374d4aa1222931287c857b0abe65947f SIRT1_regulates_DNA_damage.pdf eab39f4689a374636970dfdd5080f133f67929eb SIRT1_regulates_DNA_damage.pdf c4d411cebbd9c6fc41cc96e8602bbd08084d986fded3b306fb8025bd457df0b4 SIRT1_regulates_DNA_damage.pdf Title: SIRT1 regulates DNA damage signaling through the PP4 phosphatase complex Subject: DOI: 10.1093/nar/gkad504 , 51, 13, 13-6-2023. Abstract: The Sirtuin family of NAD+-dependent enzymes plays an important role in maintaining genome stability upon stress. Several mammalian Sirtuins have been linked directly or indirectly to the regulation of DNA damage during replication through Homologous recombination (HR). The role of one of them, SIRT1, is intriguing as it seems to have a general regulatory role in the DNA damage response (DDR) that has not yet been addressed. SIRT1-deficient cells show impaired DDR reflected in a decrease in repair capacity, increased genome instability and decreased levels of γH2AX. Here we unveil a close functional antagonism between SIRT1 and the PP4 phosphatase multiprotein complex in the regulation of the DDR. Upon DNA damage, SIRT1 interacts specifically with the catalytical subunit PP4c and promotes its inhibition by deacetylating the WH1 domain of the regulatory subunits PP4R3α/β. This in turn regulates γH2AX and RPA2 phosphorylation, two key events in the signaling of DNA damage and repair by HR. We propose a mechanism whereby during stress, SIRT1 signaling ensures a global control of DNA damage signaling through PP4. Keywords: Author: Rasti George, Becker Maximilian, Vazquez Berta N., Espinosa-Alcantud Maria, Fernndez-Duran Irene, Gmez-Garca Andrs, Ianni Alessandro, Gonzalez Jessica, Bosch-Presegu Laia, Marazuela-Duque Anna, Guitart-Solanes Anna, Segura-Bayona Sandra, Bech-Serra Joan-Josep, Scher Michael, Serrano Lourdes, Shankavaram Uma, Erdjument-Bromage Hediye, Tempst Paul, Reinberg Danny, Olivella Mireia, Stracker TravisH., delaTorre Carolina, Vaquero Alejandro Creator: OUP Producer: Acrobat Distiller 23.0 (Windows); modified using iTextSharp™ 5.5.10 ©2000-2016 iText Group NV (AGPL-version) CreationDate: Tue Jul 11 08:16:56 2023 CEST ModDate: Tue Jul 11 08:18:17 2023 CEST Tagged: yes UserProperties: no Suspects: no Form: none JavaScript: no Pages: 16 Encrypted: no Page size: 612.284 x 790.866 pts Page rot: 0 File size: 2969342 bytes Optimized: no PDF version: 1.4 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- LEBOJG+TimesNewRomanMTStd Type 1C Custom yes yes yes 49 0 LEBPGK+RMTMIB Type 1C Custom yes yes yes 2012 0 LEBPGL+CMSY10 Type 1C Custom yes yes yes 2013 0 LEBPGM+MTSY Type 1C Custom yes yes yes 50 0 LEBOJH+dummy-space Type 1C WinAnsi yes yes no 53 0 LEBOJI+TimesNewRomanMTStd-BoldIt Type 1C Custom yes yes yes 54 0 LEBOJJ+TimesNewRomanMTStd-Italic Type 1C Custom yes yes yes 55 0 LEBOJK+Helvetica-Bold Type 1C Custom yes yes no 56 0 LEBOKL+CMBSY10 Type 1C Custom yes yes yes 2014 0 LEBPBJ+Helvetica Type 1C Custom yes yes no 2015 0 LEBPCK+RMTMI Type 1C Custom yes yes yes 57 0 LEBPFJ+MathematicalPi-Four Type 1C Custom yes yes no 357 0 LECBAD+MathematicalPi-One Type 1C Custom yes yes no 51 0 LECBJB+TimesNewRomanMTStd-Bold Type 1C Custom yes yes yes 52 0 LECBPP+SFRM1000 Type 1C Custom yes yes yes 223 0 LECNOH+TimesNewRomanPS Type 1C Custom yes yes no 630 0 Jhove (Rel. 1.28.0, 2023-05-18) Date: 2024-03-13 