SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

Fan, Wei; Luo, Jianyuan

doi:10.1016/j.molcel.2010.07.006

Cited by 224DNA Repair MechanismsSirtuins and Resveratrol in MedicineNuclear Structure and Function

SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

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Fan, Wei, Luo, Jianyuan·2010·Molecular Cell

DOI 10.1016/j.molcel.2010.07.006

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Abstract

SIRT1, a NAD(+)-dependent histone deacetylase, plays crucial roles in multiple biological processes including gene transcription, cellular metabolism, stress response, and tumorigenesis. Xeroderma pigmentosum group A (XPA) is a core nucleotide excision repair (NER) factor essential for NER process. Here we show that SIRT1 plays an important role in the regulation of NER pathway. Downregulation of SIRT1 significantly sensitizes cells to UV irradiation. SIRT1 interacts with XPA, and the interaction is enhanced after UV irradiation. XPA can be acetylated at lysines 63 and 67. SIRT1 deacetylates XPA both in vitro and in cells. Importantly, SIRT1-mediated deacetylation of XPA is required for optimal NER pathway since XPA-deficient cells complemented with XPA-K6367Q, which mimics hyperacetylated XPA, display significantly higher UV sensitivity compared with the XPA cells complemented with wild-type XPA. Furthermore, SIRT1-mediated XPA deacetylation enhances its interaction with RPA32. Our results demonstrate that SIRT1 regulates NER pathway through modulation of XPA acetylation status.

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Reduced NAD+ downregulates SIRT1, an NAD+-dependent deacetylase involved in mitochondrial homeostasis and XPA repair activity.
“They observed that the reduced level of NAD+ downregulated SIRT1, a NAD+- dependent deacetylase involved in regulating mitochondrial homeostasis and XPA repair activity 91–93.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [91]
ATR was involved in the regulation of the UV-induced XPA nuclear import.
“It previously was reported that the DNA damage checkpoint protein kinase ATR was involved in the regulation of the UV-induced XPA nuclear import23.”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [23]

