ArticleMolecular biology of the cell1999
The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn).
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed, 192 citations in OpenAlex.
- Article
- Non-receptor tyrosine kinase signaling pathways and therapeutic implications.Signal transduction and targeted therapy · 2026Review
- NNature reviews. Cancer · 2026Review
- Human papillomavirus 16 E6 oncoprotein promotes up-regulation of RNA-binding protein Sam68 in head and neck cancer.Frontiers in microbiology · 2026Article
- mActa pharmaceutica Sinica. B · 2025Review
- An Investigation of the RNA Modification mInternational journal of molecular sciences · 2025Article
- Interplay between hypoxia, RNA methylation, and HPV in head and neck squamous cell carcinomas: drivers of oncogenesis and resistance to therapy.EXCLI journal · 2025Review
- The role of N(6)-methyladenosine (m6a) modification in cancer: recent advances and future directions.EXCLI journal · 2025Review
- The three YTHDF paralogs and VIRMA are strong cross-histotype tumor driver candidates among mNAR cancer · 2024Article
- NMolecular medicine (Cambridge, Mass.) · 2024Review
- Regulatory roles of N6-methyladenosine (mCancer gene therapy · 2024Review
- Reading the mCell & bioscience · 2024Review
- The YTH domain-containing protein family: Emerging players in immunomodulation and tumour immunotherapy targets.Clinical and translational medicine · 2024Review
- The YTHDF proteins display distinct cellular functions on mTrends in biochemical sciences · 2024Review
- Genome-Wide Identification and Expression Analysis ofInternational journal of molecular sciences · 2024Article
- Sam68 is a druggable vulnerability point in cancer stem cells.Cancer metastasis reviews · 2024Review
- The mFrontiers in pharmacology · 2024Review
- The Proteins of mRNA Modification: Writers, Readers, and Erasers.Annual review of biochemistry · 2023Review
- Genome-Wide Identification and Evolutionary Analysis ofPlants (Basel, Switzerland) · 2023Article
- Structural and dynamic properties of the YTH domain in complex with NQuantitative biology (Beijing, China) · 2023Article
41 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Alternative pre-mRNA splicing patterns can change an extracellular stimulus, but the signaling pathways leading to these changes are still poorly characterized. Here, we describe a tyrosine-phosphorylated nuclear protein, YT521-B, and show that it interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. Northern blot analysis demonstrated ubiquitous expression, but detailed RNA in situ analysis revealed cell type specificity in the brain. YT521-B protein is localized in the nucleoplasm and concentrated in 5-20 large nuclear dots. Deletion analysis demonstrated that the formation of these dots depends on the presence of the amino-terminal glutamic acid-rich domain and the carboxyl-terminal glutamic acid/arginine-rich region. We show that the latter comprises an important protein-protein interaction domain. The Src family kinase p59(fyn)-mediated tyrosine phosphorylation of Sam68 negatively regulates its association with YT521-B, and overexpression of p59(fyn) dissolves nuclear dots containing YT521-B. In vivo splicing assays demonstrated that YT521-B modulates alternative splice site selection in a concentration-dependent manner. Together, our data indicate that YT521-B and Sam68 may be part of a signal transduction pathway that influences splice site selection.
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