The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin
Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunopreci...
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| Published in: | Nature cell biology Vol. 24; no. 1; pp. 62 - 73 |
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| Main Authors: | , , , , , , , , , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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London
Nature Publishing Group UK
01.01.2022
Nature Publishing Group |
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| ISSN: | 1465-7392, 1476-4679, 1476-4679 |
| Online Access: | Get full text |
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| Abstract | Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors.
Krastev et al. report that trapped PARP1 undergoes SUMOylation, followed by ubiquitylation, resulting in the recruitment of the p97 ATPase to remove trapped PARP1 from chromatin and prevent PARP inhibitor-induced cytotoxicity. |
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| AbstractList | Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors.Krastev et al. report that trapped PARP1 undergoes SUMOylation, followed by ubiquitylation, resulting in the recruitment of the p97 ATPase to remove trapped PARP1 from chromatin and prevent PARP inhibitor-induced cytotoxicity. Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors.Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors. Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors. Krastev et al. report that trapped PARP1 undergoes SUMOylation, followed by ubiquitylation, resulting in the recruitment of the p97 ATPase to remove trapped PARP1 from chromatin and prevent PARP inhibitor-induced cytotoxicity. Poly (ADP-ribose) polymerase (PARP) inhibitors elicit antitumour activity in homologous recombination-defective cancers by trapping PARP1 in a chromatin-bound state. How cells process trapped PARP1 remains unclear. Using wild-type and a trapping-deficient PARP1 mutant combined with rapid immunoprecipitation mass spectrometry of endogenous proteins and Apex2 proximity labelling, we delineated mass spectrometry-based interactomes of trapped and non-trapped PARP1. These analyses identified an interaction between trapped PARP1 and the ubiquitin-regulated p97 ATPase/segregase. We found that following trapping, PARP1 is SUMOylated by PIAS4 and subsequently ubiquitylated by the SUMO-targeted E3 ubiquitin ligase RNF4, events that promote recruitment of p97 and removal of trapped PARP1 from chromatin. Small-molecule p97-complex inhibitors, including a metabolite of the clinically used drug disulfiram (CuET), prolonged PARP1 trapping and enhanced PARP inhibitor-induced cytotoxicity in homologous recombination-defective tumour cells and patient-derived tumour organoids. Together, these results suggest that p97 ATPase plays a key role in the processing of trapped PARP1 and the response of tumour cells to PARP inhibitors. |
| Author | Tutt, Andrew N. J. Talele, Tanaji T. Bartek, Jiri Wicks, Andrew J. Sun, Yilun Hoslett, Gwendoline Knight, Eleanor G. Ramadan, Kristijan Weekes, Daniel Badder, Luned M. Pettitt, Stephen J. Lord, Christopher J. Marlow, Rebecca Krastev, Dragomir B. Li, Shudong Pommier, Yves Choudhary, Jyoti S. Pardo, Mercedes Calvo Yu, Lu |
