ArticleGenetics2008
Functioning of the Drosophila Wilms'-tumor-1-associated protein homolog, Fl(2)d, in Sex-lethal-dependent alternative splicing.
Article in Genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
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- Beyond Transcription: Roles of Transcription Factors in Pre-mRNA Splicing.Chemical reviews · 2018Review
- Xio is a component of theProceedings of the National Academy of Sciences of the United States of America · 2018Article
- N6-methyladenosine demethylase FTO targets pre-mRNAs and regulates alternative splicing and 3'-end processing.Nucleic acids research · 2017Article
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- The composition and organization of Drosophila heterochromatin are heterogeneous and dynamic.eLife · 2016Article
- spenito is required for sex determination in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- RNA N6-methyladenosine methylation in post-transcriptional gene expression regulation.Genes & development · 2015Review
- The Drosophila Wilms׳ Tumor 1-Associating Protein (WTAP) homolog is required for eye development.Developmental biology · 2014Article
- Mammalian WTAP is a regulatory subunit of the RNA N6-methyladenosine methyltransferase.Cell research · 2014Article
- Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
fl(2)d, the Drosophila homolog of Wilms'-tumor-1-associated protein (WTAP), regulates the alternative splicing of Sex-lethal (Sxl), transformer (tra), and Ultrabithorax (Ubx). Although WTAP has been found in functional human spliceosomes, exactly how it contributes to the splicing process remains unknown. Here we attempt to identify factors that interact genetically and physically with fl(2)d. We begin by analyzing the Sxl-Fl(2)d protein-protein interaction in detail and present evidence suggesting that the female-specific fl(2)d(1) allele is antimorphic with respect to the process of sex determination. Next we show that fl(2)d interacts genetically with early acting general splicing regulators and that Fl(2)d is present in immunoprecipitable complexes with Snf, U2AF50, U2AF38, and U1-70K. By contrast, we could not detect Fl(2)d complexes containing the U5 snRNP protein U5-40K or with a protein that associates with the activated B spliceosomal complex SKIP. Significantly, the genetic and molecular interactions observed for Sxl are quite similar to those detected for fl(2)d. Taken together, our findings suggest that Sxl and fl(2)d function to alter splice-site selection at an early step in spliceosome assembly.
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