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  1. AU="Giansanti, Celeste"
  2. AU="Chang, Susan"
  3. AU="Schneider, Henning"
  4. AU="Quirion, Philippe"
  5. AU="Kinnunen, Ritva"
  6. AU=Doherty Taylor A.
  7. AU="Ganesha Rai"
  8. AU="Edwards, Kurtis"
  9. AU="Schneider, Clément"
  10. AU="Lara-Hernandez, A"
  11. AU=Turck J
  12. AU="Aali, Ghazaleh"
  13. AU="Catapano, Joshua S"
  14. AU=Zoloth Laurie
  15. AU="Scholtz, Clarke H"
  16. AU="Meirelles, Gustavo de Souza Portes"
  17. AU=Demirbilek Nevzat
  18. AU="Larrosa-Escartín, Nieves"
  19. AU=Crago Aimee M.
  20. AU="Mármora, Lelio"
  21. AU="Asbell, Madison"
  22. AU="Yuka Ikeda"
  23. AU="Oppenheimer, Federic"
  24. AU=Guillevin Loic
  25. AU="Sabiha Alam"
  26. AU="Taher, Bianca Petra"
  27. AU="Obier, Frank"
  28. AU=Davila Eduardo AU=Davila Eduardo
  29. AU="Albizu, Constanza Lopez"
  30. AU="Antonova, Anastasiia"
  31. AU=Crowther L. M.
  32. AU=Zhan Xiping
  33. AU="Xuhui Bao"
  34. AU="Zuman Dou"

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  1. Artikel ; Online: Self-reversal facilitates the resolution of HMCES DNA-protein crosslinks in cells.

    Rua-Fernandez, Jorge / Lovejoy, Courtney A / Mehta, Kavi P M / Paulin, Katherine A / Toudji, Yasmine T / Giansanti, Celeste / Eichman, Brandt F / Cortez, David

    Cell reports

    2023  Band 42, Heft 11, Seite(n) 113427

    Abstract: Abasic sites are common DNA lesions stalling polymerases and threatening genome stability. When located in single-stranded DNA (ssDNA), they are shielded from aberrant processing by 5-hydroxymethyl cytosine, embryonic stem cell (ESC)-specific (HMCES) via ...

    Abstract Abasic sites are common DNA lesions stalling polymerases and threatening genome stability. When located in single-stranded DNA (ssDNA), they are shielded from aberrant processing by 5-hydroxymethyl cytosine, embryonic stem cell (ESC)-specific (HMCES) via a DNA-protein crosslink (DPC) that prevents double-strand breaks. Nevertheless, HMCES-DPCs must be removed to complete DNA repair. Here, we find that DNA polymerase α inhibition generates ssDNA abasic sites and HMCES-DPCs. These DPCs are resolved with a half-life of approximately 1.5 h. HMCES can catalyze its own DPC self-reversal reaction, which is dependent on glutamate 127 and is favored when the ssDNA is converted to duplex DNA. When the self-reversal mechanism is inactivated in cells, HMCES-DPC removal is delayed, cell proliferation is slowed, and cells become hypersensitive to DNA damage agents that increase AP (apurinic/apyrimidinic) site formation. In these circumstances, proteolysis may become an important mechanism of HMCES-DPC resolution. Thus, HMCES-DPC formation followed by self-reversal is an important mechanism for ssDNA AP site management.
    Mesh-Begriff(e) DNA Damage ; Proteins/genetics ; DNA Replication ; DNA Repair ; DNA/genetics ; DNA, Single-Stranded
    Chemische Substanzen Proteins ; DNA (9007-49-2) ; DNA, Single-Stranded
    Sprache Englisch
    Erscheinungsdatum 2023-11-11
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113427
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  2. Buch ; Online ; Dissertation / Habilitation: The MDM2 oncoprotein antagonizes Poly(ADP-ribosyl)ation

    Giansanti, Celeste [Verfasser] / Dobbelstein, Matthias [Akademischer Betreuer] / Dobbelstein, Matthias [Gutachter] / Hahn, Heidi [Gutachter]

    2023  

    Verfasserangabe Celeste Giansanti ; Gutachter: Matthias Dobbelstein, Heidi Hahn ; Betreuer: Matthias Dobbelstein
    Schlagwörter Medizin, Gesundheit ; Medicine, Health
    Thema/Rubrik (Code) sg610
    Sprache Englisch
    Verlag Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Erscheinungsort Göttingen
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
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  3. Artikel ; Online: The interplay of TARG1 and PARG protects against genomic instability.

