ArticleThe Journal of biological chemistry2020
Structural basis for shieldin complex subunit 3-mediated recruitment of the checkpoint protein REV7 during DNA double-strand break repair.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- Probing hot spots of protein-protein interactions mediated by the safety-belt region of REV7.Structure (London, England : 1993) · 2024Article
- REV7: a small but mighty regulator of genome maintenance and cancer development.Frontiers in oncology · 2024Review
- An AlphaFold2 map of the 53BP1 pathway identifies a direct SHLD3-RIF1 interaction critical for shieldin activity.EMBO reports · 2023Article
- Shieldin complex assembly kinetics and DNA binding by SHLD3.Communications biology · 2023Article
- Changes in Ploidy Drive Reproduction Transition and Genomic Diversity in a Polyploid Fish Complex.Molecular biology and evolution · 2022Article
- Review
- Genetic Variants in Double-Strand Break Repair Pathway Genes to Predict Platinum-Based Chemotherapy Prognosis in Patients With Lung Cancer.Frontiers in pharmacology · 2022Article
- REV7 directs DNA repair pathway choice.Trends in cell biology · 2021Review
- MAD2L2 dimerization and TRIP13 control shieldin activity in DNA repair.Nature communications · 2021Article
- REV7: Jack of many trades.Trends in cell biology · 2021Review
- The dystonia gene THAP1 controls DNA double-strand break repair choice.Molecular cell · 2021Article
- Molecular mechanisms of assembly and TRIP13-mediated remodeling of the human Shieldin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Regulation of DNA double-strand break repair pathway choice: a new focus on 53BP1.Journal of Zhejiang University. Science. B · 2021Review
- p31Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Disassembly of the Shieldin Complex by TRIP13.Cell cycle (Georgetown, Tex.) · 2020Review
- REV7 is required for processing AID initiated DNA lesions in activated B cells.Nature communications · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Shieldin complex subunit 3 (SHLD3) is the apical subunit of a recently-identified shieldin complex and plays a critical role in DNA double-strand break repair. To fulfill its function in DNA repair, SHLD3 interacts with the mitotic spindle assembly checkpoint protein REV7 homolog (REV7), but the details of this interaction remain obscure. Here, we present the crystal structures of REV7 in complex with SHLD3's REV7-binding domain (RBD) at 2.2-2.3 Å resolutions. The structures revealed that the ladle-shaped RBD in SHLD3 uses its N-terminal loop and C-terminal α-helix (αC-helix) in its interaction with REV7. The N-terminal loop exhibited a structure similar to those previously identified in other REV7-binding proteins, and the less-conserved αC-helix region adopted a distinct mode for binding REV7.
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