ArticleDiscover oncology2026
Phosphoproteome landscape of ARID1A and its implications in DNA damage response and breast cancer pathogenesis.
Article in Discover oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Cyclins and Cyclin-Dependent Kinases: Structure, Biological Functions, and Innovative Targeting Strategies in Cancer.MedComm · 2026Review
- SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026Review
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
ARID1A, a subunit of the SWI/SNF chromatin-remodeling complex, plays a critical role in maintaining genomic stability and regulating estrogen receptor (ER) signaling, yet its phosphorylation dynamics in cancer remain underexplored. This study employed phosphoproteomic analysis to investigate ARID1A phosphorylation in breast cancer, identifying predominant phosphosites-S363, S1184, and S696-regulated by kinases such as MAPK14, CDK16, and MAPK9. Functional enrichment revealed ARID1A interactions with SWI/SNF components (e.g., PBRM1, SMARCC2, BRD9) and DNA damage response (DDR) proteins (e.g., TP53BP1, TOP2A, CHEK2, NBN), underscoring its dual role in chromatin remodeling and double-strand break repair. Notably, phosphorylation at S363 and S1184 was significantly upregulated in breast cancer, suggesting tumour-specific hyperphosphorylation that may disrupt ARID1A tumour-suppressive function and contribute to endocrine resistance. Dysregulation of these phosphorylation events correlated with enhanced MAPK signaling, cancer progression, and poor prognosis. These findings position ARID1A as a molecular hub linking chromatin dynamics to genome integrity, with implications for therapeutic resistance. Targeting ARID1A phosphorylation pathways, potentially via MAPK inhibitors or BRD4/BRD9 antagonists, could restore its suppressive activity and improve treatment outcomes in breast cancer. This study enhances our understanding of ARID1A regulatory mechanisms, highlighting its phosphorylation as a key driver of breast cancer biology. Future research should validate these kinase-substrate interactions and explore their transcriptional and chromatin-level impacts to develop precision therapies for ARID1A-dysregulated cancers.
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Registered trials
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