    Groslambert, Joséphine / Prokhorova, Evgeniia / Wondisford, Anne R / Tromans-Coia, Callum / Giansanti, Celeste / Jansen, Jennifer / Timinszky, Gyula / Dobbelstein, Matthias / Ahel, Dragana / O'Sullivan, Roderick J / Ahel, Ivan

    Cell reports

    2023  Band 42, Heft 9, Seite(n) 113113

    Abstract: The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspartate/ ... ...

    Abstract The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspartate/glutamate-linked ADP-ribosylation. We reveal its function in the DNA damage response and show that the loss of TARG1 sensitizes cells to inhibitors of topoisomerase II, ATR, and PARP. Furthermore, we find a PARP1-mediated synthetic lethal interaction between TARG1 and PARG, driven by the toxic accumulation of ADP-ribosylation, that induces replication stress and genomic instability. Finally, we show that histone PARylation factor 1 (HPF1) deficiency exacerbates the toxicity and genomic instability induced by excessive ADP-ribosylation, suggesting a close crosstalk between components of the serine- and aspartate/glutamate-linked ADP-ribosylation pathways. Altogether, our data identify TARG1 as a potential biomarker for the response of cancer cells to PARP and PARG inhibition and establish that the interplay of TARG1 and PARG protects cells against genomic instability.
    Mesh-Begriff(e) Humans ; Poly(ADP-ribose) Polymerase Inhibitors/pharmacology ; Aspartic Acid/metabolism ; ADP-Ribosylation ; Genomic Instability ; Glutamates/metabolism ; Carrier Proteins/metabolism ; Nuclear Proteins/metabolism
    Chemische Substanzen Poly(ADP-ribose) Polymerase Inhibitors ; Aspartic Acid (30KYC7MIAI) ; Glutamates ; HPF1 protein, human ; Carrier Proteins ; Nuclear Proteins
    Sprache Englisch
    Erscheinungsdatum 2023-09-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113113
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: MYCN recruits the nuclear exosome complex to RNA polymerase II to prevent transcription-replication conflicts

    Papadopoulos, Dimitrios / Solvie, Daniel / Baluapuri, Apoorva / Endres, Theresa / Ha, Stefanie Anh / Herold, Steffi / Kalb, Jacqueline / Giansanti, Celeste / Schülein-Völk, Christina / Ade, Carsten Patrick / Schneider, Cornelius / Gaballa, Abdallah / Vos, Seychelle / Fischer, Utz / Dobbelstein, Matthias / Wolf, Elmar / Eilers, Martin

    Molecular cell. 2022 Jan. 06, v. 82, no. 1

    2022  

    Abstract: The MYCN oncoprotein drives the development of numerous neuroendocrine and pediatric tumors. Here we show that MYCN interacts with the nuclear RNA exosome, a 3′-5′ exoribonuclease complex, and recruits the exosome to its target genes. In the absence of ... ...

    Abstract The MYCN oncoprotein drives the development of numerous neuroendocrine and pediatric tumors. Here we show that MYCN interacts with the nuclear RNA exosome, a 3′-5′ exoribonuclease complex, and recruits the exosome to its target genes. In the absence of the exosome, MYCN-directed elongation by RNA polymerase II (RNAPII) is slow and non-productive on a large group of cell-cycle-regulated genes. During the S phase of MYCN-driven tumor cells, the exosome is required to prevent the accumulation of stalled replication forks and of double-strand breaks close to the transcription start sites. Upon depletion of the exosome, activation of ATM causes recruitment of BRCA1, which stabilizes nuclear mRNA decapping complexes, leading to MYCN-dependent transcription termination. Disruption of mRNA decapping in turn activates ATR, indicating transcription-replication conflicts. We propose that exosome recruitment by MYCN maintains productive transcription elongation during S phase and prevents transcription-replication conflicts to maintain the rapid proliferation of neuroendocrine tumor cells.
    Schlagwörter DNA-directed RNA polymerase ; exoribonucleases ; exosomes ; interphase ; neoplasms ; oncogene proteins ; transcription termination ; tumor suppressor proteins
    Sprache Englisch
    Erscheinungsverlauf 2022-0106
    Umfang p. 159-176.e12.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.11.002
    Datenquelle NAL Katalog (AGRICOLA)