| Author_xml | – sequence: 1 givenname: Dragomir B. orcidid: 0000-0003-4298-7272 surname: Krastev fullname: Krastev, Dragomir B. organization: The CRUK Gene Function Laboratory, Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 2 givenname: Shudong surname: Li fullname: Li, Shudong organization: MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford – sequence: 3 givenname: Yilun orcidid: 0000-0002-6249-2704 surname: Sun fullname: Sun, Yilun organization: Developmental Therapeutics Branch, Laboratory of Molecular Pharmacology, Center for Cancer Research, National Cancer Institute, NIH – sequence: 4 givenname: Andrew J. orcidid: 0000-0002-9307-3262 surname: Wicks fullname: Wicks, Andrew J. organization: The CRUK Gene Function Laboratory, Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 5 givenname: Gwendoline orcidid: 0000-0002-0030-7761 surname: Hoslett fullname: Hoslett, Gwendoline organization: MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford – sequence: 6 givenname: Daniel surname: Weekes fullname: Weekes, Daniel organization: Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 7 givenname: Luned M. surname: Badder fullname: Badder, Luned M. organization: The Breast Cancer Now Research Unit, King’s College London – sequence: 8 givenname: Eleanor G. surname: Knight fullname: Knight, Eleanor G. organization: Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 9 givenname: Rebecca surname: Marlow fullname: Marlow, Rebecca organization: Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 10 givenname: Mercedes Calvo orcidid: 0000-0002-3477-9695 surname: Pardo fullname: Pardo, Mercedes Calvo organization: Functional Proteomics Laboratory, The Institute of Cancer Research – sequence: 11 givenname: Lu orcidid: 0000-0001-8378-9112 surname: Yu fullname: Yu, Lu organization: Functional Proteomics Laboratory, The Institute of Cancer Research – sequence: 12 givenname: Tanaji T. surname: Talele fullname: Talele, Tanaji T. organization: Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John’s University – sequence: 13 givenname: Jiri orcidid: 0000-0003-2013-7525 surname: Bartek fullname: Bartek, Jiri organization: Danish Cancer Society Research Center, Division of Genome Biology, Department of Medical Biochemistry and Biophysics, Science for Life Laboratory, Karolinska Institute – sequence: 14 givenname: Jyoti S. orcidid: 0000-0003-0881-5477 surname: Choudhary fullname: Choudhary, Jyoti S. organization: Functional Proteomics Laboratory, The Institute of Cancer Research – sequence: 15 givenname: Yves surname: Pommier fullname: Pommier, Yves organization: Developmental Therapeutics Branch, Laboratory of Molecular Pharmacology, Center for Cancer Research, National Cancer Institute, NIH – sequence: 16 givenname: Stephen J. orcidid: 0000-0003-3313-3857 surname: Pettitt fullname: Pettitt, Stephen J. email: Stephen.Pettitt@icr.ac.uk organization: The CRUK Gene Function Laboratory, Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 17 givenname: Andrew N. J. orcidid: 0000-0001-8715-2901 surname: Tutt fullname: Tutt, Andrew N. J. email: Andrew.Tutt@icr.ac.uk organization: Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research – sequence: 18 givenname: Kristijan orcidid: 0000-0001-5522-021X surname: Ramadan fullname: Ramadan, Kristijan email: Kristijan.Ramadan@oncology.ox.ac.uk organization: MRC Oxford Institute for Radiation Oncology, Department of Oncology, University of Oxford – sequence: 19 givenname: Christopher J. orcidid: 0000-0002-3226-0515 surname: Lord fullname: Lord, Christopher J. email: Chris.Lord@icr.ac.uk organization: The CRUK Gene Function Laboratory, Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35013556$$D View this record in MEDLINE/PubMed http://kipublications.ki.se/Default.aspx?queryparsed=id:148555552$$DView record from Swedish Publication Index (Karolinska Institutet) |
