SIRT7 regulates NUCKS1 chromatin binding to elicit metabolic and inflammatory gene expression in senescence and liver aging
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Abstract
Sirtuin enzymes are deeply associated with senescence and aging. Sirtuin proteins are tightly regulated, but how their levels are governed during aging and how they elicit tissue-specific cellular changes are unclear. Here, we demonstrate that SIRT7 undergoes proteasomal degradation during senescence via targeting by the E3 ligase TRIP12. We identified the transcription factor nuclear casein kinase and cyclin-dependent kinase substrate 1 (NUCKS1) as an interactor of SIRT7 and found NUCKS1 recruitment onto chromatin during senescence mediated by SIRT7 loss, correlating with increased NUCKS1 acetylation. NUCKS1 depletion delayed senescence, leading to reduced inflammatory gene expression associated with transcription factors RELA and CEBPβ. In Sirt7 knockout and aged mouse livers, NUCKS1 was bound at the promoters and enhancers of age-related genes, and these regulatory regions gained accessibility during aging. Overall, our results uncover NUCKS1 as an interactor of SIRT7 and indicate that proteasomal loss of SIRT7 during senescence and liver aging promotes NUCKS1 acetylation and chromatin binding to induce metabolic and inflammatory genes.
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Cites
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400 · see citing works
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Model-based Analysis of ChIP-Seq (MACS)
Zhang, Y., Liu, T., Meyer, C. A., Eeckhoute, J., Johnson, D. S., Bernstein, B. E., Nusbaum, C., Myers, R. M., Brown, M., Li, W., et al. (2008) · Genome Biology · doi:10.1186/gb-2008-9-9-r137 · Cited by 18,386 · see citing works
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072 · see citing works
Szklarczyk, D., Gable, A. L., Lyon, D., Junge, A., Wyder, S., Huerta-Cepas, J., Simonovic, M., Doncheva, N. T., Morris, J. H., Bork, P., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1131 · Cited by 17,749 · see citing works
Robinson, J. T., Thorvaldsdóttir, H., Winckler, W., Guttman, M., Lander, E. S., Getz, G., & Mesirov, J. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1754 · Cited by 15,390 · see citing works
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
deepTools2: a next generation web server for deep-sequencing data analysis
Ramírez, F., Ryan, D. P., Grüning, B., Bhardwaj, V., Kilpert, F., Richter, A. S., Heyne, S., Dündar, F., & Manke, T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw257 · Cited by 8,096 · see citing works
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697 · see citing works
A cross-platform toolkit for mass spectrometry and proteomics
Chambers, M., MacLean, B., Burke, R., Amodei, D., Ruderman, D., Neumann, S., Gatto, L., Fischer, B., Pratt, B. S., Egertson, J. D., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2377 · Cited by 4,042 · see citing works
Clearance of p16Ink4a-positive senescent cells delays ageing-associated disorders
Baker, D. J., Wijshake, T., Tchkonia, T., LeBrasseur, N. K., Childs, B. G., van de Sluis, B., Kirkland, J. L., & van Deursen, J. M. (2011) · Nature · doi:10.1038/nature10600 · Cited by 3,670 · see citing works
Naturally occurring p16Ink4a-positive cells shorten healthy lifespan
Baker, D. J., Childs, B. G., Durik, M., Wijers, M. E., Sieben, C. J., Zhong, J., A. Saltness, R., Jeganathan, K. B., Verzosa, G. C., Pezeshki, A., et al. (2016) · Nature · doi:10.1038/nature16932 · Cited by 2,891 · see citing works
Geroscience: Linking Aging to Chronic Disease