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 2,653 · see citing works
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works
Self-citation
UV-induced DNA damage and repair: a review
Sinha, R. P., & Häder, D.-P. (2002) · Photochemical & Photobiological Sciences · doi:10.1039/b201230h · Cited by 1,978 · see citing works
Sirtuins in mammals: insights into their biological function
Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,719 · see citing works
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,351 · see citing works
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231 · see citing works
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works
Involvement of the TIP60 Histone Acetylase Complex in DNA Repair and Apoptosis
Ikura, T., Ogryzko, V. V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M., Scully, R., Qin, J., & Nakatani, Y. (2000) · Cell · doi:10.1016/s0092-8674(00)00051-9 · Cited by 1,029 · see citing works
Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.
Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.031 · Cited by 916 · see citing works
SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
Oberdoerffer, P., Michan, S., McVay, M., Mostoslavsky, R., Vann, J., Park, S.-K., Hartlerode, A., Stegmuller, J., Hafner, A., Loerch, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.025 · Cited by 852 · see citing works
Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB
Chen, L., Mu, Y., & Greene, W. C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf660 · Cited by 827 · see citing works
Impaired DNA Damage Response, Genome Instability, and Tumorigenesis in SIRT1 Mutant Mice
Wang, R.-H., Sengupta, K., Li, C., Kim, H., Cao, L., Xiao, C., Kim, S., Xu, X., Yin, Z., Chilton, B. S., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.09.001 · Cited by 769 · see citing works
A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
Sun, Y., Jiang, X., Chen, S., Fernandes, N., & Price, B. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504211102 · Cited by 738 · see citing works
The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth.
Firestein, R., Blander, G., Michan, S., Oberdoerffer, P., Ogino, S., Campbell, J., Bhimavarapu, A., Luikenhuis, S., de Cabo, R., Fuchs, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002020 · Cited by 588 · see citing works
DBC1 is a negative regulator of SIRT1
Kim, J., Chen, J., & Lou, Z. (2008) · Nature · doi:10.1038/nature06500 · Cited by 503 · see citing works
Negative regulation of the deacetylase SIRT1 by DBC1
Zhao, W., Kruse, J.-P., Tang, Y., Jung, S. Y., Qin, J., & Gu, W. J. (2008) · Nature · doi:10.1038/nature06515 · Cited by 464 · see citing works
Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage
Wang, C., Chen, L., Hou, X., Li, Z., Kabra, N., Ma, Y., Nemoto, S., Finkel, T., Gu, W. J., Cress, W. D., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1468 · Cited by 447 · see citing works
Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras–MAPK signaling in human cancer cells
Ota, H., Tokunaga, E., Chang, K., Hikasa, M., Iijima, K., Eto, M., Kozaki, K., Akishita, M., Ouchi, Y., & Kaneki, M. (2005) · Oncogene · doi:10.1038/sj.onc.1209049 · Cited by 431 · see citing works
How does SIRT1 affect metabolism, senescence and cancer?
Brooks, C. L., & Gu, W. J. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2562 · Cited by 426 · see citing works
The eukaryotic nucleotide excision repair pathway
Costa, R. (2003) · Biochimie · doi:10.1016/j.biochi.2003.10.017 · Cited by 373 · see citing works
Interplay among BRCA1, SIRT1, and Survivin during BRCA1-Associated Tumorigenesis
Wang, R.-H., Yin, Z., Kim, H., Xu, X., Cao, L., Lahusen, T. J., Lee, M., Xiao, C., Vassilopoulos, A., Chen, W., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.011 · Cited by 361 · see citing works
SIRT1 promotes DNA repair activity and deacetylation of Ku70
Jeong, J., Juhn, K., Lee, H., Kim, S. H., Min, B.-H., Lee, K., Cho, M., Park, G. H., & Lee, K.-H. (2007) · Experimental & Molecular Medicine · doi:10.1038/emm.2007.2 · Cited by 356 · see citing works
SIRT1, Is It a Tumor Promoter or Tumor Suppressor?
Deng, C. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.147 · Cited by 323 · see citing works
Activation of Stat3 Sequence-specific DNA Binding and Transcription by p300/CREB-binding Protein-mediated Acetylation
Wang, R., Cherukuri, P., & Luo, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413930200 · Cited by 275 · see citing works
Self-citation
SIRT1 Regulates the Function of the Nijmegen Breakage Syndrome Protein
Yuan, Z., Zhang, X. M., Sengupta, N., Lane, W. S., & Seto, E. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.029 · Cited by 271 · see citing works
Regulation of WRN Protein Cellular Localization and Enzymatic Activities by SIRT1-mediated Deacetylation
Li, K., Casta, A., Wang, R., Lozada, E., Fan, W., Kane, S. E., Ge, Q., Gu, W. J., Orren, D. K., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709707200 · Cited by 177 · see citing works
Self-citation
DNA damage triggers disruption of telomeric silencing and Mec1p-dependent relocation of Sir3p
McAinsh, A. D., Scott-Drew, S., Murray, J. A. H., & Jackson, S. P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80424-2 · Cited by 115 · see citing works
SIRT1: roles in aging and cancer
Kim, E.-J., & Um, S. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.11.751 · Cited by 89 · see citing works
Checkpoint Kinase ATR Promotes Nucleotide Excision Repair of UV-induced DNA Damage via Physical Interaction with Xeroderma Pigmentosum Group A
Shell, S. M., Li, Z., Shkriabai, N., Kvaratskhelia, M., Brosey, C., Serrano, M. A., Chazin, W. J., Musich, P. R., & Zou, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000745 · Cited by 86 · see citing works
Phosphorylation of Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A by Ataxia Telangiectasia Mutated and Rad3-Related–Dependent Checkpoint Pathway Promotes Cell Survival in Response to UV Irradiation
Wu, X., Shell, S. M., Yang, Z., & Zou, Y. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3403 · Cited by 85 · cited 2× · see citing works
“XPA is also regulated by phosphorylation (Wu et al., 2006).”
Background
A Functional Link Between SIRT1 Deacetylase and NBS1 in DNA Damage Response
Yuan, Z., & Seto, E. (2007) · Cell Cycle · doi:10.4161/cc.6.23.5026 · Cited by 77 · see citing works
RecQ4 Facilitates UV Light-induced DNA Damage Repair through Interaction with Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A (XPA)
Fan, W., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801928200 · Cited by 72 · see citing works
Self-citation
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KOBAYASHI, N., Katsumi, S., Imoto, K., Nakagawa, A., Miyagawa, S., Furumura, M., & Mori, T. (2001) · Pigment Cell Research · doi:10.1034/j.1600-0749.2001.140204.x · Cited by 66 · see citing works
Sirtuins (histone deacetylases III) in the cellular response to DNA damage—Facts and hypotheses
Kruszewski, M. K., & Szumiel, I. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.06.013 · Cited by 64 · see citing works
Human Xeroderma Pigmentosum Group A Protein Interacts with Human Replication Protein A and Inhibits DNA Replication
Lee, S., Kim, D., & Drissi, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21800 · Cited by 58 · see citing works
Acetylation of MyoD by p300 Requires More Than Its Histone Acetyltransferase Domain
Polesskaya, A., & Harel‐Bellan, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106501200 · Cited by 42 · see citing works
Domains in the XPA protein important in its role as a processivity factor
Bartels, C. L., & Lambert, M. W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.125 · Cited by 27 · see citing works

