ArticleThe Journal of biological chemistry2011
The RNA binding motif protein 15B (RBM15B/OTT3) is a functional competitor of serine-arginine (SR) proteins and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- RBM15B recognizes H3K79me2 to guide selective mThe EMBO journal · 2026Article
- Why does the m6A writer complex require so many proteins?PLoS biology · 2025Review
- Global Co-regulatory Cross Talk Between mMolecular neurobiology · 2025Article
- M6A RNA modification: focusing on non-small cell lung cancer progression, therapeutic strategies and challenges.Frontiers in oncology · 2025Review
- CDK11 requires a critical activator SAP30BP to regulate pre-mRNA splicing.The EMBO journal · 2023Article
- Prognostic value of comprehensive typing based on m6A and gene cluster in TNBC.Journal of cancer research and clinical oncology · 2023Article
- SPOC domain proteins in health and disease.Genes & development · 2023Review
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- NFrontiers in immunology · 2022Article
- CDK11 Loss Induces Cell Cycle Dysfunction and Death of BRAF and NRAS Melanoma Cells.Pharmaceuticals (Basel, Switzerland) · 2019Article
- Article
- Identification and characterization of the BmCyclin L1-BmCDK11A/B complex in relation to cell cycle regulation.Cell cycle (Georgetown, Tex.) · 2017Article
- The emerging roles and therapeutic potential of cyclin-dependent kinase 11 (CDK11) in human cancer.Oncotarget · 2016Review
- Cyclin-dependent kinase 11(p110) (CDK11(p110)) is crucial for human breast cancer cell proliferation and growth.Scientific reports · 2015Article
- Preclinical evaluation of cyclin dependent kinase 11 and casein kinase 2 survival kinases as RNA interference targets for triple negative breast cancer therapy.Breast cancer research : BCR · 2015Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Here, we report the identification of the RNA binding motif protein RBM15B/OTT3 as a new CDK11(p110) binding partner that alters the effects of CDK11 on splicing. RBM15B was initially identified as a binding partner of the Epstein-Barr virus mRNA export factor and, more recently, as a cofactor of the nuclear export receptor NXF1. In this study, we found that RBM15B co-elutes with CDK11(p110), cyclin L2α, and serine-arginine (SR) proteins, including SF2/ASF, in a large nuclear complex of ∼1-MDa molecular mass following size exclusion chromatography. Using co-immunoprecipitation experiments and in vitro pulldown assays, we mapped two distinct domains of RBM15B that are essential for its direct interaction with the N-terminal extension of CDK11(p110), cyclin L2α, and SR proteins such as 9G8 and SF2/ASF. Finally, we established that RBM15B is a functional competitor of the SR proteins SF2/ASF and 9G8, inhibits formation of the functional spliceosomal E complex, and antagonizes the positive effect of the CDK11(p110)-cyclin L2α complex on splicing both in vitro and in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.