Kennedy, B. K., Berger, S. L., Brunet, A., Campisi, J., Cuervo, A. M., Epel, E. S., Franceschi, C., Lithgow, G. J., Morimoto, R. I., Pessin, J. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.10.039 · Cited by 2,764 · see citing works
Self-citationCellular senescence in aging and age-related disease: from mechanisms to therapy
Childs, B. G., Durik, M., Baker, D. J., & van Deursen, J. M. (2015) · Nature Medicine · doi:10.1038/nm.4000 · Cited by 2,363 · see citing works
CellProfiler 4: improvements in speed, utility and usability
Stirling, D. R., Swain-Bowden, M. J., Lucas, A. M., Carpenter, A. E., Cimini, B. A., & Goodman, A. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04344-9 · Cited by 2,099 · see citing works
Oncogene-Induced Senescence Relayed by an Interleukin-Dependent Inflammatory Network
Kuilman, T., Michaloglou, C., Vredeveld, L. C. W., Douma, S., van Doorn, R., Desmet, C. J., Aarden, L. A., Mooi, W. J., & Peeper, D. S. (2008) · Cell · doi:10.1016/j.cell.2008.03.039 · Cited by 2,086 · see citing works
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
TRRUST v2: an expanded reference database of human and mouse transcriptional regulatory interactions
Han, H., Cho, J.-W., Lee, S., Yun, A., Kim, H., Bae, D., Yang, S., Kim, C. Y., Lee, M., Kim, E., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1013 · Cited by 1,983 · see citing works
Crosstalk in NF-κB Signaling Pathways
Oeckinghaus, A., Hayden, M. S., & Ghosh, S. (2011) · Nature Immunology · doi:10.1038/ni.2065 · Cited by 1,942 · see citing works
The CRAPome: a contaminant repository for affinity purification–mass spectrometry data
Mellacheruvu, D., Wright, Z., Couzens, A. L., Lambert, J.-P., St-Denis, N. A., Li, T., Miteva, Y. V., Hauri, S., Sardiu, M. E., Low, T. Y., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2557 · Cited by 1,686 · see citing works
NAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works
Cellular senescence mediates fibrotic pulmonary disease
Schafer, M. J., White, T. A., Iijima, K., Haak, A. J., Ligresti, G., Atkinson, E. J., Oberg, A. L., Birch, J., Salmonowicz, H., Zhu, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms14532 · Cited by 1,613 · see citing works
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,484 · see citing works
Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works
Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works
Clearance of senescent glial cells prevents tau-dependent pathology and cognitive decline
Bussian, T. J., Aziz, A., Meyer, C. F., Swenson, B. L., van Deursen, J. M., & Baker, D. J. (2018) · Nature · doi:10.1038/s41586-018-0543-y · Cited by 1,289 · see citing works
Zhang, H., Ryu, D., Wu, Y., Gariani, K., Wang, X., Luan, P., D’Amico, D., Ropelle, E. R., Lutolf, M. P., Aebersold, R., et al. (2016) · Science · doi:10.1126/science.aaf2693 · Cited by 1,255 · see citing works
Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works
Senescent intimal foam cells are deleterious at all stages of atherosclerosis
Childs, B. G., Baker, D. J., Wijshake, T., Conover, C. A., Campisi, J., & van Deursen, J. M. (2016) · Science · doi:10.1126/science.aaf6659 · Cited by 1,195 · see citing works
ChIPpeakAnno: a Bioconductor package to annotate ChIP-seq and ChIP-chip data
Zhu, L., Gazin, C., Lawson, N., Pagès, H., Lin, S. M., Lapointe, D. S., & Green, M. R. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-237 · Cited by 1,144 · see citing works
Analysing high-throughput sequencing data in Python with HTSeq 2.0
Putri, G., Anders, S., Pyl, P. T., Pimanda, J. E., & Zanini, F. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac166 · Cited by 1,108 · see citing works