02:29:27 CET RepresentationInformation: SIRT1_regulates_DNA_damage.pdf ReportingModule: PDF-hul, Rel. 1.12.4 (2023-03-16) LastModified: 2024-03-12 17:46:22 CET Size: 2969342 Format: PDF Version: 1.4 Status: Well-Formed, but not valid SignatureMatches: PDF-hul ErrorMessage: Invalid indirect destination - 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referenced object 'B28-R' cannot be found ID: PDF-HUL-122 Offset: 2800358 MIMEtype: application/pdf Profile: Tagged PDF PDFMetadata: Objects: 2065 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: ViewerPreferences: HideToolbar: false HideMenubar: false HideWindowUI: false FitWindow: false CenterWindow: false DisplayDocTitle: true NonFullScreenPageMode: UseNone Direction: L2R ViewArea: CropBox ViewClip: CropBox PrintArea: CropBox PageClip: CropBox PageLayout: OneColumn PageMode: UseThumbs Language: English Outlines: Item: Title: ABSTRACT Destination: section.1.1.0 Item: Title: GRAPHICAL ABSTRACT Destination: section.2.2.0 Item: Title: INTRODUCTION Destination: section.3.3.0 Item: Title: MATERIALS AND METHODS Destination: section.4.4.0 Item: Title: RESULTS Destination: section.5.19.0 Item: Title: DISCUSSION Destination: section.6.27.0 Item: Title: DATA AVAILABILITY Destination: section.7.28.0 Item: Title: SUPPLEMENTARY DATA Destination: section.8.29.0 Item: Title: ACKNOWLEDGEMENTS Destination: section.9.30.0 Item: Title: FUNDING Destination: section.10.31.0 Item: Title: Conflict of interest statement Destination: section.11.32.0 Item: Title: REFERENCES Destination: section.12.32.0 Info: Title: SIRT1 regulates DNA damage signaling through the PP4 phosphatase complex Author: Rasti George, Becker Maximilian, Vazquez Berta N., Espinosa-Alcantud Maria, Fernndez-Duran Irene, Gmez-Garca Andrs, Ianni Alessandro, Gonzalez Jessica, Bosch-Presegu Laia, Marazuela-Duque Anna, Guitart-Solanes Anna, Segura-Bayona Sandra, Bech-Serra Joan-Josep, Scher Michael, Serrano Lourdes, Shankavaram Uma, Erdjument-Bromage Hediye, Tempst Paul, Reinberg Danny, Olivella Mireia, Stracker TravisH., delaTorre Carolina, Vaquero Alejandro Subject: DOI: 10.1093/nar/gkad504 , 51, 13, 13-6-2023. Abstract: The Sirtuin family of NAD+-dependent enzymes plays an important role in maintaining genome stability upon stress. Several mammalian Sirtuins have been linked directly or indirectly to the regulation of DNA damage during replication through Homologous recombination (HR). The role of one of them, SIRT1, is intriguing as it seems to have a general regulatory role in the DNA damage response (DDR) that has not yet been addressed. SIRT1-deficient cells show impaired DDR reflected in a decrease in repair capacity, increased genome instability and decreased levels of γH2AX. Here we unveil a close functional antagonism between SIRT1 and the PP4 phosphatase multiprotein complex in the regulation of the DDR. Upon DNA damage, SIRT1 interacts specifically with the catalytical subunit PP4c and promotes its inhibition by deacetylating the WH1 domain of the regulatory subunits PP4R3α/β. This in turn regulates γH2AX and RPA2 phosphorylation, two key events in the signaling of DNA damage and repair by HR. We propose a mechanism whereby during stress, SIRT1 signaling ensures a global control of DNA damage signaling through PP4. 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