ArticleRNA (New York, N.Y.)2006
p54nrb is a component of the snRNP-free U1A (SF-A) complex that promotes pre-mRNA cleavage during polyadenylation.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.
- Identification of novel pathway partners of p68 and p72 RNA helicases through Oncomine meta-analysis.BMC genomics · 2007Pooled it
- U1 snRNP proteins promote proximal alternative polyadenylation sites by directly interacting with 3' end processing core factors.Journal of molecular cell biology · 2022Article
- Molecular Modelling of NONO and SFPQ Dimerization Process and RNA Recognition Mechanism.International journal of molecular sciences · 2022Article
- Nono deficiency compromises TET1 chromatin association and impedes neuronal differentiation of mouse embryonic stem cells.Nucleic acids research · 2020Article
- NONO and tumorigenesis: More than splicing.Journal of cellular and molecular medicine · 2020Review
- RNF8 mediates NONO degradation following UV-induced DNA damage to properly terminate ATR-CHK1 checkpoint signaling.Nucleic acids research · 2019Article
- The Length of the Expressed 3' UTR Is an Intermediate Molecular Phenotype Linking Genetic Variants to Complex Diseases.Frontiers in genetics · 2019Article
- NEAT1 scaffolds RNA-binding proteins and the Microprocessor to globally enhance pri-miRNA processing.Nature structural & molecular biology · 2017Article
- Roles of Sumoylation in mRNA Processing and Metabolism.Advances in experimental medicine and biology · 2017Review
- A crystallographic study of human NONO (p54(nrb)): overcoming pathological problems with purification, data collection and noncrystallographic symmetry.Acta crystallographica. Section D, Structural biology · 2016Article
- The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.Nucleic acids research · 2016Article
- New Noncoding Lytic Transcripts Derived from the Epstein-Barr Virus Latency Origin of Replication, oriP, Are Hyperedited, Bind the Paraspeckle Protein, NONO/p54nrb, and Support Viral Lytic Transcription.Journal of virology · 2015Article
- U1A regulates 3' processing of the survival motor neuron mRNA.The Journal of biological chemistry · 2014Article
- Assembly, activation, and substrate specificity of cyclin D1/Cdk2 complexes.Biochemistry · 2013Article
- Transcriptional activity regulates alternative cleavage and polyadenylation.Molecular systems biology · 2011Article
- Consensus PP1 binding motifs regulate transcriptional corepression and alternative RNA splicing activities of the steroid receptor coregulators, p54nrb and PSF.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Control of the stability of a protein-RNA complex by the position of fluorine in a base analogue.Journal of the American Chemical Society · 2011Article
- Molecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.Nucleic acids research · 2010Review
- Transcription termination by nuclear RNA polymerases.Genes & development · 2009Article
- Complex assembly on the human CYP17 promoter.Molecular and cellular endocrinology · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The U1 snRNP-A (U1A) protein has been known for many years as a component of the U1 snRNP. We have previously described a form of U1A present in human cells in significant amounts that is not associated with the U1 snRNP or U1 RNA but instead is part of a novel complex of non-snRNP proteins that we have termed snRNP-free U1A, or SF-A. Antibodies that specifically recognize this complex inhibit in vitro splicing and polyadenylation of pre-mRNA, suggesting that this complex may play an important functional role in these mRNA-processing activities. This finding was underscored by the determination that one of the components of this complex is the polypyrimidine-tract-binding protein-associated splicing factor, PSF. In order to further our studies on this complex and to determine the rest of the components of the SF-A complex, we prepared several stable HeLa cell lines that overexpress a tandem-affinity-purification-tagged version of U1A (TAP-tagged U1A). Nuclear extract was prepared from one of these cell lines, line 107, and affinity purification was performed along with RNase treatment. We have used mass spectrometry analysis to identify the candidate factors that associate with U1A. We have now identified and characterized PSF, p54(nrb), and p68 as novel components of the SF-A complex. We have explored the function of this complex in RNA processing, specifically cleavage and polyadenylation, by performing immunodepletions followed by reconstitution experiments, and have found that p54(nrb) is critical.
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