Chien, Y., Scuoppo, C., Wang, X., Fang, X., Balgley, B., Bolden, J. E., Premsrirut, P., Luo, W., Chicas, A., Lee, C. S., et al. (2011) · Genes & Development · doi:10.1101/gad.17276711 · Cited by 1,046 · see citing works
Cellular senescence drives age-dependent hepatic steatosis
Ogrodnik, M., Miwa, S., Tchkonia, T., Tiniakos, D., Wilson, C. L., Lahat, A., Day, C. P., Burt, A., Palmer, A., Anstee, Q. M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15691 · Cited by 1,044 · see citing works
New developments on the Encyclopedia of DNA Elements (ENCODE) data portal
Luo, Y., Hitz, B. C., Gabdank, I., Hilton, J. A., Kagda, M. S., Lam, B. R., Myers, Z., Sud, P., Jou, J., Lin, K. Z., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1062 · Cited by 949 · see citing works
mTOR regulates MAPKAPK2 translation to control the senescence-associated secretory phenotype
Herranz, N., Gallage, S., Mellone, M., Wuestefeld, T., Klotz, S., Hanley, C. J., Raguz, S., Acosta, J. C., Innes, A. J., Banito, A., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3225 · Cited by 788 · see citing works
DNA damage response and cellular senescence in tissues of aging mice
Wang, C., Jurk, D., Maddick, M., Nelson, G., Martin‐Ruiz, C., & Von Zglinicki, T. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00481.x · Cited by 696 · see citing works
Histone H4 lysine 16 acetylation regulates cellular lifespan
Dang, W., Steffen, K. K., Perry, R., Dorsey, J. A., Johnson, F. B., Shilatifard, A., Kaeberlein, M., Kennedy, B. K., & Berger, S. L. (2009) · Nature · doi:10.1038/nature08085 · Cited by 667 · see citing works
Self-citationOrjalo, A. V., Bhaumik, D., Gengler, B. K., Scott, G. K., & Campisi, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905299106 · Cited by 654 · see citing works
Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 639 · see citing works
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 621 · see citing works
Self-citationSearle, B. C., Pino, L. K., Egertson, J. D., Ting, Y. S., Lawrence, R., MacLean, B., Villén, J., & MacCoss, M. J. (2018) · Nature Communications · doi:10.1038/s41467-018-07454-w · Cited by 508 · see citing works
A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging
Mohrin, M., Shin, J., Liu, Y., Brown, K., Luo, H., Xi, Y., Haynes, C. M., & Chen, D. (2015) · Science · doi:10.1126/science.aaa2361 · Cited by 490 · see citing works
SIRT1 is downregulated by autophagy in senescence and ageing
Xu, C., Wang, L., Fozouni, P., Evjen, G., Chandra, V., Jiang, J., Lu, C., Nicastri, M. C., Bretz, C. L., Winkler, J. D., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00579-5 · Cited by 471 · see citing works
Self-citationElevated histone expression promotes life span extension
Feser, J., Truong, D., Das, C., Carson, J. J., Kieft, J., Harkness, T., & Tyler, J. K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.015 · Cited by 435 · see citing works
Mcafee, Q. W., Zhang, Z., Samanta, A., Levi, S. M., Ma, X.-H., Piao, S., Lynch, J. P., Uehara, T., Sepulveda, A. R., Davis, L. E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118193109 · Cited by 423 · see citing works
Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres
O'Sullivan, R. J., Kubicek, S., Schreiber, S. L., & Karlseder, J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1897 · Cited by 416 · see citing works
Analyzing and interpreting genome data at the network level with ConsensusPathDB
Herwig, R., Hardt, C., Lienhard, M., & Kamburov, A. (2016) · Nature Protocols · doi:10.1038/nprot.2016.117 · Cited by 404 · see citing works
