchel, K. L., & Escalante‐Semerena, J. C. (2015) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00020-15 · Cited by 190 · see citing works
NAMPT-Mediated NAD+ Biosynthesis Is Essential for Vision In Mice
Lin, J. B., Kubota, S., Ban, N., Yoshida, M., Santeford, A. C., Sène, A., Nakamura, R. E. I., Zapata, N., Kubota, M., Tsubota, K., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.073 · Cited by 185 · see citing works
“These findings strongly suggest that SIRT3 and SIRT5 are not redundant, even though they may regulate the acylation status of the same mitochondrial proteins and even the same lysine residues within the same proteins (Hebert et al., 2013; Park et al., 2013; Rardin et al., 2013a, 2013b; Schwer et al., 2009; Sol et al.,…”
InfluentialSIRT3 regulates mitochondrial protein acetylation and intermediary metabolism
Hirschey, M. D., Shimazu, T., Huang, J. Y., Schwer, B., & Verdin, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010850 · Cited by 180 · see citing works
“Changes in metabolic status, including CR (Schwer et al. 2009) and HFD feeding (Hirschey et al. 2011), lead to changes in mitochondria protein acetylation.”
BackgroundInfluentialSelf-citationThe effects of dietary restriction on oxidative stress in rodents
Walsh, M. E., Shi, Y., & Van Remmen, H. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.037 · Cited by 181 · see citing works
“Consistent with this notion, isocitrate dehydrogenase 2, a generator of the redox-required NADPH, is deacetylated by Sirt3 in the mitochondria in response to dietary restriction [27], and DR is known to alter acetylation of mitochondrial proteins [142, 143].”
The role of mitochondrial sirtuins in health and disease
Osborne, B., Bentley, N. L., Montgomery, M. K., & Turner, N. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.197 · Cited by 179 · see citing works
Vassilopoulos, A., Pennington, J. D., Andresson, T., Rees, D. M., Bosley, A. D., Fearnley, I. M., Ham, A., Flynn, C. R., Hill, S., Rose, K. L., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5420 · Cited by 173 · see citing works
“In addition, large-scale mass spectrometry screening pre- and postcaloric restriction identified reversible acetyl-lysines in 72 mitochondrial proteins from a wide variety of metabolic pathways (23).”
Site-Specific Reactivity of Nonenzymatic Lysine Acetylation
Baeza, J., Smallegan, M. J., & Denu, J. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500848p · Cited by 169 · see citing works
Acetylation of Mitochondrial Proteins in the Heart: The Role of SIRT3
Parodi‐Rullán, R. M., Chapa‐Dubocq, X. R., & Javadov, S. A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01094 · Cited by 168 · see citing works
Comprehensive lysine acetylomes emerging from bacteria to humans
Kim, G.-W., & Yang, X. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.10.001 · Cited by 165 · see citing works
Sirtuins and their Biological Relevance in Aging and Age-Related Diseases
Zhao, L., Cao, J., Hu, K., He, X., Dou, Y., Tong, T., & Han, L. (2020) · Aging and Disease · doi:10.14336/ad.2019.0820 · Cited by 174 · see citing works
“In contrast to sirt3, hepatic sirt4 expression declines slightly during caloric restriction (CR) and increases in genetic models of diabetes [34, 131, 132].”
BackgroundMitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation
Pougovkina, O., Brinke, H. T., Ofman, R., van Cruchten, A. G., Kulik, W., Wanders, R. J. A., Houten, S. M., & de Boer, V. C. J. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu059 · Cited by 161 · see citing works
Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer
Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 158 · see citing works
“SIRT3 is expressed abundantly in tissues with high oxidative capacity, such as liver, brain, kidney, skeletal muscle, and brown adipose tissue, and its expression is increased by CR, fasting, or exercise (58, 111, 139, 143).”
