TRIP13 regulates DNA repair pathway choice through REV7 conformational change

DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53B...

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Vydáno v:Nature cell biology Ročník 22; číslo 1; s. 87 - 96
Hlavní autoři: Clairmont, Connor S, Sarangi, Prabha, Ponnienselvan, Karthikeyan, Galli, Lucas D, Csete, Isabelle, Moreau, Lisa, Adelmant, Guillaume, Chowdhury, Dipanjan, Marto, Jarrod A, D'Andrea, Alan D
Médium: Journal Article
Jazyk:angličtina
Vydáno: England Nature Publishing Group 01.01.2020
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ISSN:1465-7392, 1476-4679, 1476-4679
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Abstract DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53BP1, RIF1, REV7-Shieldin (SHLD1-3) or CST-DNA polymerase alpha (Pol-α) in BRCA1-deficient cells restores HDR and PARPi resistance. Here, we identify the TRIP13 ATPase as a negative regulator of REV7. We show that REV7 exists in active 'closed' and inactive 'open' conformations, and TRIP13 catalyses the inactivating conformational change, thereby dissociating REV7-Shieldin to promote HDR. TRIP13 similarly disassembles the REV7-REV3 translesion synthesis (TLS) complex, a component of the Fanconi anaemia pathway, inhibiting error-prone replicative lesion bypass and interstrand crosslink repair. Importantly, TRIP13 overexpression is common in BRCA1-deficient cancers, confers PARPi resistance and correlates with poor prognosis. Thus, TRIP13 emerges as an important regulator of DNA repair pathway choice-promoting HDR, while suppressing NHEJ and TLS.
AbstractList DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53BP1, RIF1, REV7-Shieldin (SHLD1-3) or CST-DNA polymerase alpha (Pol-α) in BRCA1-deficient cells restores HDR and PARPi resistance. Here, we identify the TRIP13 ATPase as a negative regulator of REV7. We show that REV7 exists in active 'closed' and inactive 'open' conformations, and TRIP13 catalyses the inactivating conformational change, thereby dissociating REV7-Shieldin to promote HDR. TRIP13 similarly disassembles the REV7-REV3 translesion synthesis (TLS) complex, a component of the Fanconi anaemia pathway, inhibiting error-prone replicative lesion bypass and interstrand crosslink repair. Importantly, TRIP13 overexpression is common in BRCA1-deficient cancers, confers PARPi resistance and correlates with poor prognosis. Thus, TRIP13 emerges as an important regulator of DNA repair pathway choice-promoting HDR, while suppressing NHEJ and TLS.DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53BP1, RIF1, REV7-Shieldin (SHLD1-3) or CST-DNA polymerase alpha (Pol-α) in BRCA1-deficient cells restores HDR and PARPi resistance. Here, we identify the TRIP13 ATPase as a negative regulator of REV7. We show that REV7 exists in active 'closed' and inactive 'open' conformations, and TRIP13 catalyses the inactivating conformational change, thereby dissociating REV7-Shieldin to promote HDR. TRIP13 similarly disassembles the REV7-REV3 translesion synthesis (TLS) complex, a component of the Fanconi anaemia pathway, inhibiting error-prone replicative lesion bypass and interstrand crosslink repair. Importantly, TRIP13 overexpression is common in BRCA1-deficient cancers, confers PARPi resistance and correlates with poor prognosis. Thus, TRIP13 emerges as an important regulator of DNA repair pathway choice-promoting HDR, while suppressing NHEJ and TLS.
DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53BP1, RIF1, REV7-Shieldin (SHLD1-3) or CST-DNA polymerase alpha (Pol-α) in BRCA1-deficient cells restores HDR and PARPi resistance. Here, we identify the TRIP13 ATPase as a negative regulator of REV7. We show that REV7 exists in active 'closed' and inactive 'open' conformations, and TRIP13 catalyses the inactivating conformational change, thereby dissociating REV7-Shieldin to promote HDR. TRIP13 similarly disassembles the REV7-REV3 translesion synthesis (TLS) complex, a component of the Fanconi anaemia pathway, inhibiting error-prone replicative lesion bypass and interstrand crosslink repair. Importantly, TRIP13 overexpression is common in BRCA1-deficient cancers, confers PARPi resistance and correlates with poor prognosis. Thus, TRIP13 emerges as an important regulator of DNA repair pathway choice-promoting HDR, while suppressing NHEJ and TLS.
DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot perform HDR, conferring sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPi). However, concomitant loss of the pro-NHEJ factors 53BP1, RIF1, REV7–Shieldin (SHLD1–3) or CST–DNA polymerase alpha (Pol-α) in BRCA1-deficient cells restores HDR and PARPi resistance. Here, we identify the TRIP13 ATPase as a negative regulator of REV7. We show that REV7 exists in active ‘closed’ and inactive ‘open’ conformations, and TRIP13 catalyses the inactivating conformational change, thereby dissociating REV7–Shieldin to promote HDR. TRIP13 similarly disassembles the REV7–REV3 translesion synthesis (TLS) complex, a component of the Fanconi anaemia pathway, inhibiting error-prone replicative lesion bypass and interstrand crosslink repair. Importantly, TRIP13 overexpression is common in BRCA1-deficient cancers, confers PARPi resistance and correlates with poor prognosis. Thus, TRIP13 emerges as an important regulator of DNA repair pathway choice—promoting HDR, while suppressing NHEJ and TLS.Clairmont et al. find that the TRIP13 ATPase regulates REV7–Shieldin dissociation to promote homology-directed repair and suppress non-homologous end joining, and show the importance of PARPi resistance in BRCA1-deficient cancers.
Author Galli, Lucas D
Chowdhury, Dipanjan
Csete, Isabelle
Adelmant, Guillaume
Marto, Jarrod A
Sarangi, Prabha
D'Andrea, Alan D
Clairmont, Connor S
Ponnienselvan, Karthikeyan
Moreau, Lisa
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  fullname: Ponnienselvan, Karthikeyan
  organization: Department of Radiation Oncology, Dana-Farber Cancer Institute, Boston, MA, USA
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  surname: Galli
  fullname: Galli, Lucas D
  organization: Department of Radiation Oncology, Dana-Farber Cancer Institute, Boston, MA, USA
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  surname: Csete
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  organization: Department of Radiation Oncology, Dana-Farber Cancer Institute, Boston, MA, USA
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  surname: Moreau
  fullname: Moreau, Lisa
  organization: Department of Radiation Oncology, Dana-Farber Cancer Institute, Boston, MA, USA
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  orcidid: 0000-0003-4075-5486
  surname: Adelmant
  fullname: Adelmant, Guillaume
  organization: Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA
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  orcidid: 0000-0001-5645-3752
  surname: Chowdhury
  fullname: Chowdhury, Dipanjan
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  givenname: Jarrod A
  orcidid: 0000-0003-2086-1134
  surname: Marto
  fullname: Marto, Jarrod A
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  fullname: D'Andrea, Alan D
  email: Alan_Dandrea@dfci.harvard.edu, Alan_Dandrea@dfci.harvard.edu
  organization: Center for DNA Damage and Repair, Dana-Farber Cancer Institute, Boston, MA, USA. Alan_Dandrea@dfci.harvard.edu
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31915374$$D View this record in MEDLINE/PubMed
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OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/7336368
PMID 31915374
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PublicationDate 2020-01-01
PublicationDateYYYYMMDD 2020-01-01
PublicationDate_xml – month: 01
  year: 2020
  text: 2020-01-01
  day: 01
PublicationDecade 2020
PublicationPlace England
PublicationPlace_xml – name: England
– name: London
PublicationTitle Nature cell biology
PublicationTitleAlternate Nat Cell Biol
PublicationYear 2020
Publisher Nature Publishing Group
Publisher_xml – name: Nature Publishing Group
References 33122436 - Proc Natl Acad Sci U S A. 2020 Nov 10;117(45):27761-27763
References_xml – reference: 33122436 - Proc Natl Acad Sci U S A. 2020 Nov 10;117(45):27761-27763
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Snippet DNA double-strand breaks (DSBs) are repaired through homology-directed repair (HDR) or non-homologous end joining (NHEJ). BRCA1/2-deficient cancer cells cannot...
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StartPage 87
SubjectTerms Adenosine diphosphate
Adenosine triphosphatase
Anemia
ATPases Associated with Diverse Cellular Activities - drug effects
ATPases Associated with Diverse Cellular Activities - genetics
BRCA1 protein
BRCA1 Protein - deficiency
Breast cancer
Cell Cycle Proteins - drug effects
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Crosslinking
Deoxyribonucleic acid
Dismantling
DNA
DNA damage
DNA Damage - drug effects
DNA End-Joining Repair - genetics
DNA polymerase
DNA repair
DNA Repair - drug effects
DNA Repair - genetics
DNA Replication - drug effects
DNA Replication - genetics
DNA-directed DNA polymerase
Homology
Humans
Mad2 Proteins - genetics
Non-homologous end joining
Poly(ADP-ribose)
Poly(ADP-ribose) polymerase
Poly(ADP-ribose) Polymerase Inhibitors - pharmacology
Recombinational DNA Repair - genetics
Repair
Ribose
Telomere-Binding Proteins - drug effects
Telomere-Binding Proteins - genetics
Title TRIP13 regulates DNA repair pathway choice through REV7 conformational change
URI https://www.ncbi.nlm.nih.gov/pubmed/31915374
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Volume 22
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