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| Cites_doi | 10.1038/ncomms5217 10.15252/embj.2019102361 10.1038/ncb1997 10.1038/s41467-020-15000-w 10.1016/j.molcel.2014.02.002 10.1038/s41586-020-2690-1 10.1038/nmeth.3179 10.1093/nar/gky1106 10.4161/cc.19978 10.1038/ncomms8289 10.1016/j.cell.2017.04.020 10.1016/j.celrep.2020.107985 10.1038/s41467-018-05031-9 10.1158/1078-0432.CCR-19-1089 10.1158/0008-5472.CAN-12-2753 10.1016/j.molcel.2018.01.012 10.1093/nar/gkw706 10.1126/science.aax6367 10.1158/1541-7786.MCR-18-0138 10.1074/jbc.M511658200 10.1016/j.molcel.2017.10.028 10.1126/science.1253596 10.1038/nprot.2016.020 10.1038/s41467-018-04466-4 10.1126/science.aam7344 10.1038/ncb2367 10.1038/nmeth.4535 10.1038/nature08657 10.1038/sdata.2017.20 10.1093/nar/gkaa718 10.1038/s41467-019-08301-2 10.1074/jbc.M109.074583 10.1038/ncb2407 10.1016/j.celrep.2021.109153 10.1016/j.ccell.2018.05.008 10.1038/emboj.2009.279 10.1091/mbc.E17-08-0514 10.1074/mcp.RA117.000471 10.1038/nature25016 10.1038/s41467-018-03917-2 10.1038/s41467-020-20359-x 10.1038/s41467-018-04619-5 10.1038/nature06388 10.1016/j.molcel.2011.06.036 10.15252/embr.201744754 10.1124/mol.118.114256 10.1038/ncb2301 10.1073/pnas.1008322108 10.1242/jcs.247809 10.1016/j.molcel.2016.03.008 10.1093/emboj/cdf579 10.1126/sciadv.aba6290 |
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| DOI | 10.1038/s41556-021-00807-6 |
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| References | Pettitt (CR51) 2017; 4 Vivelo, Wat, Agrawal, Tee, Leung (CR16) 2017; 45 Murai (CR2) 2012; 72 Mohammed (CR12) 2016; 11 Meyer, Weihl (CR36) 2014; 127 Duarte (CR41) 2018; 15 Lord, Ashworth (CR1) 2017; 355 Yeow (CR50) 2020; 585 Michelena (CR34) 2018; 9 Maric, Maculins, De Piccoli, Labib (CR10) 2014; 346 Hendriks, D’Souza, Chang, Mann, Vertegaal (CR23) 2015; 6 Ramadan (CR9) 2007; 450 Krastev (CR15) 2018; 9 Kilgas (CR44) 2021; 35 Tang, Odzorig, Jin, Xia (CR30) 2019; 95 Papachristou (CR14) 2018; 9 Fielden (CR11) 2020; 11 Xu (CR28) 2014; 5 Huang (CR29) 2018; 29 Zandarashvili (CR4) 2020; 368 Pettitt (CR3) 2018; 9 Skrott (CR37) 2017; 552 Singh (CR31) 2019; 38 Ritz (CR33) 2011; 13 Gong, Yeh (CR52) 2006; 281 Hulsmann (CR32) 2018; 17 Annunziato (CR49) 2019; 10 Perez-Riverol (CR54) 2019; 47 Gogola (CR5) 2018; 33 Martin (CR25) 2009; 28 van den Boom, Meyer (CR7) 2018; 69 Murai (CR45) 2018; 69 Wilcox, Laney (CR20) 2009; 11 Lam (CR13) 2015; 12 Bodnar, Rapoport (CR6) 2017; 169 Shao (CR40) 2020; 48 Gatti, Imhof, Huang, Baudis, Altmeyer (CR43) 2020; 32 Yusa, Zhou, Li, Bradley, Craig (CR47) 2011; 108 Thomas, Pommier (CR46) 2019; 25 Hopkins (CR39) 2019; 17 Pan (CR38) 2021; 12 Galanty (CR27) 2009; 462 Pfeiffer (CR42) 2021; 134 Gibbs-Seymour, Fontana, Rack, Ahel (CR48) 2016; 62 Raman, Havens, Walter, Harper (CR8) 2011; 44 Ryu (CR24) 2010; 285 CR26 Ndoja, Cohen, Yao (CR19) 2014; 53 Meyer, Bug, Bremer (CR21) 2012; 14 Meerang (CR18) 2011; 13 Henderson, Wolf (CR53) 1992; 10 Heidelberger (CR22) 2018; 19 Moudry (CR17) 2012; 11 Meyer, Wang, Warren (CR35) 2002; 21 J van den Boom (807_CR7) 2018; 69 Z Shao (807_CR40) 2020; 48 AA Duarte (807_CR41) 2018; 15 M Pan (807_CR38) 2021; 12 L Zandarashvili (807_CR4) 2020; 368 SJ Pettitt (807_CR3) 2018; 9 WK Tang (807_CR30) 2019; 95 M Raman (807_CR8) 2011; 44 J Murai (807_CR2) 2012; 72 H Meyer (807_CR36) 2014; 127 HH Meyer (807_CR35) 2002; 21 J Murai (807_CR45) 2018; 69 K Ramadan (807_CR9) 2007; 450 SS Lam (807_CR13) 2015; 12 ZY Yeow (807_CR50) 2020; 585 N Martin (807_CR25) 2009; 28 M Gatti (807_CR43) 2020; 32 DB Krastev (807_CR15) 2018; 9 Y Perez-Riverol (807_CR54) 2019; 47 S Kilgas (807_CR44) 2021; 35 M Maric (807_CR10) 2014; 346 A Ndoja (807_CR19) 2014; 53 J Fielden (807_CR11) 2020; 11 IA Hendriks (807_CR23) 2015; 6 Y Xu (807_CR28) 2014; 5 NO Bodnar (807_CR6) 2017; 169 CJ Lord (807_CR1) 2017; 355 JB Heidelberger (807_CR22) 