Self-citationAnalysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions
Weinert, B. T., Moustafa, T., Iešmantavičius, V., Zechner, R., & Choudhary, C. (2015) · The EMBO Journal · doi:10.15252/embj.201591271 · Cited by 150 · see citing works
“Interestingly, while calorie restriction and fasting cause a similar global increase in mitochondrial acetylation in liver tissue (Schwer et al , 2009; Hebert et al , 2013; Pougovkina et al , 2014), acetylation at SIRT3-targeted sites remains mostly unchanged in calorie-restricted wild-type animals…”
Circadian acetylome reveals regulation of mitochondrial metabolic pathways
Masri, S., Patel, V. R., Eckel‐Mahan, K. L., Peleg, S., Forné, I., Ladurner, A. G., Baldi, P., Imhof, A., & Sassone‐Corsi, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217632110 · Cited by 149 · see citing works
“used mouse liver for an acetylome analysis in response to calorie restriction and identified 348 unique acetylated proteins, of which 165 are mitochondrial (43).”
BackgroundMitochondrial response to nutrient availability and its role in metabolic disease
Gao, A. W., Cantó, C., & Houtkooper, R. H. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201303782 · Cited by 148 · see citing works
“Intriguingly, CR enhances mitochondrial protein acetylation in diverse tissues, such as liver, heart, and kidney (Schwer et al , 2009).”
Castaño‐Cerezo, S., Bernal, V., Post, H., Fuhrer, T., Cappadona, S., Sánchez‐Díaz, N. C., Sauer, U., Heck, A. J. R., Altelaar, M. A. F., & Cánovas, M. (2014) · Molecular Systems Biology · doi:10.15252/msb.20145227 · Cited by 146 · see citing works
“…and in the environmental signals to which they respond, there are increasing evidences that many proteins are either chemically or autocatalyti-cally acetylated (Ramponi et al , 1975; Barak et al , 2004; Schwer et al , 2009; Kuo & Andrews, 2013; Weinert et al , 2013a,b, 2014; Kuhn et al , 2014).”
Sirtuins and Insulin Resistance
Zhou, S., Tang, X., & Chen, H. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00748 · Cited by 143 · see citing works
“In contrast to the other two mitochondrial Sirtuins, SIRT5 protein levels do not change during CR (121, 207).”
BackgroundAcetylation Goes Global: The Emergence of Acetylation Biology
Norris, K. L., Lee, J., & Yao, T. (2009) · Science Signaling · doi:10.1126/scisignal.297pe76 · Cited by 139 · see citing works
“determined changes in liver acetylation events in response to calorie restriction (CR), a regimen that extends life span (32).”
BackgroundCardiac metabolism in HFpEF: from fuel to signalling
Capone, F., Sotomayor-Flores, C., Bode, D., Wang, R., Rodolico, D., Strocchi, S., & Schiattarella, G. G. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac166 · Cited by 141 · see citing works
Buler, M., Aatsinki, S., Izzi, V., Uusimaa, J., & Hakkola, A. J. (2014) · The FASEB Journal · doi:10.1096/fj.13-245241 · Cited by 131 · see citing works
Metabolic regulation by SIRT3: implications for tumorigenesis
Finley, L. W. S., & Haigis, M. C. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.004 · Cited by 130 · see citing works
Disruption of uridine homeostasis links liver pyrimidine metabolism to lipid accumulation
Le, T. T., Ziemba, A. J., Urasaki, Y., Hayes, E. D., Brotman, S. J., & Pizzorno, G. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m034249 · Cited by 131 · see citing works
Electron transfer flavoprotein and its role in mitochondrial energy metabolism in health and disease
Henriques, B. J., Olsen, R. K. J., Gomes, C. M., & Bross, P. (2021) · Gene · doi:10.1016/j.gene.2021.145407 · Cited by 130 · see citing works
Morris, K. C., Lin, H. W., Thompson, J. W., & Pérez‐Pinzón, M. A. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.229 · Cited by 128 · see citing works
“During CR, the mitochondria undergo significant alterations in mitochondrial protein lysine-acetylation (Schwer et al, 2009), which suggests that this may be an important mitochondrial adaptation for conferring mitochondrial protection.”
