ArticleMolecular and cellular biology2002
Characterization of U2AF(6), a splicing factor related to U2AF(35).
Article in Molecular and cellular biology, 2002. 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.
- Primate-specific adaptation of Ku protects transcriptomic integrity by suppressing Alu-mediated alternative splicing.bioRxiv : the preprint server for biology · 2025Article
- Global analysis of binding sites of U2AF1 and ZRSR2 reveals RNA elements required for mutually exclusive splicing by the U2- and U12-type spliceosome.Nucleic acids research · 2024Article
- Article
- The zinc finger domains in U2AF26 and U2AF35 have diverse functionalities including a role in controlling translation.RNA biology · 2020Article
- Postsplicing-Derived Full-Length Intron Circles in the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2018Article
- Diverse regulation of 3' splice site usage.Cellular and molecular life sciences : CMLS · 2015Review
- Identification of U2AF(35)-dependent exons by RNA-Seq reveals a link between 3' splice-site organization and activity of U2AF-related proteins.Nucleic acids research · 2015Article
- Genomic functions of U2AF in constitutive and regulated splicing.RNA biology · 2015Article
- Mechanisms for U2AF to define 3' splice sites and regulate alternative splicing in the human genome.Nature structural & molecular biology · 2014Article
- Control of alternative splicing by forskolin through hnRNP K during neuronal differentiation.Nucleic acids research · 2012Article
- The U2AF35-related protein Urp contacts the 3' splice site to promote U12-type intron splicing and the second step of U2-type intron splicing.Genes & development · 2010Article
- Allele-specific recognition of the 3' splice site of INS intron 1.Human genetics · 2010Article
- Spatial mapping of splicing factor complexes involved in exon and intron definition.The Journal of cell biology · 2008Article
- Host proteins interacting with the Moloney murine leukemia virus integrase: multiple transcriptional regulators and chromatin binding factors.Retrovirology · 2008Article
- The impact of alternative splicing in vivo: mouse models show the way.RNA (New York, N.Y.) · 2007Review
- In vivo requirement of the small subunit of U2AF for recognition of a weak 3' splice site.Molecular and cellular biology · 2006Article
- Molecular characterization and phylogeny of U2AF35 homologs in plants.Plant physiology · 2006Article
- Systematic genome-wide annotation of spliceosomal proteins reveals differential gene family expansion.Genome research · 2006Article
- FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.RNA (New York, N.Y.) · 2005Article
- A novel SR-related protein is required for the second step of Pre-mRNA splicing.Molecular and cellular biology · 2005Article
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4 authors.
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Abstract
The essential splicing factor U2AF (U2 auxiliary factor) is a heterodimer composed of 65-kDa (U2AF(65)) and 35-kDa (U2AF(35)) subunits. U2AF(35) has multiple functions in pre-mRNA splicing. First, U2AF(35) has been shown to function by directly interacting with the AG at the 3' splice site. Second, U2AF(35) is thought to play a role in the recruitment of U2AF(65) by serine-arginine-rich (SR) proteins in enhancer-dependent splicing. It has been proposed that the physical interaction between the arginine-serine-rich (RS) domain of U2AF(35) and SR proteins is important for this activity. However, other data suggest that this may not be the case. Here, we report the identification of a mammalian gene that encodes a 26-kDa protein bearing strong sequence similarity to U2AF(35), designated U2AF(26). The N-terminal 187 amino acids of U2AF(35) and U2AF(26) are nearly identical. However, the C-terminal domain of U2AF(26) lacks many characteristics of the U2AF(35) RS domain and, therefore, might be incapable of interacting with SR proteins. We show that U2AF(26) can associate with U2AF(65) and can functionally substitute for U2AF(35) in both constitutive and enhancer-dependent splicing, demonstrating that the RS domain of the small U2AF subunit is not required for splicing enhancer function. Finally, we show that U2AF(26) functions by enhancing the binding of U2AF(65) to weak 3' splice sites. These studies identify U2AF(26) as a mammalian splicing factor and demonstrate that distinct U2AF complexes can participate in pre-mRNA splicing. Based on its sequence and functional similarity to U2AF(35), U2AF(26) may play a role in regulating alternative splicing.
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