2018; 19 Y Galanty (807_CR27) 2009; 462 AJ Wilcox (807_CR20) 2009; 11 D Ritz (807_CR33) 2011; 13 S Annunziato (807_CR49) 2019; 10 P Moudry (807_CR17) 2012; 11 J Michelena (807_CR34) 2018; 9 K Yusa (807_CR47) 2011; 108 807_CR26 H Meyer (807_CR21) 2012; 14 H Ryu (807_CR24) 2010; 285 CJ Henderson (807_CR53) 1992; 10 A Pfeiffer (807_CR42) 2021; 134 M Meerang (807_CR18) 2011; 13 I Gibbs-Seymour (807_CR48) 2016; 62 L Gong (807_CR52) 2006; 281 J Hulsmann (807_CR32) 2018; 17 E Gogola (807_CR5) 2018; 33 H Mohammed (807_CR12) 2016; 11 Z Skrott (807_CR37) 2017; 552 EY Huang (807_CR29) 2018; 29 CA Vivelo (807_CR16) 2017; 45 SJ Pettitt (807_CR51) 2017; 4 TA Hopkins (807_CR39) 2019; 17 EK Papachristou (807_CR14) 2018; 9 A Thomas (807_CR46) 2019; 25 AN Singh (807_CR31) 2019; 38 35013555 - Nat Cell Biol. 2022 Jan;24(1):2-4. doi: 10.1038/s41556-021-00819-2. 35245455 - Mol Cell. 2022 Mar 3;82(5):889-890. doi: 10.1016/j.molcel.2022.02.012. |
| References_xml | – volume: 5 year: 2014 ident: CR28 article-title: Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4 publication-title: Nat. Commun. doi: 10.1038/ncomms5217 – volume: 38 start-page: e102361 year: 2019 ident: CR31 article-title: The p97–Ataxin 3 complex regulates homeostasis of the DNA damage response E3 ubiquitin ligase RNF8 publication-title: EMBO J. doi: 10.15252/embj.2019102361 – volume: 11 start-page: 1481 year: 2009 end-page: 1486 ident: CR20 article-title: A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex publication-title: Nat. Cell Biol. doi: 10.1038/ncb1997 – volume: 11 year: 2020 ident: CR11 article-title: TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-DNA adducts publication-title: Nat. Commun. doi: 10.1038/s41467-020-15000-w – volume: 53 start-page: 893 year: 2014 end-page: 903 ident: CR19 article-title: Ubiquitin signals proteolysis-independent stripping of transcription factors publication-title: Mol. Cell doi: 10.1016/j.molcel.2014.02.002 – volume: 585 start-page: 447 year: 2020 end-page: 452 ident: CR50 article-title: Targeting TRIM37-driven centrosome dysfunction in 17q23-amplified breast cancer publication-title: Nature doi: 10.1038/s41586-020-2690-1 – volume: 12 start-page: 51 year: 2015 end-page: 54 ident: CR13 article-title: Directed evolution of APEX2 for electron microscopy and proximity labeling publication-title: Nat. Methods doi: 10.1038/nmeth.3179 – volume: 47 start-page: D442 year: 2019 end-page: D450 ident: CR54 article-title: The PRIDE database and related tools and resources in 2019: improving support for quantification data publication-title: Nucleic Acids Res. doi: 10.1093/nar/gky1106 – volume: 11 start-page: 1573 year: 2012 end-page: 1582 ident: CR17 article-title: Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage publication-title: Cell Cycle doi: 10.4161/cc.19978 – volume: 6 year: 2015 ident: CR23 article-title: System-wide identification of wild-type SUMO-2 conjugation sites publication-title: Nat. Commun. doi: 10.1038/ncomms8289 – volume: 169 start-page: 722 year: 2017 end-page: 735 ident: CR6 article-title: Molecular mechanism of substrate processing by the Cdc48 ATPase complex publication-title: Cell doi: 10.1016/j.cell.2017.04.020 – volume: 32 start-page: 107985 year: 2020 ident: CR43 article-title: The ubiquitin ligase TRIP12 limits PARP1 trapping and constrains PARP inhibitor efficiency publication-title: Cell Rep. doi: 10.1016/j.celrep.2020.107985 – volume: 9 year: 2018 ident: CR34 article-title: Analysis of PARP inhibitor toxicity by multidimensional fluorescence microscopy reveals mechanisms of sensitivity and resistance publication-title: Nat. Commun. doi: 10.1038/s41467-018-05031-9 – volume: 25 start-page: 