BackgroundMitochondrial Sirtuins in the Regulation of Mitochondrial Activity and Metabolic Adaptation
Lombard, D. B., Tishkoff, D. X., & Bao, J. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_8 · Cited by 124 · see citing works
“In this regard, CPS1 possesses over 20 acetylation sites, implying that acetylation-mediated regulation of CPS1 activity may be quite complex (Schwer et al. 2009).”
BackgroundInfluentialSelf-citationRovira‐Llopis, S., Apostolova, N., Bañuls, C., Muntané, J., Rocha, M., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7313 · Cited by 120 · see citing works
“SIRT3 is also involved in the regulation of mitochondrial b -oxidation; for example, SIRT3-deficient animals show impaired b -oxidation and high levels of long-chain fatty acids upon fasting (279).”
Jeffers, V., & Sullivan, W. J. (2012) · Eukaryotic Cell · doi:10.1128/ec.00088-12 · Cited by 118 · see citing works
Albaugh, B. N., Arnold, K. M., & Denu, J. M. (2010) · ChemBioChem · doi:10.1002/cbic.201000438 · Cited by 117 · see citing works
Biochemical Genetic Pathways that Modulate Aging in Multiple Species: Figure 1.Preprint
Bitto, A., Wang, A. M., Bennett, C. F., & Kaeberlein, M. R. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025114 · Cited by 117 · see citing works
Mitochondrial sirtuins: Emerging roles in metabolic regulations, energy homeostasis and diseases
Parihar, P., Solanki, I., Mansuri, M. L., & Parihar, M. S. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.12.004 · Cited by 112 · see citing works
“…data revealed that a large fraction of mitochondrial proteins such as enzymes of tricarboxylic acid (TCA) cycle, fatty acid oxidation and oxidative phosphorylation are found to be acetylated during posttranslational modifications (Schwer et al., 2009; Verdin et al., 2010; Zhao et al., 2010).”
BackgroundTyagarajan, S. K., Ghosh, H., Yévenes, G. E., Imanishi, S. Y., Zeilhofer, H. U., Gerrits, B., & Fritschy, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442616 · Cited by 112 · see citing works
“lation at Lys-148 (23), the functional significance of acetylation on gephyrin is presently unknown.”
BackgroundSIRT3 Regulation of Mitochondrial Quality Control in Neurodegenerative Diseases
Meng, H., Yan, W.-Y., Lei, Y.-H., Wan, Z., Hou, Y.-Y., Sun, L., & Zhou, J.-P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00313 · Cited by 112 · see citing works
“SIRT3 belongs to the histone deacetylase family of silent information regulator 2 (Sir2) proteins, or sirtuins, whose deacetylase activity affects the acetylation status of at least 165 proteins in the mitochondrial proteome (Lombard et al., 2007; Schwer et al., 2009; Hebert et al., 2013).”
BackgroundYao, Y.-L., & Yang, W.-M. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2011/146493 · Cited by 120 · see citing works
Madkour, M. I., El-Serafi, A. T., Jahrami, H., Sherif, N. M., Hassan, R. E., Awadallah, S. M., & Faris, M. E. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.107801 · Cited by 112 · see citing works
Nallamilli, B. R. R., Edelmann, M. J., Zhong, X., Tan, F., Mujahid, H., Zhang, J., Nanduri, B., & Peng, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089283 · Cited by 109 · see citing works
“Peptides were incubated with 30 ml anti-acetyl-lysine antibody conjugated to agarose (ICP0388, Immunechem, USA) for 12 hours at 4uC as it has been previously published [30].”
