DHX9 SUMOylation is required for the suppression of R-loop-associated genome instability Article Swipe
YOU?
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· 2024
· Open Access
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· DOI: https://doi.org/10.1038/s41467-024-50428-4
RNA helicase DHX9 is essential for genome stability by resolving aberrant R-loops. However, its regulatory mechanisms remain unclear. Here we show that SUMOylation at lysine 120 (K120) is crucial for DHX9 function. Preventing SUMOylation at K120 leads to R-loop dysregulation, increased DNA damage, and cell death. Cells expressing DHX9 K120R mutant which cannot be SUMOylated are more sensitive to genotoxic agents and this sensitivity is mitigated by RNase H overexpression. Unlike the mutant, wild-type DHX9 interacts with R-loop-associated proteins such as PARP1 and DDX21 via SUMO-interacting motifs. Fusion of SUMO2 to the DHX9 K120R mutant enhances its association with these proteins, reduces R-loop accumulation, and alleviates survival defects of DHX9 K120R. Our findings highlight the critical role of DHX9 SUMOylation in maintaining genome stability by regulating protein interactions necessary for R-loop balance.
Related Topics
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-024-50428-4
- https://www.nature.com/articles/s41467-024-50428-4.pdf
- OA Status
- gold
- Cited By
- 14
- References
- 70
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4400737869
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4400737869Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41467-024-50428-4Digital Object Identifier
- Title
-
DHX9 SUMOylation is required for the suppression of R-loop-associated genome instabilityWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-07-17Full publication date if available
- Authors
-
Bing-Ze Yang, Mei-Yin Liu, K. Chiu, Yuh-Ling Chien, Ching-An Cheng, Yulin Chen, Li-Yu Tsui, Keng-Ru Lin, Hsueh‐Ping Chu, Ching-Shyi WuList of authors in order
- Landing page
-
https://doi.org/10.1038/s41467-024-50428-4Publisher landing page
- PDF URL
-
https://www.nature.com/articles/s41467-024-50428-4.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s41467-024-50428-4.pdfDirect OA link when available
- Concepts
-
SUMO protein, Helicase, RNA Helicase A, Cell biology, Biology, Mutant, Genome instability, Genetics, RNA, DNA, DNA damage, Gene, UbiquitinTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
14Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 14Per-year citation counts (last 5 years)
- References (count)
-
70Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.which | 52 |
| abstract_inverted_index.(K120) | 27 |
| abstract_inverted_index.Fusion | 88 |
| abstract_inverted_index.K120R. | 111 |
| abstract_inverted_index.R-loop | 39, 103, 131 |
| abstract_inverted_index.Unlike | 71 |
| abstract_inverted_index.agents | 61 |
| abstract_inverted_index.cannot | 53 |
| abstract_inverted_index.death. | 46 |
| abstract_inverted_index.genome | 7, 123 |
| abstract_inverted_index.lysine | 25 |
| abstract_inverted_index.mutant | 51, 95 |
| abstract_inverted_index.remain | 17 |
| abstract_inverted_index.crucial | 29 |
| abstract_inverted_index.damage, | 43 |
| abstract_inverted_index.defects | 108 |
| abstract_inverted_index.motifs. | 87 |
| abstract_inverted_index.mutant, | 73 |
| abstract_inverted_index.protein | 127 |
| abstract_inverted_index.reduces | 102 |
| abstract_inverted_index.Abstract | 0 |
| abstract_inverted_index.However, | 13 |
| abstract_inverted_index.R-loops. | 12 |
| abstract_inverted_index.aberrant | 11 |
| abstract_inverted_index.balance. | 132 |
| abstract_inverted_index.critical | 116 |
| abstract_inverted_index.enhances | 96 |
| abstract_inverted_index.findings | 113 |
| abstract_inverted_index.helicase | 2 |
| abstract_inverted_index.proteins | 79 |
| abstract_inverted_index.survival | 107 |
| abstract_inverted_index.unclear. | 18 |
| abstract_inverted_index.essential | 5 |
| abstract_inverted_index.function. | 32 |
| abstract_inverted_index.genotoxic | 60 |
| abstract_inverted_index.highlight | 114 |
| abstract_inverted_index.increased | 41 |
| abstract_inverted_index.interacts | 76 |
| abstract_inverted_index.mitigated | 66 |
| abstract_inverted_index.necessary | 129 |
| abstract_inverted_index.proteins, | 101 |
| abstract_inverted_index.resolving | 10 |
| abstract_inverted_index.sensitive | 58 |
| abstract_inverted_index.stability | 8, 124 |
| abstract_inverted_index.wild-type | 74 |
| abstract_inverted_index.Preventing | 33 |
| abstract_inverted_index.SUMOylated | 55 |
| abstract_inverted_index.alleviates | 106 |
| abstract_inverted_index.expressing | 48 |
| abstract_inverted_index.mechanisms | 16 |
| abstract_inverted_index.regulating | 126 |
| abstract_inverted_index.regulatory | 15 |
| abstract_inverted_index.SUMOylation | 23, 34, 120 |
| abstract_inverted_index.association | 98 |
| abstract_inverted_index.maintaining | 122 |
| abstract_inverted_index.sensitivity | 64 |
| abstract_inverted_index.interactions | 128 |
| abstract_inverted_index.accumulation, | 104 |
| abstract_inverted_index.dysregulation, | 40 |
| abstract_inverted_index.overexpression. | 70 |
| abstract_inverted_index.SUMO-interacting | 86 |
| abstract_inverted_index.R-loop-associated | 78 |
| cited_by_percentile_year.max | 100 |
| cited_by_percentile_year.min | 99 |
| countries_distinct_count | 1 |
| institutions_distinct_count | 10 |
| citation_normalized_percentile.value | 0.95308472 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | True |