6581 year: 2019 end-page: 6589 ident: CR46 article-title: Targeting topoisomerase I in the era of precision medicine publication-title: Clin. Cancer Res. doi: 10.1158/1078-0432.CCR-19-1089 – volume: 72 start-page: 5588 year: 2012 end-page: 5599 ident: CR2 article-title: Trapping of PARP1 and PARP2 by clinical PARP inhibitors publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-12-2753 – volume: 69 start-page: 371 year: 2018 end-page: 384 ident: CR45 article-title: SLFN11 blocks stressed replication forks independently of ATR publication-title: Mol. Cell doi: 10.1016/j.molcel.2018.01.012 – volume: 45 start-page: D204 year: 2017 end-page: D209 ident: CR16 article-title: ADPriboDB: the database of ADP-ribosylated proteins publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw706 – volume: 368 start-page: eaax6367 year: 2020 ident: CR4 article-title: Structural basis for allosteric PARP-1 retention on DNA breaks publication-title: Science doi: 10.1126/science.aax6367 – volume: 17 start-page: 409 year: 2019 end-page: 419 ident: CR39 article-title: PARP1 trapping by PARP inhibitors drives cytotoxicity in both cancer cells and healthy bone marrow publication-title: Mol. Cancer Res doi: 10.1158/1541-7786.MCR-18-0138 – volume: 281 start-page: 15869 year: 2006 end-page: 15877 ident: CR52 article-title: Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M511658200 – volume: 69 start-page: 182 year: 2018 end-page: 194 ident: CR7 article-title: VCP/p97-mediated unfolding as a principle in protein homeostasis and signaling publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.10.028 – volume: 346 start-page: 1253596 year: 2014 ident: CR10 article-title: Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication publication-title: Science doi: 10.1126/science.1253596 – volume: 11 start-page: 316 year: 2016 end-page: 326 ident: CR12 article-title: Rapid immunoprecipitation mass spectrometry of endogenous proteins (RIME) for analysis of chromatin complexes publication-title: Nat. Protoc. doi: 10.1038/nprot.2016.020 – volume: 9 year: 2018 ident: CR15 article-title: Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets publication-title: Nat. Commun. doi: 10.1038/s41467-018-04466-4 – ident: CR26 – volume: 355 start-page: 1152 year: 2017 end-page: 1158 ident: CR1 article-title: PARP inhibitors: synthetic lethality in the clinic publication-title: Science doi: 10.1126/science.aam7344 – volume: 13 start-page: 1376 year: 2011 end-page: 1382 ident: CR18 article-title: The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks publication-title: Nat. Cell Biol. doi: 10.1038/ncb2367 – volume: 15 start-page: 134 year: 2018 end-page: 140 ident: CR41 article-title: BRCA-deficient mouse mammary tumor organoids to study cancer-drug resistance publication-title: Nat. Methods doi: 10.1038/nmeth.4535 – volume: 462 start-page: 935 year: 2009 end-page: 939 ident: CR27 article-title: Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks publication-title: Nature doi: 10.1038/nature08657 – volume: 10 start-page: 221 year: 1992 end-page: 233 ident: CR53 article-title: Immunodetection of proteins by western blotting publication-title: Methods Mol. Biol. – volume: 4 year: 2017 ident: CR51 article-title: Genome-wide barcoded transposon screen for cancer drug sensitivity in haploid mouse embryonic stem cells publication-title: Sci. Data doi: 10.1038/sdata.2017.20 – volume: 48 start-page: 9694 year: 2020 end-page: 9709 ident: CR40 article-title: Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkaa718 – volume: 10 year: 2019 ident: CR49 article-title: Comparative oncogenomics identifies combinations of driver genes and drug targets