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  5. Artikel ; Online: MDM2 binds and ubiquitinates PARP1 to enhance DNA replication fork progression.

    Giansanti, Celeste / Manzini, Valentina / Dickmanns, Antje / Dickmanns, Achim / Palumbieri, Maria Dilia / Sanchi, Andrea / Kienle, Simon Maria / Rieth, Sonja / Scheffner, Martin / Lopes, Massimo / Dobbelstein, Matthias

    Cell reports

    2022  Band 39, Heft 9, Seite(n) 110879

    Abstract: The MDM2 oncoprotein antagonizes the tumor suppressor p53 by physical interaction and ubiquitination. However, it also sustains the progression of DNA replication forks, even in the absence of functional p53. Here, we show that MDM2 binds, inhibits, ... ...

    Abstract The MDM2 oncoprotein antagonizes the tumor suppressor p53 by physical interaction and ubiquitination. However, it also sustains the progression of DNA replication forks, even in the absence of functional p53. Here, we show that MDM2 binds, inhibits, ubiquitinates, and destabilizes poly(ADP-ribose) polymerase 1 (PARP1). When cellular MDM2 levels are increased, this leads to accelerated progression of DNA replication forks, much like pharmacological inhibition of PARP1. Conversely, overexpressed PARP1 restores normal fork progression despite elevated MDM2. Strikingly, MDM2 profoundly reduces the frequency of fork reversal, revealed as four-way junctions through electron microscopy. Depletion of RECQ1 or the primase/polymerase (PRIMPOL) reverses the MDM2-mediated acceleration of the nascent DNA elongation rate. MDM2 also increases the occurrence of micronuclei, and it exacerbates camptothecin-induced cell death. In conclusion, high MDM2 levels phenocopy PARP inhibition in modulation of fork restart, representing a potential vulnerability of cancer cells.
    Mesh-Begriff(e) DNA/genetics ; DNA Damage ; DNA Primase/metabolism ; DNA Replication ; Tumor Suppressor Protein p53/metabolism
    Chemische Substanzen Tumor Suppressor Protein p53 ; DNA (9007-49-2) ; DNA Primase (EC 2.7.7.-)
    Sprache Englisch
    Erscheinungsdatum 2022-06-01
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2022.110879
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Mdm4 supports DNA replication in a p53-independent fashion.

    Wohlberedt, Kai / Klusmann, Ina / Derevyanko, Polina K / Henningsen, Kester / Choo, Josephine Ann Mun Yee / Manzini, Valentina / Magerhans, Anna / Giansanti, Celeste / Eischen, Christine M / Jochemsen, Aart G / Dobbelstein, Matthias

    Oncogene

    2020  Band 39, Heft 25, Seite(n) 4828–4843

    Abstract: The Mdm4 (alias MdmX) oncoprotein, like its paralogue and interaction partner Mdm2, antagonizes the tumor suppressor p53. p53-independent roles of the Mdm proteins are emerging, and we have reported the ability of Mdm2 to modify chromatin and to support ... ...