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Shen, H., Qi, X., Hu, Y., Wang, Y., Zhang, J., Liu, Z., & Qin, Z. (2024) · Theranostics · doi:10.7150/thno.100667 · Cited by 95 · see citing works
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Zannini, L., Buscemi, G., Kim, J., Fontanella, E., & Delia, D. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs035 · Cited by 93 · see citing works
Current role of mammalian sirtuins in DNA repair
Lagunas‐Rangel, F. A. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.06.009 · Cited by 93 · see citing works
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Meng, F., Qian, M., Peng, B., Peng, L., Wang, X., ZHENG, K. C., Liu, Z., Tang, X., Zhang, S., Sun, S., et al. (2020) · eLife · doi:10.7554/elife.55828 · Cited by 83 · see citing works
Sirtuin 1 and Skin: Implications in Intrinsic and Extrinsic Aging—A Systematic Review
Bielach-Bazyluk, A., Zbroch, E., Myśliwiec, H., Rydzewska–Rosołowska, A., Kakareko, K., Flisiak, I., & Hryszko, T. (2021) · Cells · doi:10.3390/cells10040813 · Cited by 83 · see citing works
Emerging Roles of SIRT1 in Cancer Drug Resistance
Wang, Z., & Chen, W. (2013) · Genes & Cancer · doi:10.1177/1947601912473826 · Cited by 84 · 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
Trending topics of SIRT1 in tumorigenicity
Garcia‐Peterson, L. M., & Li, X. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129952 · Cited by 78 · see citing works
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Martínez-Pastor, B., & Mostoslavsky, R. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00022 · Cited by 78 · see citing works
Sirtuins in Cancer: a Balancing Act between Genome Stability and Metabolism
Jeong, S. M., & Haigis, M. C. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0167 · Cited by 74 · see citing works
Poly(<scp>ADP</scp>‐ribose)‐mediated interplay of <scp>XPA</scp> and <scp>PARP</scp>1 leads to reciprocal regulation of protein function
Fischer, J. M. F., Popp, O., Gebhard, D., Veith, S., Fischbach, A., Beneke, S., Leitenstorfer, A., Bergemann, J., Scheffner, M., Ferrando‐May, E., et al. (2014) · The FEBS Journal · doi:10.1111/febs.12885 · Cited by 72 · see citing works
Updates on the epigenetic roles of sirtuins
Kosciuk, T., Wang, M., Hong, J. Y., & Lin, H. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.01.023 · Cited by 70 · see citing works
Sirt1 in cerebral ischemia
Pérez‐Pinzón, M. A., & Koronowski, K. B. (2015) · Brain Circulation · doi:10.4103/2394-8108.162532 · Cited by 69 · see citing works
Stress Inducibility of SIRT1 and Its Role in Cytoprotection and Cancer
Raynes, R., Brunquell, J., & Westerheide, S. D. (2013) · Genes & Cancer · doi:10.1177/1947601913484497 · Cited by 68 · see citing works
Causes and Consequences of Age-Related Changes in DNA Methylation: A Role for ROS?
Rang, F. J., & Boonstra, J. (2014) · Biology · doi:10.3390/biology3020403 · Cited by 65 · see citing works
XPA: DNA Repair Protein of Significant Clinical Importance
Pulzová, L., Ward, T. A., & Chovanec, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062182 · Cited by 66 · see citing works
Effects of Niacin Restriction on Sirtuin and PARP Responses to Photodamage in Human Skin
Benavente, C. A., Schnell, S. A., & Jacobson, E. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042276 · Cited by 65 · see citing works
SIRT1 is a Highly Networked Protein That Mediates the Adaptation to Chronic Physiological Stress
McBurney, M. W., Clark-Knowles, K. V., Caron, A. Z., & Gray, D. A. (2013) · Genes & Cancer · doi:10.1177/1947601912474893 · Cited by 66 · see citing works
Oxidative stress and inflammation regulation of sirtuins: New insights into common oral diseases
