ArticleCell biology international2025
DRIM modulates Src activation and regulates angiogenic functions in vascular endothelial cells.
Article in Cell biology international, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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Who cites it
3 citing papers in PubMed.
- CD95 ligand drives abdominal aortic aneurysm progression through Caspase-8-mediated GSDMD-dependent endothelial pyroptosis: modulation by SRC kinase.Apoptosis : an international journal on programmed cell death · 2026Article
- DRIM modulates Src activation and regulates angiogenic functions in vascular endothelial cells.Cell biology international · 2025Article
- Ribosome biogenesis-related gene signature predicts prognosis and immune landscape in glioma and identifies UTP20 as a therapeutic target.Frontiers in immunology · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Downregulated in Metastasis Protein (DRIM) was discovered in malignant epithelial cells and was thought to be mainly a nucleus protein affecting cancer cells. Recent single-cell sequencing analysis suggests that DRIM is abundantly expressed in vascular endothelial cells. There has been no knowledge of the role of DRIM in the endothelium. In the present study, using protein fraction method and cell imaging, we identified that the DRIM protein was abundantly present in both nucleus and the cytoskeletal fractions of human vascular endothelial cells. Knockdown of DRIM in the endothelial cells significantly affected growth, migration, and angiogenic tubule formation. Proteomics analyses revealed that Src was an important direct target protein of DRIM, a finding further confirmed by protein interaction assay. Silencing DRIM activated the tyrosine 419 site phosphorylation of Src kinase in endothelial cells, thereby affecting the downstream proteins of Src including p-FAK and p-STAT3, and exerting biological effects. To conclude, our results provide evidence of DRIM being a nuclear and cytoskeletal-associated protein, having a novel key role of the protein in vascular endothelial cells.
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