NAD+ metabolism governs the proinflammatory senescence-associated secretome
Nacarelli, T., Lau, L., Fukumoto, T., Zundell, J., Fatkhutdinov, N., Wu, S., Aird, K. M., Iwasaki, O., Kossenkov, A. V., Schultz, D., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0287-4 · Cited by 402 · see citing works
Hallmarks of Aging in the Liver
Hunt, N. J., Kang, S. W., Lockwood, G. P., Couteur, D. G. L., & Cogger, V. C. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.07.021 · Cited by 315 · see citing works
SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease
Shin, J., He, M., Liu, Y., Paredes, S., Villanova, L., Brown, K., Qiu, X., Nabavi, N., Mohrin, M., Wojnoonski, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.007 · Cited by 287 · see citing works
SIRT7 promotes genome integrity and modulates non‐homologous end joining DNA repair
Vázquez, B. N., Thackray, J. K., Simonet, N. G., Kane‐Goldsmith, N., Martínez‐Redondo, P., Nguyen, T. T. T., Bunting, S. F., Vaquero, A., Tischfield, J. A., & Serrano, L. (2016) · The EMBO Journal · doi:10.15252/embj.201593499 · Cited by 267 · see citing works
Self-citationA Fast SEQUEST Cross Correlation Algorithm
Eng, J. K., Fischer, B., Grossmann, J., & MacCoss, M. J. (2008) · Journal of Proteome Research · doi:10.1021/pr800420s · Cited by 244 · see citing works
SIRT7 Controls Hepatic Lipid Metabolism by Regulating the Ubiquitin-Proteasome Pathway
Yoshizawa, T., Karim, M. F., Sato, Y., Senokuchi, T., Miyata, K., Fukuda, T., Go, C., Tasaki, M., Uchimura, K., Kadomatsu, T., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.006 · Cited by 217 · see citing works
Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 198 · see citing works
IL-6-STAT3 signaling and premature senescence
Kojima, H., Inoue, T., Kunimoto, H., & Nakajima, K. (2013) · JAK-STAT · doi:10.4161/jkst.25763 · Cited by 170 · see citing works
McReynolds, M. R., Chellappa, K., & Baur, J. A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110888 · Cited by 169 · see citing works
SIRT7 antagonizes human stem cell aging as a heterochromatin stabilizer
Bi, S., Liu, Z., Wu, Z., Wang, Z., Liu, X., Wang, S., Ren, J., Yao, Y., Zhang, W., Song, M., et al. (2020) · Protein & Cell · doi:10.1007/s13238-020-00728-4 · Cited by 160 · see citing works
Kohler, D., Staniak, M., Tsai, T., Huang, T. C., Shulman, N., Bernhardt, O. M., MacLean, B., Nesvizhskii, A. I., Reiter, L., Sabidó, E., et al. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00834 · Cited by 138 · see citing works
Intracellular distribution of human SIRT 7 and mapping of the nuclear/nucleolar localization signal
Kiran, S., Chatterjee, N., Singh, S., Kaul, S. C., Wadhwa, R., & Ramakrishna, G. (2013) · FEBS Journal · doi:10.1111/febs.12346 · Cited by 127 · see citing works
SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing
Chen, S., Blank, M. F., Iyer-Bierhoff, A., Huang, B., Wang, L., Grummt, I., & Voit, R. (2016) · Nature Communications · doi:10.1038/ncomms10734 · Cited by 126 · see citing works
Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1
Fang, J. C., Ianni, A., Smolka, C., Vakhrusheva, O., Nolte, H., Krüger, M., Wietelmann, A., Simonet, N. G., Adrian-Segarra, J. M., Vaquero, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706945114 · Cited by 118 · see citing works
Self-citationSIRT7 has a critical role in bone formation by regulating lysine acylation of SP7/Osterix
FUKUDA, M., Yoshizawa, T., Karim, M. F., Sobuz, S. U., Korogi, W., Kobayasi, D., Okanishi, H., Tasaki, M., Ono, K., Sawa, T., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05187-4 · Cited by 108 · see citing works