Pan, Z., Dong, H., Huang, N., & Fang, J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.953078 · Cited by 65 · see citing works
The deacetylase SIRT6 promotes the repair of UV-induced DNA damage by targeting DDB2
Geng, A.-K., Tang, H.-Y., Huang, J., Qian, Z., Qin, N., Yao, Y., Xu, Z., Chen, H., Lan, L., Xie, H., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa661 · Cited by 61 · see citing works
Loss of sirtuin 1 (SIRT1) disrupts skin barrier integrity and sensitizes mice to epicutaneous allergen challenge
Ming, M., Zhao, B., Shea, C. R., Shah, P., Qiang, L., White, S. R., Sims, D. M., & He, Y. (2014) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2014.09.035 · Cited by 62 · see citing works
Coordinated regulation of XPA stability by ATR and HERC2 during nucleotide excision repair
Lee, T.-H., Park, J.-M., Leem, S.-H., & Kang, T.-H. (2014) · Oncogene · doi:10.1038/onc.2012.539 · Cited by 61 · see citing works
Fight to the bitter end: DNA repair and aging
Chen, Y., Geng, A., Zhang, W., Qian, Z. Y., Wan, X., Jiang, Y., & Mao, Z. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101154 · Cited by 60 · see citing works
Citrate synthase desuccinylation by SIRT5 promotes colon cancer cell proliferation and migration
Ren, M., Yang, X. P., Bie, J., Wang, Z., Liu, M., Li, Y., Shao, G., & Luo, J. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0118 · Cited by 60 · see citing works
Self-citation
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Huber, K., & Superti‐Furga, G. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.01.018 · Cited by 59 · see citing works
High SIRT1 expression is a negative prognosticator in pancreatic ductal adenocarcinoma
Stenzinger, A., Endris, V., Klauschen, F., Sinn, B. V., Lorenz, K., Warth, A., Goeppert, B. F., Ehemann, V., Muckenhuber, A., Kamphues, C., et al. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-450 · Cited by 59 · see citing works
Chromatin modifications during repair of environmental exposure‐induced DNA damage: A potential mechanism for stable epigenetic alterations
O’Hagan, H. M. (2013) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21830 · Cited by 58 · see citing works
Role of nucleotide excision repair proteins in oxidative DNA damage repair: an updating
Pascucci, B., D’Errico, M., Parlanti, E., Giovannini, S., & Eugenia Dogliotti, Y. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911010032 · Cited by 58 · see citing works
Genome Instability and DNA Repair in Somatic and Reproductive Aging
Panier, S., Wang, S., & Schumacher, B. (2023) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-051122-093128 · Cited by 60 · see citing works
Hippo pathway and protection of genome stability in response to DNA damage
Pefani, D., & O’Neill, E. E. (2015) · FEBS Journal · doi:10.1111/febs.13604 · Cited by 55 · see citing works
Characterization of Nuclear Sirtuins: Molecular Mechanisms and Physiological Relevance
Toiber, D., Sebastián, C., & Mostoslavsky, R. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_9 · Cited by 55 · see citing works
Dual role of SIRT1 in UVB-induced skin tumorigenesis
Ming, M. E., Soltani, K., Shea, C. R., Li, X., & He, Y. (2014) · Oncogene · doi:10.1038/onc.2013.583 · Cited by 56 · see citing works
Sirtuins in dermatology: applications for future research and therapeutics
Serravallo, M., Jagdeo, J. R., Glick, S. A., Siegel, D. M., & Brody, N. (2013) · Archives of Dermatological Research · doi:10.1007/s00403-013-1320-2 · Cited by 57 · see citing works
Shedding light on structure, function and regulation of human sirtuins: a comprehensive review
Sharma, A. B., Mahur, P., Muthukumaran, J., Singh, A. K., & Jain, M. (2022) · 3 Biotech · doi:10.1007/s13205-022-03455-1 · Cited by 58 · see citing works
