ArticleMolecular cell2025
The phenylalanine-and-glycine repeats of NUP98 oncofusions form condensates that selectively partition transcriptional coactivators.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Nucleoporins in Cancer: Functional Roles and Therapeutic Opportunities.Cancer discovery · 2026Article
- BRD4: From molecular understanding to therapeutics development.Molecular cell · 2026Review
- Condensates in fusion oncoprotein-driven leukemia: new biology and therapeutic opportunities.Trends in cancer · 2026Review
- An EZH2-SREBP2 axis promotes cholesterol biosynthesis and represents a noncanonical vulnerability in tumorigenesis.Nature cell biology · 2026Article
- Beyond nuclear export: chromatin-bound XPO1/CRM1 as a transcriptional scaffold.International journal of hematology · 2026Review
- Liquid-Liquid Phase Separation (LLPS) in Tumor Biology: Special Focus on the Process of Transcription.International journal of molecular sciences · 2026Review
- A Unified Model: Chromatin-Bound Multicomponent Condensates.Cancer research · 2026Article
- Preferential formation of NUP98-KDM5A condensates at specific H3K4me3-rich loci drives leukemogenic gene expression.bioRxiv : the preprint server for biology · 2026Article
- Proteasomal control of transcription factors: mechanisms, regulation and dysregulation.Cellular and molecular life sciences : CMLS · 2026Review
- Deregulated enhancer-promoter communication in cancer through altered nuclear architecture.International journal of cancer · 2026Review
- Identification and validation of SUMOylation-related key genes for osteoarthritis through integration of single-cell, bulk RNA sequencing and animal model experiments.Frontiers in medicine · 2026Article
- Protein codes and mobility together shape cellular function and disease.Trends in biochemical sciences · 2026Review
- Co-condensation between transcription factor and cBAF selectively modulates chromatin remodeling and gene expression.Nature communications · 2025Article
- Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition.Nature structural & molecular biology · 2025Article
- Transcriptional condensates and the nuclear pore complex regulate gene expression and 3D genome architecture in response to stress.Biochemical Society transactions · 2025Review
- Sequence-based prediction of condensate composition reveals that specificity can emerge from multivalent interactions among disordered regions.Communications chemistry · 2025Article
- Sequence-based prediction of condensate composition reveals that specificity can emerge from multivalent interactions among disordered regions.bioRxiv : the preprint server for biology · 2025Article
- Article
- Liquid-liquid phase separation in normal hematopoiesis and hematological diseases.Cell and tissue research · 2025Review
- BAHCC1 binds H4K20me1 to facilitate the MCM complex loading and DNA replication.Nature communications · 2025Article
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12 authors.
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Abstract
Recurrent cancer-causing fusions of NUP98 produce higher-order assemblies known as condensates. How NUP98 oncofusion-driven condensates activate oncogenes remains poorly understood. Here, we investigate NUP98-PHF23, a leukemogenic chimera of the disordered phenylalanine-and-glycine (FG)-repeat-rich region of NUP98 and the H3K4me3/2-binding plant homeodomain (PHD) finger domain of PHF23. Our integrated analyses using mutagenesis, proteomics, genomics, and condensate reconstitution demonstrate that the PHD domain targets condensate to the H3K4me3/2-demarcated developmental genes, while FG repeats determine the condensate composition and gene activation. FG repeats are necessary to form condensates that partition a specific set of transcriptional regulators, notably the KMT2/MLL H3K4 methyltransferases, histone acetyltransferases, and BRD4. FG repeats are sufficient to partition transcriptional regulators and activate a reporter when tethered to a genomic locus. NUP98-PHF23 assembles the chromatin-bound condensates that partition multiple positive regulators, initiating a feedforward loop of reading-and-writing the active histone modifications. This network of interactions enforces an open chromatin landscape at proto-oncogenes, thereby driving cancerous transcriptional programs.
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