in BRCA1-mutated breast cancer publication-title: Nat. Commun. doi: 10.1038/s41467-019-08301-2 – volume: 285 start-page: 14415 year: 2010 end-page: 14423 ident: CR24 article-title: PIASy mediates SUMO-2/3 conjugation of poly(ADP-ribose) polymerase 1 (PARP1) on mitotic chromosomes publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.074583 – volume: 14 start-page: 117 year: 2012 end-page: 123 ident: CR21 article-title: Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system publication-title: Nat. Cell Biol. doi: 10.1038/ncb2407 – volume: 35 start-page: 109153 year: 2021 ident: CR44 article-title: p97/VCP inhibition causes excessive MRE11-dependent DNA end resection promoting cell killing after ionizing radiation publication-title: Cell Rep. doi: 10.1016/j.celrep.2021.109153 – volume: 33 start-page: 1078 year: 2018 end-page: 1093 ident: CR5 article-title: Selective loss of PARG restores PARylation and counteracts PARP inhibitor-mediated synthetic lethality publication-title: Cancer Cell doi: 10.1016/j.ccell.2018.05.008 – volume: 28 start-page: 3534 year: 2009 end-page: 3548 ident: CR25 article-title: PARP-1 transcriptional activity is regulated by sumoylation upon heat shock publication-title: EMBO J. doi: 10.1038/emboj.2009.279 – volume: 29 start-page: 1021 year: 2018 end-page: 1030 ident: CR29 article-title: A VCP inhibitor substrate trapping approach (VISTA) enables proteomic profiling of endogenous ERAD substrates publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E17-08-0514 – volume: 17 start-page: 1295 year: 2018 end-page: 1307 ident: CR32 article-title: AP-SWATH reveals direct involvement of VCP/p97 in integrated stress response signaling through facilitating CReP/PPP1R15B degradation publication-title: Mol. Cell Proteom. doi: 10.1074/mcp.RA117.000471 – volume: 552 start-page: 194 year: 2017 end-page: 199 ident: CR37 article-title: Alcohol-abuse drug disulfiram targets cancer via p97 segregase adaptor NPL4 publication-title: Nature doi: 10.1038/nature25016 – volume: 9 year: 2018 ident: CR3 article-title: Genome-wide and high-density CRISPR–Cas9 screens identify point mutations in PARP1 causing PARP inhibitor resistance publication-title: Nat. Commun. doi: 10.1038/s41467-018-03917-2 – volume: 12 year: 2021 ident: CR38 article-title: Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative publication-title: Nat. Commun. doi: 10.1038/s41467-020-20359-x – volume: 9 year: 2018 ident: CR14 article-title: A quantitative mass spectrometry-based approach to monitor the dynamics of endogenous chromatin-associated protein complexes publication-title: Nat. Commun. doi: 10.1038/s41467-018-04619-5 – volume: 450 start-page: 1258 year: 2007 end-page: 1262 ident: CR9 article-title: Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin publication-title: Nature doi: 10.1038/nature06388 – volume: 127 start-page: 3877 year: 2014 end-page: 3883 ident: CR36 article-title: The VCP/p97 system at a glance: connecting cellular function to disease pathogenesis publication-title: J. Cell Sci. – volume: 44 start-page: 72 year: 2011 end-page: 84 ident: CR8 article-title: A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.06.036 – volume: 19 start-page: e44754 year: 2018 ident: CR22 article-title: Proteomic profiling of VCP substrates links VCP to K6-linked ubiquitylation and c-Myc function publication-title: EMBO Rep. doi: 10.15252/embr.201744754 – volume: 95 start-page: 286 year: 2019 end-page: 293 ident: CR30 article-title: Structural basis of p97 inhibition by the site-selective anticancer compound CB-5083 publication-title: Mol. Pharmacol. doi: 10.1124/mol.118.114256 – volume: 13 start-page: 1116 year: 