SIRT6 Promotes DNA Repair Under Stress by Activating PARP1
Open accessAbstract
A genome stability regulator integrates DNA repair and stress signaling pathways.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SIRT6 promotes DNA double strand break repair, regulates telomere stability, suppresses inflammation and opposes tumorigenesis.
“SIRT6 promotes DNA double strand break repair19,20, regulates telomere stability21, suppresses inflammation22 and opposes tumorigenesis23,24.”
From SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age (2014) · cites this paper as [19]
SIRT6 has multiple biochemical activities, including protein deacetylation and mono-ADP ribosylation.
“SIRT6 has multiple biochemical activities, including protein deacetylation22 and mono-ADP ribosylation19,29.”
From SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age (2014) · cites this paper as [19]
SIRT6 rapidly relocalizes to DNA damage sites in response to oxidative stress.
“SIRT6 is known to rapidly relocalize to DNA damage sites in response to oxidative stress19,36.”
From SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age (2014) · cites this paper as [19]
SIRT6 has been reported to mono-ADP ribosylate PARP1.
“SIRT6 has been reported to mono-ADP ribosylate PARP119”
From SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age (2014) · cites this paper as [19]
In vitro mono-ADP ribosylation experiments were conducted essentially as previously described.
“In vitro mono-ADP ribosylation experiments were conducted essentially as previously described19.”
From SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age (2014) · cites this paper as [19]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works
Calorie restriction–the SIR2 connection
Guarente, L., & Picard, F. (2005) · Cell · doi:10.1016/j.cell.2005.01.029 · Cited by 793 · see citing works
Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase
Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works
SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair
McCord, R. A., Michishita, E., Hong, T., Berber, E., Boxer, L. D., Kusumoto, R., Guan, S., Shi, X., Gozani, O., Burlingame, A. L., et al. (2009) · Aging · doi:10.18632/aging.100011 · Cited by 313 · see citing works
Flagged first, then by citations
Research works printed but not linked: 36
- [1]Sinclair DA Guarente L Cell 91 1033 1997 9428525
- [2]Kennedy BK Cell 89 381 1997 9150138
- [3]Dang W Nature 459 802 2009 19516333 PMC2702157
- [4]Haber JE Cell 97 829 1999 10399911
- [5]Guarente L Picard F Cell 120 473 2005 15734680
- [6]Saunders LR Verdin E Science 323 1021 2009 19229027
- [7]Westerheide SD Anckar J Stevens SM Jr Sistonen L Morimoto RI Science 323 1063 2009 19229036 PMC3429349
- [8]Dioum EM Science 324 1289 2009 19498162
- [9]Oberdoerffer P Cell 135 907 2008 19041753 PMC2853975
- [10]McCord RA Aging 1 109 2009 20157594 PMC2815768
- [11]Mostoslavsky R Cell 124 315 2006 16439206
- [12]Kaidi A Weinert BT Choudhary C Jackson SP Science 329 1348 PMC3276839 20829486
- [13]Gorbunova V Seluanov A Mech Ageing Dev 126 621 2005 15888314
- [14]Mao Z Seluanov A Jiang Y Gorbunova V Proc Natl Acad Sci U S A 104 13068 2007 17670947 PMC1941808
- [15]Michishita E Park JY Burneskis JM Barrett JC Horikawa I Mol Biol Cell 16 4623 2005 16079181 PMC1237069
- [16]Imai S Armstrong CM Kaeberlein M Guarente L Nature 403 795 2000 10693811
- [17]Landry J Proc Natl Acad Sci U S A 97 5807 2000 10811920 PMC18515
- [18]Frye RA Biochem Biophys Res Commun 260 273 1999 10381378
- [19]Michishita E Nature 452 492 2008 18337721 PMC2646112
- [20]Michishita E Cell Cycle 8 2664 2009 19625767 PMC4474138
- [21]Yang B Zwaans BM Eckersdorff M Lombard DB Cell Cycle 8 2662 2009 19597350 PMC2728171
- [22]Hassa PO Haenni SS Elser M Hottiger MO Microbiol Mol Biol Rev 70 789 2006 16959969 PMC1594587
- [23]Burkle A Biogerontology 1 41 2000 11707919
- [24]Ahel D Science 325 1240 2009 19661379 PMC3443743
- [25]El-Khamisy SF Masutani M Suzuki H Caldecott KW Nucleic Acids Res 31 5526 2003 14500814 PMC206461
- [26]Tao Z Gao P Liu HW J Am Chem Soc 131 14258 2009 19764761
- [27]Altmeyer M Messner S Hassa PO Fey M Hottiger MO Nucleic Acids Res 37 3723 2009 19372272 PMC2699514
- [28]Hochegger H Embo J 25 1305 2006 16498404 PMC1422167
- [29]Paddock MN Buelow BD Takeda S Scharenberg AM PLoS Biol 8 e1000428 PMC2907289 20652015
