Cited by 2,081Sirtuins and Resveratrol in MedicineCancer-related Molecular PathwaysHistone Deacetylase Inhibitors Research

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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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Luo, Jianyuan, Nikolaev, Anatoly Y., Imai, Shin-ichiro, Chen, Delin, Su, Fei, Shiloh, Ariel, Guarente, Leonard, Gu, Wei·2001·Cell

DOI 10.1016/s0092-8674(01)00524-4

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Abstract

The NAD-dependent histone deacetylation of Sir2 connects cellular metabolism with gene silencing as well as aging in yeast. Here, we show that mammalian Sir2alpha physically interacts with p53 and attenuates p53-mediated functions. Nicotinamide (Vitamin B3) inhibits an NAD-dependent p53 deacetylation induced by Sir2alpha, and also enhances the p53 acetylation levels in vivo. Furthermore, Sir2alpha represses p53-dependent apoptosis in response to DNA damage and oxidative stress, whereas expression of a Sir2alpha point mutant increases the sensitivity of cells in the stress response. Thus, our findings implicate a p53 regulatory pathway mediated by mammalian Sir2alpha. These results have significant implications regarding an important role for Sir2alpha in modulating the sensitivity of cells in p53-dependent apoptotic response and the possible effect in cancer therapy.

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p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693
Surfing the p53 network
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607
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
Self-citation
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
Self-citation
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
Self-citation
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Nakano, K., & Vousden, K. H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00214-3 · Cited by 2,315
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824
Requirement of NAD and SIR2 for Life-Span Extension by Calorie Restriction in Saccharomyces cerevisiae
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Self-citation
Atmospheric carbon dioxide concentrations over the past 60 million years
Pearson, P. N., & Palmer, M. R. (2000) · Nature · doi:10.1038/35021000 · Cited by 1,771
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Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
Self-citation
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409
PUMA Induces the Rapid Apoptosis of Colorectal Cancer Cells
Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., & Vogelstein, B. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00213-1 · Cited by 1,289
Acetylation: a regulatory modification to rival phosphorylation?
Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155
The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970
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Pearson, M. A., Carbone, R., Sebastiani, C., Cioce, M., Fagioli, M., Saito, S., Higashimoto, Y., Appella, E., Minucci, S., Pandolfi, P. P., et al. (2000) · Nature · doi:10.1038/35018127 · Cited by 869
Deacetylation of p53 modulates its effect on cell growth and apoptosis
Luo, J., Su, F., Chen, D., Shiloh, A., & Gu, W. J. (2000) · Nature · doi:10.1038/35042612 · Cited by 838
Self-citation
Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity
Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809
ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
Maya, R., Balass, M., Kim, S.-T., Shkedy, D., Leal, J.-F. M., Shifman, O., Moas, M., Buschmann, T., Ronai, Z., Shiloh, Y., et al. (2001) · Genes & Development · doi:10.1101/gad.886901 · Cited by 731
Sir2 links chromatin silencing, metabolism, and agingPreprint
Guarente, L. (2000) · Genes & Development · doi:10.1101/gad.14.9.1021 · Cited by 718
Self-citation
A phylogenetically conserved NAD + -dependent protein deacetylase activity in the Sir2 protein family
Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718
Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
Yoshida, M., Horinouchi, S., & Beppu, T. (1995) · BioEssays · doi:10.1002/bies.950170510 · Cited by 715
Binding and modulation of p53 by p300/CBP coactivators
Lill, N. L., Grossman, S. R., Ginsberg, D., DeCaprio, J. A., & Livingston, D. M. (1997) · Nature · doi:10.1038/42981 · Cited by 693
Recruitment of p300/CBP in p53-Dependent Signal Pathways
Avantaggiati, M. L., Ogryzko, V. V., Gardner, K., Giordano, A., Levine, A. S., & Kelly, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80304-9 · Cited by 668
Signaling to p53
Prives, C. (1998) · Cell · doi:10.1016/s0092-8674(00)81774-2 · Cited by 623
Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo.
Butler, L. M., Agus, D. B., Scher, H. I., Higgins, B., Rose, A., Cordon‐Cardo, C., Thaler, H. T., Rifkind, R. A., Marks, P. A., & Richon, V. M. (2000) · PubMed · Cited by 609
Synergistic activation of transcription by CBP and p53
Gu, W., Shi, X.-L., & Roeder, R. G. (1997) · Nature · doi:10.1038/42972 · Cited by 599
Self-citation
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Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 597
Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1- O- acetyl-ADP-ribose
Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557
PML is induced by oncogenic ras and promotes premature senescence
Ferbeyre, G., de Stanchina, E., Querido, E., Baptiste, N., Prives, C., & Lowe, S. W. (2000) · Genes & Development · doi:10.1101/gad.14.16.2015 · Cited by 536
Impaired Fas Response and Autoimmunity in Pten +/− Mice
Cristofano, A. D., Kotsi, P., Peng, Y. F., Cordon‐Cardo, C., Elkon, K. B., & Pandolfi, P. P. (1999) · Science · doi:10.1126/science.285.5436.2122 · Cited by 521
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Guo, A., Salomoni, P., Luo, J., Shih, A. H., Zhong, S., Gu, W., & Pandolfi, P. P. (2000) · Nature Cell Biology · doi:10.1038/35036365 · Cited by 470
Self-citation
Genomewide studies of histone deacetylase function in yeast
Bernstein, B., Tong, J. K., & Schreiber, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250477697 · Cited by 419
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Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Lane, D. P., & Hay, R. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8458-8467.2000 · Cited by 386
ATM‐dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post‐translational activation of p53 protein involving poly(ADP‐ribose) polymerase
Vaziri, H., West, M. D., Allsopp, R., Davison, T. S., Wu, Y., Arrowsmith, C. H., Poirier, G. G., & Benchimol, S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.19.6018 · Cited by 384
Apoptosis or senescence-like growth arrest: influence of cell-cycle position, p53, p21 and bax in H2O2 response of normal human fibroblasts
Chen, Q. M., Juping, L. I. U., & MERRETT, J. B. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3470543 · Cited by 280
Apoptosis or Senescence-like Growth Arrest: Influence of Cell-Cycle Position, P53, P21 and Bax in H2O2 Response of Normal Human FIbroblasts
CHEN, Q. M., LIU, J., & MERRETT, J. B. (2000) · Biochemical Journal · doi:10.1042/bj3470543 · Cited by 280
A Novel Human SRB/MED-Containing Cofactor Complex, SMCC, Involved in Transcription Regulation
Gu, W., Malik, S., Ito, M., Yuan, C., Fondell, J. D., Zhang, X., Martinez, E., Qin, J., & Roeder, R. G. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80178-1 · Cited by 276
Self-citation
p53 transcriptional activity is essential for p53‐dependent apoptosis following DNA damage
Chao, C., Saito, S., Kang, J., Anderson, C. W., Appella, E., & Xu, Y. (2000) · The EMBO Journal · doi:10.1093/emboj/19.18.4967 · Cited by 260
Role of NAD+ in the Deacetylase Activity of the SIR2-like Proteins
Landry, J. W., Slama, J. T., & Sternglanz, R. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3854 · Cited by 254
Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
Tanny, J. C., & Moazed, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.415 · Cited by 253
A functionally inactive p53 protein interatocarcinoma cells is activated by either DNA damage or cellular differentiation
Lutzker, S. G., & Levine, A. J. (1996) · Nature Medicine · doi:10.1038/nm0796-804 · Cited by 206
Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination
Nakamura, S., Roth, J. A., & Mukhopadhyay, T. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9391-9398.2000 · Cited by 198
A transactivation-deficient mouse model provides insights into Trp53 regulation and function
Jimenez, G. S., Nistér, M., Stommel, J. M., Beeche, M., Barcarse, E. A., Zhang, X.-Q., O’Gorman, S., & Wahl, G. M. (2000) · Nature Genetics · doi:10.1038/79152 · Cited by 197
Involvement of p85 in p53-dependent apoptotic response to oxidative stress
Yin, Y., Terauchi, Y., Solomon, G. G., Aizawa, S., Rangarajan, P. N., Yazaki, Y., Kadowaki, T., & Barrett, J. C. (1998) · Nature · doi:10.1038/35648 · Cited by 155
Signaling to p53: breaking the posttranslational modification code.
Appella, E., & Anderson, C. W. (2000) · PubMed · Cited by 141
Inhibitors of histone deacetylase are potentially effective anticancer agents.
Marks, P. A., Rifkind, R. A., Richon, V. M., et al. (2001) · PubMed · Cited by 118
Activation of p53 or Loss of the Cockayne Syndrome Group B Repair Protein Causes Metaphase Fragility of Human U1, U2, and 5S Genes
Yu, A., Fan, H.-Y., Liao, D., Bailey, A. D., & Weiner, A. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80320-2 · Cited by 94
The Sir2 protein family: A novel deacetylase for gene silencing and more
Shore, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011506198 · Cited by 82
Aging, Chromatin, and Food Restriction--Connecting the Dots
Campisi, J. (2000) · Science · doi:10.1126/science.289.5487.2062 · Cited by 45
Oddball p53 in testicular tumors
Chresta, C. M., & Hickman, J. A. (1996) · Nature Medicine · doi:10.1038/nm0796-745 · Cited by 25
Aging, Chromatin, and Food Restriction
Campisi, J. (2001) · Science of Aging Knowledge Environment · Cited by 1
Cellular senescence and cancer
(1999) · doi:10.1002/(sici)1096-9896(199901)187:1