    Abstract The Mdm4 (alias MdmX) oncoprotein, like its paralogue and interaction partner Mdm2, antagonizes the tumor suppressor p53. p53-independent roles of the Mdm proteins are emerging, and we have reported the ability of Mdm2 to modify chromatin and to support DNA replication by suppressing the formation of R-loops (DNA/RNA-hybrids). We show here that the depletion of Mdm4 in p53-deficient cells compromises DNA replication fork progression as well. Among various deletion mutants, only full-length Mdm4 was able to support DNA replication fork progression. Co-depletion of Mdm4 and Mdm2 further impaired DNA replication, and the overexpression of each partially compensated for the other's loss. Despite impairing replication, Mdm4 depletion only marginally hindered cell proliferation, likely due to compensation through increased firing of replication origins. However, depleting Mdm4 sensitized p53-/- cells to the nucleoside analog gemcitabine, raising the future perspective of using Mdm4 inhibitors as chemosensitizers. Mechanistically, Mdm4 interacts with members of the Polycomb Repressor Complexes and supports the ubiquitination of H2A, thereby preventing the accumulation of DNA/RNA-hybrids. Thus, in analogy to previously reported activities of Mdm2, Mdm4 enables unperturbed DNA replication through the avoidance of R-loops.
    Mesh-Begriff(e) Animals ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; DNA Replication/genetics ; Embryo, Mammalian/cytology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Humans ; Mice, Knockout ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; RNA Interference ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
    Chemische Substanzen Cell Cycle Proteins ; MDM4 protein, human ; Mdm4 protein, mouse ; Proto-Oncogene Proteins ; Tumor Suppressor Protein p53
    Sprache Englisch
    Erscheinungsdatum 2020-05-19
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639046-8
    ISSN 1476-5594 ; 0950-9232
    ISSN (online) 1476-5594
    ISSN 0950-9232
    DOI 10.1038/s41388-020-1325-1
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2218: Hefte anzeigen Standort:
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  7. Artikel ; Online: MYCN recruits the nuclear exosome complex to RNA polymerase II to prevent transcription-replication conflicts.

    Papadopoulos, Dimitrios / Solvie, Daniel / Baluapuri, Apoorva / Endres, Theresa / Ha, Stefanie Anh / Herold, Steffi / Kalb, Jacqueline / Giansanti, Celeste / Schülein-Völk, Christina / Ade, Carsten Patrick / Schneider, Cornelius / Gaballa, Abdallah / Vos, Seychelle / Fischer, Utz / Dobbelstein, Matthias / Wolf, Elmar / Eilers, Martin

    Molecular cell

    2021  Band 82, Heft 1, Seite(n) 159–176.e12

    Abstract: The MYCN oncoprotein drives the development of numerous neuroendocrine and pediatric tumors. Here we show that MYCN interacts with the nuclear RNA exosome, a 3'-5' exoribonuclease complex, and recruits the exosome to its target genes. In the absence of ... ...

    Abstract The MYCN oncoprotein drives the development of numerous neuroendocrine and pediatric tumors. Here we show that MYCN interacts with the nuclear RNA exosome, a 3'-5' exoribonuclease complex, and recruits the exosome to its target genes. In the absence of the exosome, MYCN-directed elongation by RNA polymerase II (RNAPII) is slow and non-productive on a large group of cell-cycle-regulated genes. During the S phase of MYCN-driven tumor cells, the exosome is required to prevent the accumulation of stalled replication forks and of double-strand breaks close to the transcription start sites. Upon depletion of the exosome, activation of ATM causes recruitment of BRCA1, which stabilizes nuclear mRNA decapping complexes, leading to MYCN-dependent transcription termination. Disruption of mRNA decapping in turn activates ATR, indicating transcription-replication conflicts. We propose that exosome recruitment by MYCN maintains productive transcription elongation during S phase and prevents transcription-replication conflicts to maintain the rapid proliferation of neuroendocrine tumor cells.
    Mesh-Begriff(e) Animals ; Ataxia Telangiectasia Mutated Proteins/genetics ; Ataxia Telangiectasia Mutated Proteins/metabolism ; BRCA1 Protein/genetics ; BRCA1 Protein/metabolism ; Cell Line, Tumor ; Cell Nucleus/enzymology ; Cell Nucleus/genetics ; Cell Proliferation ; DNA Breaks, Double-Stranded ; DNA Replication ; Exoribonucleases/genetics ; Exoribonucleases/metabolism ; Exosomes/enzymology ; Exosomes/genetics ; Female ; Gene Expression Regulation, Neoplastic ; HEK293 Cells ; Humans ; Male ; Mice ; N-Myc Proto-Oncogene Protein/genetics ; N-Myc Proto-Oncogene Protein/metabolism ; NIH 3T3 Cells ; Neuroblastoma/enzymology ; Neuroblastoma/genetics ; Neuroblastoma/pathology ; Promoter Regions, Genetic ; RNA Caps/genetics ; RNA Caps/metabolism ; RNA Polymerase II/genetics ; RNA Polymerase II/metabolism ; Transcription Termination, Genetic ; Transcription, Genetic
    Chemische Substanzen BRCA1 Protein ; BRCA1 protein, human ; MYCN protein, human ; N-Myc Proto-Oncogene Protein ; RNA Caps ; ATM protein, human (EC 2.7.11.1) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; RNA Polymerase II (EC 2.7.7.-) ; Exoribonucleases (EC 3.1.-)
    Sprache Englisch
    Erscheinungsdatum 2021-11-29
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.11.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: MYC multimers shield stalled replication forks from RNA polymerase.