MethodNAD and ADP ‐ribose metabolism in mitochondria
Dölle, C., Rack, J. G. M., & Ziegler, M. (2013) · FEBS Journal · doi:10.1111/febs.12304 · Cited by 108 · see citing works
Sirt3, Mitochondrial ROS, Ageing, and Carcinogenesis
Park, S., Özden, Ö., Jiang, H., Cha, Y. I., Pennington, J. D., Aykin‐Burns, N., Spitz, D. R., Gius, D. R., & Kim, H. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12096226 · Cited by 107 · see citing works
“Sirt3 appears to be the primary mitochondrial deacetylase it has been proposed that Sirt3 may function as a mitochondrial fidelity gene [72,73].”
The protein acetylome and the regulation of metabolism
Xing, S., & Poirier, Y. (2012) · Trends in Plant Science · doi:10.1016/j.tplants.2012.03.008 · Cited by 104 · see citing works
Quantitating the Specificity and Selectivity of Gcn5-Mediated Acetylation of Histone H3
Kuo, Y., & Andrews, A. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054896 · Cited by 104 · see citing works
“This would imply that the KATs are capable of leaving signals as to which complex activates transcription and/or which gene should be blocked from silencing.”
BackgroundInfluentialJang, Y. C., Liu, Y., Hayworth, C. R., Bhattacharya, A., Lustgarten, M. S., Müller, F. L., Chaudhuri, A. R., Qi, W., Li, Y., Huang, J., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00843.x · Cited by 94 · see citing works
“This is achieved by upregulation of mitochondrial sirtuin, SIRT3 (Schwer et al., 2009).”
BackgroundSelf-citationFukushima, A., & Lopaschuk, G. D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.020 · Cited by 94 · see citing works
The Cardiac Acetyl-Lysine Proteome
Foster, D. B., Liu, T., Rucker, J. J., O’Meally, R. N., Devine, L. R., Cole, R. N., & O'Rourke, B. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067513 · Cited by 92 · see citing works
“Comparison with the (@) mouse liver mitochondrial lysine acetylome of Schwer et al [35].”
BackgroundCircadian and Feeding Rhythms Orchestrate the Diurnal Liver Acetylome
Mauvoisin, D., Atger, F., Dayon, L., Galindo, A. N., Wang, J., Martín, E., Silva, L. D., Montoliu, I., Collino, S., Martin, F., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.065 · Cited by 91 · see citing works
“Early studies identified hundreds of acetylated peptides in the liver, with a strong enrichment in mitochondrial proteins (Kim et al., 2006; Schwer et al., 2009; Zhao et al., 2010).”
Fine Tuning Our Cellular Factories: Sirtuins in Mitochondrial Biology
Zhong, L., & Mostoslavsky, R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.004 · Cited by 90 · see citing works
“Notably, an earlier report showed increased CPS1 acetylation levels during CR (Schwer et al., 2009).”
Background
- Authors
- Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Michigan (US)
- Cell Signaling Technology (United States) (US)
- Harvard University (US)
- Corresponding author
- Alt, Frederick W.
- Lombard, David B.
- ORCID
- Venue
- Aging Cell
- Publisher
- Wiley
- Published
- 2009-09-24
- Volume
- 8
- Issue
- 5
- Pages
- 604-606
- ISSN
- 1474-9718 (ISSN-L)
- 1474-9726
- PMC
- PMC2752488
- OpenAlex
- W2095235693
- Cited by
- 259
- References
- 16
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 6 · 2023: 4 · 2022: 10 · 2021: 15 · 2020: 8 · 2019: 15 · 2018: 8 · 2017: 11 · 2016: 24 · 2015: 13 · 2014: 26 · 2013: 37 · 2012: 32
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Aging Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Deep Blue (University of Michigan) (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (AG022325, K08AG022325)
- National Institute of General Medical Sciences (T32GM007753)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Keywords
- caloric restriction, mitochondrial protein acetylation, lysine acetylation, mitochondrial adaptation, longevity, lifespan extension, tissue-specific effects, metabolic pathways, aging
- MeSH terms
- Acetylation, Animals, Saccharomycetales, Humans, Life Expectancy, Longevity, Mammals, Mice, Inbred C57BL, Mitochondria, Mitochondria, Liver, Proteins, Caloric Restriction, Mice
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