Sun, S., Qin, W., Tang, X., Meng, Y., Hu, W., Zhang, S., Qian, M., Liu, Z., Cao, X., Pang, Q., et al. (2020) · Science Advances · doi:10.1126/sciadv.aay5556 · Cited by 107 · see citing works
Göke, J., Chan, Y.-S., Yan, J., Vingron, M., & Ng, H. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.030 · Cited by 105 · see citing works
Iyer-Bierhoff, A., Krogh, N., Tessarz, P., Ruppert, T., Nielsen, H. V., & Grummt, I. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.051 · Cited by 104 · see citing works
Zhao, J., Wozniak, A. L., Adams, A., Cox, J., Vittal, A., Voss, J. K., Bridges, B., Weinman, S. A., & Li, Z. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1246-4 · Cited by 89 · see citing works
Lagunas‐Rangel, F. A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04342-x · Cited by 89 · see citing works
Comparative interactomes of SIRT 6 and SIRT 7: Implication of functional links to aging
Lee, N., Kim, D., Kim, E., Park, S. J., Kwon, J., Shin, J., Park, S., Moon, Y. H., Wang, H.-J., Gho, Y. S., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201400001 · Cited by 85 · see citing works
Paredes, S., Angulo‐Ibáñez, M., Tasselli, L., Carlson, S. M., Zheng, W., Li, T., & Chua, K. F. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ac118.003325 · Cited by 84 · see citing works
SIRT7: the seventh key to unlocking the mystery of aging
Raza, U., Tang, X., Liu, Z., & Liu, B. (2023) · Physiological Reviews · doi:10.1152/physrev.00044.2022 · Cited by 81 · see citing works
SIRT7 mediates L1 elements transcriptional repression and their association with the nuclear lamina
Vazquez, B. N., Thackray, J. K., Simonet, N. G., Chahar, S., Kane-Goldsmith, N., Newkirk, S. J., Lee, S., Xing, J., Verzi, M. P., An, W., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz519 · Cited by 79 · see citing works
Self-citationChanges in nucleosome occupancy associated with metabolic alterations in aged mammalian liver
Bochkis, I. M., Przybylski, D., Chen, J., & Regev, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.048 · Cited by 78 · see citing works
The NUCKS1-SKP2-p21/p27 axis controls S phase entry
Hume, S., Grou, C. P. O., Lascaux, P., D’Angiolella, V., Legrand, A. J., Ramadan, K., & Dianov, G. L. (2021) · Nature Communications · doi:10.1038/s41467-021-27124-8 · Cited by 78 · see citing works
SIRT7-dependent deacetylation of CDK9 activates RNA polymerase II transcription
Blank, M. F., Chen, S., Poetz, F., Schnölzer, M., Voit, R., & Grummt, I. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx053 · Cited by 74 · see citing works
STAT3 Regulates the Onset of Oxidant-induced Senescence in Lung Fibroblasts
Waters, D. W., Blokland, K. E. C., Pathinayake, P. S., Wei, L., Schuliga, M. J., Jaffar, J., Westall, G. P., Hansbro, P. M., Prêle, C. M., Mutsaers, S. E., et al. (2019) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2018-0328oc · Cited by 70 · see citing works
Wyman, A. E., Noor, Z., Fishelevich, R., Lockatell, V., Shah, N. G., Todd, N. W., & Atamas, S. P. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00473.2016 · Cited by 69 · see citing works
SirT7 auto-ADP-ribosylation regulates glucose starvation response through mH2A1
Simonet, N. G., Thackray, J. K., Vázquez, B. N., Ianni, A., Espinosa‐Alcantud, M., Morales‐Sanfrutos, J., Hurtado-Bagès, S., Sabidó, E., Buschbeck, M., Tischfield, J. A., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz2590 · Cited by 65 · see citing works
Self-citationIanni, A., Kumari, P., Tarighi, S., Simonet, N. G., Popescu, D., Günther, S., Hölper, S., Schmidt, A., Smolka, C., Yue, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015339118 · Cited by 65 · see citing works