2011 end-page: 1123 ident: CR33 article-title: Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations publication-title: Nat. Cell Biol. doi: 10.1038/ncb2301 – volume: 108 start-page: 1531 year: 2011 end-page: 1536 ident: CR47 article-title: A hyperactive piggyBac transposase for mammalian applications publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1008322108 – volume: 134 start-page: jcs247809 year: 2021 ident: CR42 article-title: Poly(ADP-ribosyl)ation temporally confines SUMO-dependent ataxin-3 recruitment to control DNA double-strand break repair publication-title: J. Cell Sci. doi: 10.1242/jcs.247809 – volume: 62 start-page: 432 year: 2016 end-page: 442 ident: CR48 article-title: HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.03.008 – volume: 21 start-page: 5645 year: 2002 end-page: 5652 ident: CR35 article-title: Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4 publication-title: EMBO J. doi: 10.1093/emboj/cdf579 – volume: 72 start-page: 5588 year: 2012 ident: 807_CR2 publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-12-2753 – volume: 44 start-page: 72 year: 2011 ident: 807_CR8 publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.06.036 – volume: 281 start-page: 15869 year: 2006 ident: 807_CR52 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M511658200 – volume: 69 start-page: 182 year: 2018 ident: 807_CR7 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.10.028 – volume: 45 start-page: D204 year: 2017 ident: 807_CR16 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw706 – volume: 6 year: 2015 ident: 807_CR23 publication-title: Nat. Commun. doi: 10.1038/ncomms8289 – volume: 62 start-page: 432 year: 2016 ident: 807_CR48 publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.03.008 – volume: 35 start-page: 109153 year: 2021 ident: 807_CR44 publication-title: Cell Rep. doi: 10.1016/j.celrep.2021.109153 – volume: 585 start-page: 447 year: 2020 ident: 807_CR50 publication-title: Nature doi: 10.1038/s41586-020-2690-1 – volume: 169 start-page: 722 year: 2017 ident: 807_CR6 publication-title: Cell doi: 10.1016/j.cell.2017.04.020 – volume: 33 start-page: 1078 year: 2018 ident: 807_CR5 publication-title: Cancer Cell doi: 10.1016/j.ccell.2018.05.008 – volume: 11 start-page: 316 year: 2016 ident: 807_CR12 publication-title: Nat. Protoc. doi: 10.1038/nprot.2016.020 – volume: 9 year: 2018 ident: 807_CR14 publication-title: Nat. Commun. doi: 10.1038/s41467-018-04619-5 – volume: 10 year: 2019 ident: 807_CR49 publication-title: Nat. Commun. doi: 10.1038/s41467-019-08301-2 – volume: 32 start-page: 107985 year: 2020 ident: 807_CR43 publication-title: Cell Rep. doi: 10.1016/j.celrep.2020.107985 – volume: 462 start-page: 935 year: 2009 ident: 807_CR27 publication-title: Nature doi: 10.1038/nature08657 – volume: 12 start-page: 51 year: 2015 ident: 807_CR13 publication-title: Nat. Methods doi: 10.1038/nmeth.3179 – ident: 807_CR26 doi: 10.1126/sciadv.aba6290 – volume: 47 start-page: D442 year: 2019 ident: 807_CR54 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gky1106 – volume: 9 year: 2018 ident: 807_CR15 publication-title: Nat. Commun. doi: 10.1038/s41467-018-04466-4 – volume: 17 start-page: 1295 year: 2018 ident: 807_CR32 publication-title: Mol. Cell Proteom. doi: 10.1074/mcp.RA117.000471 – volume: 17 start-page: 409 year: 2019 ident: 807_CR39 publication-title: Mol. Cancer Res doi: 10.1158/1541-7786.MCR-18-0138 – volume: 108 start-page: 1531 year: 2011 ident: 807_CR47 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1008322108 – volume: 25 start-page: 6581 year: 2019 ident: 807_CR46 publication-title: Clin. Cancer Res. doi: 10.1158/1078-0432.CCR-19-1089 – volume: 