ArticleActa crystallographica. Section D, Structural biology2016
UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.
Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- RBM39 modulates UPR signaling through alternative splicing of IRE1α/Genes & development · 2026Article
- Exploitation of host U2AF1 and U2AF2 splicing factors facilitates mosquito-borne orthoflavivirus infection across species.Nucleic acids research · 2026Article
- RNA-coupled CRISPR screens reveal ZNF207 as a regulator of LMNA aberrant splicing in progeria.Molecular cell · 2026Article
- Targeting the RBM39-MEK5 axis synergizes with bortezomib to inhibit the malignant growth of multiple myeloma.Blood advances · 2025Article
- The RBM39 degrader indisulam inhibits acute megakaryoblastic leukemia by altering the alternative splicing of ZMYND8.Cell & bioscience · 2025Article
- Recent advances in anticancer mechanisms of molecular glue degraders: focus on RBM39-dgrading synthetic sulfonamide such as indisulam, E7820, tasisulam, and chloroquinoxaline sulfonamide.Genes & genomics · 2024Review
- Molecular basis of RNA-binding and autoregulation by the cancer-associated splicing factor RBM39.Nature communications · 2023Article
- Therapeutic Targeting of RNA Splicing in Cancer.Genes · 2023Review
- RNA splicing dysregulation and the hallmarks of cancer.Nature reviews. Cancer · 2023Review
- Pre-mRNA splicing-associated diseases and therapies.RNA biology · 2023Review
- The identification of protein and RNA interactors of the splicing factor Caper in the adultFrontiers in molecular neuroscience · 2023Article
- The transcription factor c-Jun inhibits RBM39 to reprogram pre-mRNA splicing during genotoxic stress.Nucleic acids research · 2022Article
- Systematic pan-cancer analysis identifies RBM39 as an immunological and prognostic biomarker.Journal of cellular and molecular medicine · 2022Article
- Genetic and compound screens uncover factors modulating cancer cell response to indisulam.Life science alliance · 2022Article
- Indisulam targets RNA splicing and metabolism to serve as a therapeutic strategy for high-risk neuroblastoma.Nature communications · 2022Article
- An Unusual U2AF2 Inhibits Splicing and Attenuates the Virulence of the Human Protozoan ParasiteFrontiers in cellular and infection microbiology · 2022Article
- Targeting the spliceosome through RBM39 degradation results in exceptional responses in high-risk neuroblastoma models.Science advances · 2021Article
- RNA-binding protein 39: a promising therapeutic target for cancer.Cell death discovery · 2021Review
- Biology of the mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities.International journal of molecular sciences · 2021Review
- RBM39 Alters Phosphorylation of c-Jun and Binds to Viral RNA to Promote PRRSV Proliferation.Frontiers in immunology · 2021Article
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Authors and funding
17 authors at 6 institutions in 1 country.
Funding
Abstract
RNA-binding protein 39 (RBM39) is a splicing factor and a transcriptional co-activator of estrogen receptors and Jun/AP-1, and its function has been associated with malignant progression in a number of cancers. The C-terminal RRM domain of RBM39 belongs to the U2AF homology motif family (UHM), which mediate protein-protein interactions through a short tryptophan-containing peptide known as the UHM-ligand motif (ULM). Here, crystal and solution NMR structures of the RBM39-UHM domain, and the crystal structure of its complex with U2AF65-ULM, are reported. The RBM39-U2AF65 interaction was confirmed by co-immunoprecipitation from human cell extracts, by isothermal titration calorimetry and by NMR chemical shift perturbation experiments with the purified proteins. When compared with related complexes, such as U2AF35-U2AF65 and RBM39-SF3b155, the RBM39-UHM-U2AF65-ULM complex reveals both common and discriminating recognition elements in the UHM-ULM binding interface, providing a rationale for the known specificity of UHM-ULM interactions. This study therefore establishes a structural basis for specific UHM-ULM interactions by splicing factors such as U2AF35, U2AF65, RBM39 and SF3b155, and a platform for continued studies of intermolecular interactions governing disease-related alternative splicing in eukaryotic cells.
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