Self-citationNUCKS1 is a novel RAD51AP1 paralog important for homologous recombination and genome stability
Parplys, A. C., Zhao, W., Sharma, N., Groesser, T., Liang, F., Maranon, D. G., Leung, S. G., Grundt, K., Dray, E. V., Idate, R., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv859 · Cited by 62 · see citing works
A Click Chemistry Approach Reveals the Chromatin-Dependent Histone H3K36 Deacylase Nature of SIRT7
Wang, W., Angulo‐Ibáñez, M., Lyu, J., Kurra, Y., Tong, Z., Wu, B., Zhang, L., Sharma, V., Zhou, J., Lin, H., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b12083 · Cited by 62 · see citing works
Identification of a novel SIRT7 inhibitor as anticancer drug candidate
Kim, J. H., Kim, D., Cho, S. J., Jung, K.-Y., Kim, J., Lee, J. M., Jung, H. J., & Kim, K. R. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.11.120 · Cited by 60 · see citing works
Singh, S., Kumar, P., Thakur, S., Kiran, S., Sen, B., Sharma, S., Rao, V. V., Poongothai, A., & Ramakrishna, G. (2015) · Tumor Biology · doi:10.1007/s13277-015-3300-y · Cited by 59 · see citing works
Histone deficiency and accelerated replication stress in T cell aging
Kim, C., Jin, J., Ye, Z., Jadhav, R. R., Gustafson, C. E., Hu, B., Cao, W., Tian, L., Weyand, C. M., & Goronzy, J. J. (2021) · Journal of Clinical Investigation · doi:10.1172/jci143632 · Cited by 47 · see citing works
Kaiser, A., Schmidt, M., Huber, O., Frietsch, J. J., Scholl, S., Heidel, F. H., Hochhaus, A., Müller, J. P., & Ernst, T. (2020) · Leukemia · doi:10.1038/s41375-020-0803-3 · Cited by 46 · see citing works
NUCKS Is a Positive Transcriptional Regulator of Insulin Signaling
Qiu, B., Shi, X., Wong, E. T., Lim, J., Bezzi, M., Low, D., Zhou, Q., Akıncılar, S. C., Lakshmanan, M., Swa, H. L. F., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.030 · Cited by 45 · see citing works
Wiśniewski, J. R., Zougman, A., Krüger, S., Ziolkowski, P. P., Pudełko, M., Bębenek, M., & Mann, M. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22104 · Cited by 44 · see citing works
Liu, Z., Qian, M., Tang, X., Hu, W., Sun, S., Guo, L., Zhang, S., Meng, F., Cao, X., Sun, J. L., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0136-6 · Cited by 43 · see citing works
Age-Related Changes in Sirtuin 7 Expression in Calorie-Restricted and Refed Rats
Wrońska, A., Ławniczak, A., Wierzbicki, P., & Kmieć, Z. (2015) · Gerontology · doi:10.1159/000441603 · Cited by 40 · see citing works
SIRT7 activates p53 by enhancing PCAF-mediated MDM2 degradation to arrest the cell cycle
Lu, Y.-F., Xu, X.-P., Lu, X.-P., Zhu, Q., Liu, G., Bao, Y.-T., Wen, H., Li, Y.-L., Gu, W., & Zhu, W.-G. (2020) · Oncogene · doi:10.1038/s41388-020-1305-5 · Cited by 40 · see citing works
Aging is associated with increased chromatin accessibility and reduced polymerase pausing in liver
Bozukova, M., Nikopoulou, C., Kleinenkuhnen, N., Grbavac, D., Goetsch, K., & Tessarz, P. (2022) · Molecular Systems Biology · doi:10.15252/msb.202211002 · Cited by 39 · see citing works
Jiao, S., Meng, F., Zhang, J. C., Yang, X. W., Zheng, X., & Wang, L. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1197-3 · Cited by 34 · see citing works
Lee, Y., Shin, M. H., Kim, M. K., Kim, Y. K., Shin, H. S., Lee, D. H., & Chung, J. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042032 · Cited by 34 · see citing works
SIRT7 Facilitates CENP-A Nucleosome Assembly and Suppresses Intestinal Tumorigenesis
Liu, X., Li, C., Li, Q., Chang, H.-C., & Tang, Y. (2020) · iScience · doi:10.1016/j.isci.2020.101461 · Cited by 32 · see citing works