11 start-page: 1573 year: 2012 ident: 807_CR17 publication-title: Cell Cycle doi: 10.4161/cc.19978 – volume: 9 year: 2018 ident: 807_CR3 publication-title: Nat. Commun. doi: 10.1038/s41467-018-03917-2 – volume: 69 start-page: 371 year: 2018 ident: 807_CR45 publication-title: Mol. Cell doi: 10.1016/j.molcel.2018.01.012 – volume: 13 start-page: 1376 year: 2011 ident: 807_CR18 publication-title: Nat. Cell Biol. doi: 10.1038/ncb2367 – volume: 9 year: 2018 ident: 807_CR34 publication-title: Nat. Commun. doi: 10.1038/s41467-018-05031-9 – volume: 127 start-page: 3877 year: 2014 ident: 807_CR36 publication-title: J. Cell Sci. – volume: 552 start-page: 194 year: 2017 ident: 807_CR37 publication-title: Nature doi: 10.1038/nature25016 – volume: 53 start-page: 893 year: 2014 ident: 807_CR19 publication-title: Mol. Cell doi: 10.1016/j.molcel.2014.02.002 – volume: 21 start-page: 5645 year: 2002 ident: 807_CR35 publication-title: EMBO J. doi: 10.1093/emboj/cdf579 – volume: 10 start-page: 221 year: 1992 ident: 807_CR53 publication-title: Methods Mol. Biol. – volume: 15 start-page: 134 year: 2018 ident: 807_CR41 publication-title: Nat. Methods doi: 10.1038/nmeth.4535 – volume: 11 start-page: 1481 year: 2009 ident: 807_CR20 publication-title: Nat. Cell Biol. doi: 10.1038/ncb1997 – volume: 4 year: 2017 ident: 807_CR51 publication-title: Sci. Data doi: 10.1038/sdata.2017.20 – volume: 12 year: 2021 ident: 807_CR38 publication-title: Nat. Commun. doi: 10.1038/s41467-020-20359-x – volume: 134 start-page: jcs247809 year: 2021 ident: 807_CR42 publication-title: J. Cell Sci. doi: 10.1242/jcs.247809 – volume: 368 start-page: eaax6367 year: 2020 ident: 807_CR4 publication-title: Science doi: 10.1126/science.aax6367 – volume: 19 start-page: e44754 year: 2018 ident: 807_CR22 publication-title: EMBO Rep. doi: 10.15252/embr.201744754 – volume: 28 start-page: 3534 year: 2009 ident: 807_CR25 publication-title: EMBO J. doi: 10.1038/emboj.2009.279 – volume: 13 start-page: 1116 year: 2011 ident: 807_CR33 publication-title: Nat. Cell Biol. doi: 10.1038/ncb2301 – volume: 38 start-page: e102361 year: 2019 ident: 807_CR31 publication-title: EMBO J. doi: 10.15252/embj.2019102361 – volume: 29 start-page: 1021 year: 2018 ident: 807_CR29 publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E17-08-0514 – volume: 285 start-page: 14415 year: 2010 ident: 807_CR24 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.074583 – volume: 48 start-page: 9694 year: 2020 ident: 807_CR40 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkaa718 – volume: 450 start-page: 1258 year: 2007 ident: 807_CR9 publication-title: Nature doi: 10.1038/nature06388 – volume: 11 year: 2020 ident: 807_CR11 publication-title: Nat. Commun. doi: 10.1038/s41467-020-15000-w – volume: 355 start-page: 1152 year: 2017 ident: 807_CR1 publication-title: Science doi: 10.1126/science.aam7344 – volume: 346 start-page: 1253596 year: 2014 ident: 807_CR10 publication-title: Science doi: 10.1126/science.1253596 – volume: 95 start-page: 286 year: 2019 ident: 807_CR30 publication-title: Mol. Pharmacol. doi: 10.1124/mol.118.114256 – volume: 5 year: 2014 ident: 807_CR28 publication-title: Nat. Commun. doi: 10.1038/ncomms5217 – volume: 14 start-page: 117 year: 2012 ident: 807_CR21 publication-title: Nat. Cell Biol. doi: 10.1038/ncb2407 – reference: 35013555 - Nat Cell Biol. 2022 Jan;24(1):2-4. doi: 10.1038/s41556-021-00819-2. – reference: 35245455 - Mol Cell. 2022 Mar 3;82(5):889-890. doi: 10.1016/j.molcel.2022.02.012. |
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| Title | The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin |
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