- [30]Jeggo PA Curr Biol 8 R49 1998 9427640
- [31]d’Adda di Fagagna F Nat Genet 23 76 1999 10471503
- [32]Wang M Nucleic Acids Res 34 6170 2006 17088286 PMC1693894
- [33]Audebert M Salles B Weinfeld M Calsou P J Mol Biol 356 257 2006 16364363
- [34]Tanny JC Dowd GJ Huang J Hilz H Moazed D Cell 99 735 1999 10619427
- [35]Liszt G Ford E Kurtev M Guarente L J Biol Chem 280 21313 2005 15795229
- [36]Gems D Partridge L Cell Metab 7 200 2008 18316025
Cited by
Sorted by citations
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226 · see citing works
Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works
Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works
Molecular mechanisms of dietary restriction promoting health and longevity
Green, C. L., Lamming, D. W., & Fontana, L. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00411-4 · Cited by 714 · see citing works
The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism
Sebastián, C., Zwaans, B. M. M., Silberman, D. M., Gymrek, M., Goren, A., Zhong, L., Ram, O., Truelove, J., Guimaraes, A. R., Toiber, D., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.047 · Cited by 660 · see citing works
DNA damage and its links to neurodegeneration
Madabhushi, R., Pan, L., & Tsai, L.-H. (2014) · Neuron · doi:10.1016/j.neuron.2014.06.034 · Cited by 654 · see citing works
The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4
Csibi, A., Fendt, S.-M., Li, C., Poulogiannis, G., Choo, A. Y., Chapski, D. J., Jeong, S. M., Dempsey, J. M., Parkhitko, A., Morrison, T., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.023 · Cited by 586 · see citing works
Fang, E. F., Kassahun, H., Croteau, D. L., Scheibye-Knudsen, M., Marosi, K., Lu, H., Shamanna, R. A., Kalyanasundaram, S., Bollineni, R. C., Wilson, M. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.004 · Cited by 575 · see citing works
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534 · see citing works
LINE1 Derepression in aged wild-type and SIRT6-deficient mice drives inflammation
Simon, M., Van Meter, M., Ablaeva, J., Ke, Z., Gonzalez, R. S., Taguchi, T., De Cecco, M., Leonova, K. I., Kogan, V., Helfand, S. L., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.02.014 · Cited by 498 · see citing works
Self-citationRedox 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
Van Meter, M., Kashyap, M., Rezazadeh, S., Geneva, A. J., Morello, T. D., Seluanov, A., & Gorbunova, V. (2014) · Nature Communications · doi:10.1038/ncomms6011 · Cited by 455 · see citing works
“SIRT6 is known to rapidly relocalize to DNA damage sites in response to oxidative stress 19,36 .”
InfluentialSelf-citationJeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445 · see citing works
SIRT6 recruits SNF2H to DNA break sites, preventing genomic instability through chromatin remodeling
Toiber, D., Erdel, F., Bouazoune, K., Silberman, D. M., Zhong, L., Mulligan, P., Sebastian, C., Cosentino, C., Martinez-Pastor, B., Giacosa, S., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.018 · Cited by 381 · see citing works
Nuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works
SIRT6 is responsible for more efficient DNA double-strand break repair in long-lived species
Tian, X., Firsanov, D., Zhang, Z., Cheng, Y., Luo, L., Tombline, G., Tan, R., Simon, M., Henderson, S., Steffan, J., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.043 · Cited by 353 · see citing works
Self-citationEpigenetic changes during aging and their reprogramming potential
Kane, A. E., & Sinclair, D. A. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1570075 · Cited by 283 · see citing works
DNA damage response and metabolic disease
Shimizu, I., Yoshida, Y., Suda, M., & Minamino, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.008 · Cited by 286 · see citing works
Poly(ADP-ribose) signaling in cell death
Virág, L., Robaszkiewicz, A., Rodriguez-Vargas, J. M., & Oliver, F. J. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.007 · Cited by 273 · see citing works
The sirtuins, oxidative stress and aging: an emerging link
Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · see citing works
Sirtuin catalysis and regulation
Feldman, J. L., Dittenhafer-Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.378877 · Cited by 248 · see citing works
Do DNA Double-Strand Breaks Drive Aging?