NUCKS1 promotes RAD54 activity in homologous recombination DNA repair
Maranon, D. G., Sharma, N., Huang, Y., Selemenakis, P., Wang, M., Altina, N. H., Zhao, W., & Wiese, C. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201911049 · Cited by 30 · see citing works
SIRT7 promotes chromosome synapsis during prophase I of female meiosis
Vázquez, B. N., Blengini, C. S., Hernandez, Y., Serrano, L., & Schindler, K. (2019) · Chromosoma · doi:10.1007/s00412-019-00713-9 · Cited by 29 · see citing works
Jin, Y., Liu, X., Liang, X., Liu, J., Liu, J., Han, Z., Lu, Q., Wang, K., Meng, B., Zhang, C., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05281-y · Cited by 29 · see citing works
Sirtuin 7-dependent deacetylation of DDB1 regulates the expression of nuclear receptor TR4
Karim, M. F., Yoshizawa, T., Sobuz, S. U., Sato, Y., & Yamagata, K. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.057 · Cited by 28 · see citing works
Inhibition of NUCKS Facilitates Corneal Recovery Following Alkali Burn
Poon, M.-W., Jiang, D., Qin, P., Zhang, Y., Qiu, B., Chanda, S. K., Tergaonkar, V., Li, Q., Wong, I. Y., Yu, Z., et al. (2017) · Scientific Reports · doi:10.1038/srep41224 · Cited by 27 · see citing works
SIRT7 is an important regulator of cartilage homeostasis and osteoarthritis development
Korogi, W., Yoshizawa, T., Karim, M. F., Tanoue, H., Yugami, M., Sobuz, S. U., Hinoi, E., Sato, Y., Oike, Y., Mizuta, H., et al. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.01.129 · Cited by 24 · see citing works
SIRT7 Deacetylates STRAP to Regulate p53 Activity and Stability
Yu, M., Shi, X., Ren, M., Liu, L., Qi, H., Zhang, C., Zou, J., Qiu, X., Zhu, W., Zhang, Y. E., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114122 · Cited by 20 · see citing works
Lee, S. H., Lee, Y. J., Jung, S., & Chung, K. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102909 · Cited by 12 · see citing works
Hypothalamic NUCKS regulates peripheral glucose homoeostasis
Qiu, B., Shi, X., Zhou, Q., Chen, H. S., Lim, J., Han, W., & Tergaonkar, V. (2015) · Biochemical Journal · doi:10.1042/bj20150450 · Cited by 11 · see citing works
Identification of kinases phosphorylating 13 sites in the nuclear, DNA-binding protein NUCKS
Grundt, K., Thiede, B., & Østvold, A. C. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.12.009 · Cited by 10 · see citing works
Signaling pathways that control mRNA translation initiation in macrophages
Tabatabaei, N., Hou, S., Kim, K.-W., & Tahmasebi, S. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109700 · Cited by 10 · see citing works
Differential Detergent Lysis of Cellular Fractions for ImmunoprecipitationPreprint
DeCaprio, J. A., & Kohl, T. O. (2020) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot098582 · Cited by 7 · see citing works
Flagged first, then by citations
2 of the 110 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Yu, W., Xu, J., Qiao, H., Liu, D., Sun, Y., Yan, R., Zhang, C., Yu, N., Song, Y., Ling, M., et al. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105335 · Cited by 11 · see citing works
Rehmannioside D ameliorates hepatocyte apoptosis and liver fibrosis by suppressing Sirt7/p53 axis
Liang, Y., Cheng, T.-Y., Pu, J.-Y., Chen, G., Liu, W., Mu, Y., Zhang, H., Chen, J., & Liu, P. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120863 · Cited by 8 · see citing works
Shi, H., Quan, P., Hou, Y., Wang, H., Wang, Y., Wang, H., & Zhang, W. (2026) · Journal of Virology · doi:10.1128/jvi.00396-26 · Cited by 3 · see citing works
A Double-Edged Role for SIRT7 in Cancer: Can Anti-Cancer Immunity Tip the Balance?