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Authors: Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W.
Affiliations: Columbia University (US)
Massachusetts Institute of Technology (US)
Corresponding author: Gu, Wei
ORCID: Luo, Jianyuan
Nikolaev, Anatoly Y.
Imai, Shin-ichiro
Chen, Delin
Guarente, Leonard
Gu, Wei
Venue: Cell
Publisher: Elsevier BV
Published: 2001-10
Volume: 107
Issue: 2
Pages: 137-148
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(01)00524-4
OpenAlex: W2012753961
Cited by: 2,081
References: 54
Citations by year: 2026: 21 · 2025: 35 · 2024: 30 · 2023: 37 · 2022: 54 · 2021: 71 · 2020: 62 · 2019: 62 · 2018: 71 · 2017: 84 · 2016: 97 · 2015: 105 · 2014: 134 · 2013: 127 · 2012: 121
FWCI: 39.40
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4307 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (2r01ca085533-16)
National Cancer Institute (R01CA85533)
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Keywords: p53, histone deacetylation, nicotinamide, p53 acetylation, apoptosis, DNA damage response, oxidative stress, stress response, cell survival, NAD+-dependent deacetylation, cancer therapy
MeSH terms: Animals, Cell Line, Cell Survival, DNA Damage, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Histone Deacetylases, Humans, NAD, Neoplasms, Niacinamide, Poly(ADP-ribose) Polymerases, Protein Binding, Blotting, Western, Transcriptional Activation, Trans-Activators, Polymerase Chain Reaction, Tumor Suppressor Protein p53, Mutagenesis, Site-Directed, Cell Death, Apoptosis, Point Mutation, Protein Structure, Tertiary, DNA, Complementary, Oxidative Stress, fas Receptor, Sirtuins, Mice, Sirtuin 1

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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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