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Lin, Y.-H., Yuan, J., Pei, H., Liu, T., Ann, D. K., & Lou, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123935 · Cited by 56 · see citing works
DNA Damage Response and Metabolic Reprogramming in Health and Disease
Chatzidoukaki, O., Goulielmaki, E., Schumacher, B., & Garinis, G. A. (2020) · Trends in Genetics · doi:10.1016/j.tig.2020.06.018 · Cited by 54 · see citing works
Overview of xeroderma pigmentosum proteins architecture, mutations and post-translational modifications
Feltes, B. C., & Bonatto, D. (2014) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2014.12.002 · Cited by 53 · see citing works
The RASSF1A Tumor Suppressor Regulates XPA-Mediated DNA Repair
Donninger, H., Clark, J. A., Rinaldo, F. M., Nelson, N. C., Barnoud, T., Schmidt, M., Hobbing, K. R., Vos, M. D., Sils, B., & Clark, G. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00202-14 · Cited by 51 · see citing works
Does the use of melatonin overcome drug resistance in cancer chemotherapy?
Asghari, M. H., Ghobadi, E., Moloudizargari, M., Fallah, M., & Abdollahi, M. R. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.01.024 · Cited by 52 · see citing works
Dynamic switching of crotonylation to ubiquitination of H2A at lysine 119 attenuates transcription–replication conflicts caused by replication stress
Hao, S., Wang, Y., Zhao, Y., Gao, W. Y., Cui, W., Li, Y., Cui, J. G., Liu, Y., Lin, L., Xu, X., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac734 · Cited by 53 · see citing works
DNA damage mediated transcription arrest: Step back to go forward
Mullenders, L. H. F. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.09.005 · Cited by 51 · see citing works
Sirtuins of parasitic protozoa: In search of function(s)
Religa, A. A., & Waters, A. P. (2012) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2012.08.003 · Cited by 49 · see citing works
Interstrand Crosslink Repair as a Target for HDAC Inhibition
Nikolova, T., Kiweler, N., & Krämer, O. H. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.05.009 · Cited by 51 · see citing works
Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation
Park, J.-M., & Kang, T.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111840 · Cited by 44 · see citing works
Nutrient sensing by the mitochondrial transcription machinery dictates oxidative phosphorylation
Liu, L., Nam, M., Fan, W., Akie, T. E., Hoaglin, D. C., Gao, G., Keaney, J. F., & Cooper, M. P. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69413 · Cited by 48 · see citing works
Self-citation
The role of SIRT1/AKT/ERK pathway in ultraviolet B induced damage on human retinal pigment epithelial cells
Chou, W., Chen, K., Wang, Y., Wang, J., Liang, C.-L., & Juo, S. H. (2013) · Toxicology in Vitro · doi:10.1016/j.tiv.2013.05.002 · Cited by 45 · see citing works
Sirt1's systemic protective roles and its promise as a target in antiaging medicine
Tang, B. L. (2010) · Translational research · doi:10.1016/j.trsl.2010.11.006 · Cited by 45 · see citing works
The Role of SIRT1 in Tumorigenesis
Li, K., Luo, J., & Azabdaftari, G. (2011) · North American Journal of Medicine and Science · doi:10.7156/v4i2p104 · Cited by 45 · see citing works
Self-citation
Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases
Jęśko, H. M., & Strosznajder, R. P. (2016) · Folia Neuropathologica · doi:10.5114/fn.2016.62531 · Cited by 44 · see citing works
p300/CBP acetyl transferases interact with and acetylate the nucleotide excision repair factor XPG
Tillhon, M., Cazzalini, O., Nardò, T., Necchi, D., Sommatis, S., Stivala, L. A., Scovassi, A. I., & Prosperi, E. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.08.001 · Cited by 43 · see citing works