Tarighi, S., Ning, Z., Gámez-García, A., Vaquero, A., Braun, T. W., & Ianni, A. (2025) · Pharmaceuticals · doi:10.3390/ph18121878 · Cited by 2 · see citing works
Self-citationThe Sirtuin Network: Linking NAD + Metabolism, Mitochondrial Function, and Metabolic Homoeostasis
Szczęsny-Małysiak, E., Schiavoni, V., Rotondo, R., Zeppa, S. D., Vignini, A., Moriconi, E., Cecati, M., Armani, A., Gorini, S., Campagna, R., et al. (2026) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.70201 · Cited by 2 · see citing works
Zhang, L., Luo, D., & Bai, L. (2025) · Molecular Oral Microbiology · doi:10.1111/omi.70012 · Cited by 1 · see citing works
Cao, M., Zhang, J., Liu, H., Fan, R., Wu, F., Meng, Y., Li, T., Wu, Y., & Tang, X. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111173 · Cited by 1 · see citing works
Emerging roles of SIRT7 in metabolic homeostasis and related disorders
Yu, S., Rabiu, L., Zhu, W., & Tian, Y. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168343 · Cited by 1 · see citing works
Guo, R., Zhang, Z., Zhang, H., Yang, Y. J., Qiao, M., Zhang, J., Wang, Y., Chen, J., Li, J., Wu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.26.696635
Research Progress of the Sirtuins Family in Intervertebral Disc Degeneration
赵, 泽. (2026) · Advances in Clinical Medicine · doi:10.12677/acm.2026.162526
Jiang, J., Wang, Y., Qin, Y., Chen, L., Xu, X., Fan, G., Jing, D., Wei, M., Yu, X., Xu, J., et al. (2026) · Advanced Science · doi:10.1002/advs.202519824
The role of HECT-type E3 ubiquitin ligases in inflammation
Wang, Z., Wang, P., Xie, H., You, Z., Liu, X., Cao, F., & Yao, S. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1810360
Zhang, C., & Zhang, J. (2026) · Biogerontology · doi:10.1007/s10522-026-10453-w
Meng, N., Zhou, J., Guo, X., Hong, T., Li, X., Wei, X., Zhang, C., Zhang, X., Liu, S., Zhang, Y., et al. (2026) · Advanced Science · doi:10.1002/advs.77642
Chen, W., Yang, D., Liu, H., Tong, S., Liang, G., Zhang, J., Yang, J., & Li, Z. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118519
- Authors
- Tran, K. A., Gilbert, M., Vazquez, B. N., Ianni, A., Garcia, B. A., Vaquero, A., & Berger, S. L.
- Affiliations
- University of Pennsylvania (US)
- Washington University in St. Louis (US)
- Josep Carreras Leukaemia Research Institute (ES)
- Corresponding author
- Berger, Shelley L.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2025-06
- Volume
- 85
- Issue
- 12
- Pages
- 2390-2408.e6
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC10871251
- OpenAlex
- W4411237880
- Cited by
- 15
- References
- 110
- Citations by year
- 2026: 10 · 2025: 4 · 2024: 1
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 383 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (acceptedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- National Institute on Aging (P01AG031862, F32AG074641, P01AG047200, R01AG092045)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD106051)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Keywords
- SIRT7, NUCKS1, senescence, liver aging, proteasomal degradation, TRIP12, E3 ubiquitin ligase, protein acetylation, chromatin binding, inflammatory gene expression, metabolic gene expression, RelA, C/EBPβ, enhancer accessibility, sirtuins
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 ›
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