White, R. R., & Vijg, J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.004 · Cited by 232 · see citing works
Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246 · see citing works
Sirtuin regulation in aging and injury
Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236 · see citing works
Protective effects and mechanisms of sirtuins in the nervous system
Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211 · see citing works
The Metabolic Impact on Histone Acetylation and Transcription in Ageing
Peleg, S., Feller, C., Ladurner, A. G., & Imhof, A. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.05.008 · Cited by 178 · see citing works
Mao, Z., Tian, X., Van Meter, M., Ke, Z., Gorbunova, V., & Seluanov, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200583109 · Cited by 176 · see citing works
Self-citationGenomic integrity and the ageing brain
Chow, H.-M., & Herrup, K. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn4020 · Cited by 174 · see citing works
Role of the inflammation-autophagy-senescence integrative network in osteoarthritis
Vinatier, C., Domínguez, E., Guicheux, J., & Caramés, B. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00706 · Cited by 135 · see citing works
Sirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Bosch‐Presegué, L., & Vaquero, A. (2015) · The FEBS Journal · doi:10.1111/febs.13053 · Cited by 132 · see citing works
Phosphoproteomic approach to characterize protein mono- and poly(ADP-ribosyl)ation sites from cells
Daniels, C. M., Ong, S.-E., & Leung, A. K. L. (2014) · Journal of Proteome Research · doi:10.1021/pr401032q · Cited by 119 · see citing works
Contributions of DNA Damage to Alzheimer’s Disease
Lin, X., Kapoor, A., Gu, Y., Chow, M. J., Peng, J., Zhao, K., & Tang, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051666 · Cited by 117 · see citing works
Lifespan and Stress Resistance in Drosophila with Overexpressed DNA Repair Genes
Shaposhnikov, M., Proshkina, E., Shilova, L., Zhavoronkov, A., & Moskalev, A. (2015) · Scientific Reports · doi:10.1038/srep15299 · Cited by 88 · see citing works
DNA double strand break repair, aging and the chromatin connection
Gorbunova, V., & Seluanov, A. (2016) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2016.02.004 · Cited by 87 · see citing works
Self-citationIdentification of and molecular basis for sirt6 loss-of-function point mutations in cancer
Kugel, S., Feldman, J. L., Klein, M. A., Silberman, D. M., Sebastián, C., Mermel, C., Dobersch, S., Clark, A. R., Getz, G., Denu, J. M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.022 · Cited by 81 · see citing works
Toward understanding genomic instability, mitochondrial dysfunction and aging
Fakouri, N. B., Hou, Y., Demarest, T. G., Christiansen, L. S., Okur, M. N., Mohanty, J. G., Croteau, D. L., & Bohr, V. A. (2019) · The FEBS Journal · doi:10.1111/febs.14663 · Cited by 77 · see citing works
Sirtuin 6—A Key Regulator of Hepatic Lipid Metabolism and Liver Health
Dong, X. C. (2023) · Cells · doi:10.3390/cells12040663 · Cited by 63 · see citing works
Ortega, I., Villanueva, J. A., Wong, D. H., Cress, A. B., Sokalska, A., Stanley, S. D., & Duleba, A. J. (2012) · Endocrinology · doi:10.1210/en.2012-1385 · Cited by 57 · see citing works
Zhang, Y., Chang, J.-F., Sun, J., Chen, L., Yang, X.-M., Tang, H.-Y., Jing, Y.-Y., Kang, X., He, Z.-M., Wu, J.-Y., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.215525 · Cited by 45 · see citing works
Self-citationPoly (ADP-ribose) polymerase 1 and neurodegenerative diseases: past, present, and future
Hu, M.-L., Pan, Y.-R., Yong, Y.-Y., Liu, Y., Yu, L., Qin, D.-L., Qiao, G., Law, B. Y.-K., Wu, J.-M., Zhou, X.-G., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102078 · Cited by 44 · see citing works
Erosion of the Epigenetic Landscape and Loss of Cellular Identity as a Cause of Aging in Mammals
Yang, J.-H., Griffin, P. T., Vera, D. L., Apostolides, J. K., Hayano, M., Meer, M. V., Salfati, E. L., Su, Q., Munding, E. M., Blanchette, M., et al. (2019) · doi:10.1101/808642 · Cited by 38 · see citing works
Carcinogenesis resistance in the longest‐lived rodent, the naked mole‐rat
Yamamura, Y., Kawamura, Y., Oka, K., & Miura, K. (2022) · Cancer Science · doi:10.1111/cas.15570 · Cited by 20 · see citing works
- Authors
- Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V.
- Affiliations
- University of Rochester (US)
- Department of Biology, University of Rochester, Rochester, NY 14627, USA.
- Corresponding author
- Seluanov, Andrei
- Gorbunova, Vera
- Venue
- Science
- Published
- 2011-06-17
- Volume
- 332
- Issue
- 6036
- Pages
- 1443-1446
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5472447
- OpenAlex
- W2054866841
- Cited by
- 867
- References
- 5
- Citations by year
- 2026: 39 · 2025: 47 · 2024: 49 · 2023: 68 · 2022: 47 · 2021: 72 · 2020: 64 · 2019: 55 · 2018: 50 · 2017: 65 · 2016: 70 · 2015: 54 · 2014: 57 · 2013: 61 · 2012: 57
- FWCI
- 24.30
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (F31AG041603, R01AG027237)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- SIRT6, PARP1, DNA double-strand break repair, oxidative stress, mono-ADP-ribosylation, non-homologous end joining, homologous recombination, genomic instability, sirtuins, ADP-ribosyltransferase activity
- MeSH terms
- Poly (ADP-Ribose) Polymerase-1, Animals, Cell Line, DNA, DNA Repair, Humans, Paraquat, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Recombination, Genetic, Transfection, Signal Transduction, Point Mutation, Mice, Knockout, Oxidative Stress, Sirtuins, Mice, DNA Breaks, Double-Stranded
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review