    Solvie, Daniel / Baluapuri, Apoorva / Uhl, Leonie / Fleischhauer, Daniel / Endres, Theresa / Papadopoulos, Dimitrios / Aziba, Amel / Gaballa, Abdallah / Mikicic, Ivan / Isaakova, Ekaterina / Giansanti, Celeste / Jansen, Jennifer / Jungblut, Marvin / Klein, Teresa / Schülein-Völk, Christina / Maric, Hans / Doose, Sören / Sauer, Markus / Beli, Petra /
    Rosenwald, Andreas / Dobbelstein, Matthias / Wolf, Elmar / Eilers, Martin

    Nature

    2022  Band 612, Heft 7938, Seite(n) 148–155

    Abstract: Oncoproteins of the MYC family drive the development of numerous human ... ...

    Abstract Oncoproteins of the MYC family drive the development of numerous human tumours
    Mesh-Begriff(e) Humans ; Chromatin/genetics ; DNA-Directed RNA Polymerases/metabolism ; Promoter Regions, Genetic/genetics ; RNA Polymerase II/metabolism ; Transcription, Genetic ; Tumor Suppressor Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism ; DNA Breaks, Double-Stranded ; S Phase ; Binding Sites ; RNA, Messenger/biosynthesis
    Chemische Substanzen Chromatin ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; HUWE1 protein, human (EC 2.3.2.26) ; RNA Polymerase II (EC 2.7.7.-) ; Tumor Suppressor Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; MYC protein, human ; BRCA1 protein, human ; FANCD2 protein, human ; ATR protein, human (EC 2.7.11.1) ; RNA, Messenger
    Sprache Englisch
    Erscheinungsdatum 2022-11-23
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05469-4
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  9. Artikel ; Online: Combined inhibition of Aurora-A and ATR kinase results in regression of

    Roeschert, Isabelle / Poon, Evon / Henssen, Anton G / Garcia, Heathcliff Dorado / Gatti, Marco / Giansanti, Celeste / Jamin, Yann / Ade, Carsten P / Gallant, Peter / Schülein-Völk, Christina / Beli, Petra / Richards, Mark / Rosenfeldt, Mathias / Altmeyer, Matthias / Anderson, John / Eggert, Angelika / Dobbelstein, Matthias / Bayliss, Richard / Chesler, Louis /
    Büchel, Gabriele / Eilers, Martin

    Nature cancer

    2021  Band 2, Heft 3, Seite(n) 312–326

    Abstract: Amplification ... ...

    Abstract Amplification of
    Mesh-Begriff(e) Animals ; Apoptosis/genetics ; Aurora Kinase A/genetics ; Cell Line, Tumor ; Mice ; N-Myc Proto-Oncogene Protein/genetics ; Neuroblastoma/drug therapy
    Chemische Substanzen N-Myc Proto-Oncogene Protein ; Aurora Kinase A (EC 2.7.11.1)
    Sprache Englisch
    Erscheinungsdatum 2021-02-11
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2662-1347
    ISSN (online) 2662-1347
    DOI 10.1038/s43018-020-00171-8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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