Regulation of the Functional Properties of Xeroderma Pigmentosum Complementation Group A (XPA) Protein through Lysine Acetylation
Njeri, C. W., Kaur, J., Turchi, J. J., & Balakrishnan, L. (2017) · The FASEB Journal · doi:10.1096/fasebj.31.1_supplement.lb56
Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C
Ming, M., Shea, C. R., Guo, X., Li, X., Soltani, K., Han, W., & He, Y.-Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010377108 · Cited by 145 · see citing works
Expression of Concern: Sirtuin 1-mediated deacetylation of XPA DNA repair protein enhances its interaction with ATR protein and promotes cAMP-induced DNA repair of UV damage.
(2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ec120.015927
Phosphorylation of Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A by Ataxia Telangiectasia Mutated and Rad3-Related–Dependent Checkpoint Pathway Promotes Cell Survival in Response to UV Irradiation
Wu, X., Shell, S. M., Yang, Z., & Zou, Y. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3403 · Cited by 85 · see citing works
NDR1 modulates the UV-induced DNA-damage checkpoint and nucleotide excision repair
Park, J., Choi, J. Y., Yi, J. M., Chung, J. W., Leem, S., Koh, S. S., & Kang, T. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.04.071 · Cited by 25 · see citing works

Authors: Fan, W., & Luo, J.
Affiliations: University of Massachusetts Chan Medical School (US)
University of Maryland, Baltimore (US)
Corresponding author: Luo, Jianyuan
ORCID: Luo, Jianyuan
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2010-07
Volume: 39
Issue: 2
Pages: 247-258
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2010.07.006
OpenAlex: W2137855486
Cited by: 223
References: 37
Citations by year: 2026: 6 · 2025: 12 · 2024: 4 · 2023: 7 · 2022: 11 · 2021: 15 · 2020: 23 · 2019: 14 · 2018: 12 · 2017: 15 · 2016: 10 · 2015: 18 · 2014: 19 · 2013: 24 · 2012: 17
FWCI: 7.42
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, 1112 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (R01AG026534)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: SIRT1, XPA, nucleotide excision repair, UV-induced DNA repair, histone deacetylase, protein acetylation, lysine acetylation, UV sensitivity, RPA32, protein-protein interaction, NAD+-dependent deacetylation
MeSH terms: Acetylation, DNA Repair, Genetic Complementation Test, HeLa Cells, Humans, Protein Processing, Post-Translational, Ultraviolet Rays, Mutation, Missense, Replication Protein A, Xeroderma Pigmentosum Group A Protein, Sirtuin 1

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SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

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