ArticleMolecular and cellular biology2006
Human transcription elongation factor CA150 localizes to splicing factor-rich nuclear speckles and assembles transcription and splicing components into complexes through its amino and carboxyl regions.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 61 citations in OpenAlex.
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- Evolution of the Early Spliceosomal Complex-From Constitutive to Regulated Splicing.International journal of molecular sciences · 2021Review
- A Role for Pre-mRNA-PROCESSING PROTEIN 40C in the Control of Growth, Development, and Stress Tolerance inFrontiers in plant science · 2019Article
- Identification of TCERG1 as a new genetic modulator of TDP-43 production in Drosophila.Acta neuropathologica communications · 2018Article
- The HIV-1 Tat Protein Enhances Splicing at the Major Splice Donor Site.Journal of virology · 2018Article
- Cholesteryl oleate-loaded cationic solid lipid nanoparticles as carriers for efficient gene-silencing therapy.International journal of nanomedicine · 2018Article
- Transcriptional Elongation Regulator 1 Affects Transcription and Splicing of Genes Associated with Cellular Morphology and Cytoskeleton Dynamics and Is Required for Neurite Outgrowth in Neuroblastoma Cells and Primary Neuronal Cultures.Molecular neurobiology · 2017Article
- The in vivo dynamics of TCERG1, a factor that couples transcriptional elongation with splicing.RNA (New York, N.Y.) · 2016Article
- Prp40 pre-mRNA processing factor 40 homolog B (PRPF40B) associates with SF1 and U2AF65 and modulates alternative pre-mRNA splicing in vivo.RNA (New York, N.Y.) · 2015Article
- Article
- Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication.Retrovirology · 2013Article
- Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.The Journal of biological chemistry · 2013Article
- The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.The Journal of biological chemistry · 2012Article
- DNA methylation biomarker candidates for early detection of colon cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2012Article
- TCERG1 regulates alternative splicing of the Bcl-x gene by modulating the rate of RNA polymerase II transcription.Molecular and cellular biology · 2012Article
- Identification of Tat-SF1 cellular targets by exon array analysis reveals dual roles in transcription and splicing.RNA (New York, N.Y.) · 2011Article
- Transcription elongation regulator 1 is a co-integrator of the cell fate determination factor Dachshund homolog 1.The Journal of biological chemistry · 2010Article
- Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The human transcription elongation factor CA150 contains three N-terminal WW domains and six consecutive FF domains. WW and FF domains, versatile modules that mediate protein-protein interactions, are found in nuclear proteins involved in transcription and splicing. CA150 interacts with the splicing factor SF1 and with the phosphorylated C-terminal repeat domain (CTD) of RNA polymerase II (RNAPII) through its WW and FF domains, respectively. WW and FF domains may, therefore, serve to link transcription and splicing components and play a role in coupling transcription and splicing in vivo. In the study presented here, we investigated the subcellular localization and association of CA150 with factors involved in pre-mRNA transcriptional elongation and splicing. Endogenous CA150 colocalized with nuclear speckles, and this was not affected either by inhibition of cellular transcription or by RNAPII CTD phosphorylation. FF domains are essential for the colocalization to speckles, while WW domains are not required for colocalization. We also performed biochemical assays to understand the role of WW and FF domains in mediating the assembly of transcription and splicing components into higher-order complexes. Transcription and splicing components bound to a region in the amino-terminal part of CA150 that contains the three WW domains; however, we identified a region of the C-terminal FF domains that was also critical. Our results suggest that sequences located at both the amino and carboxyl regions of CA150 are required to assemble transcription/splicing complexes, which may be involved in the coupling of those processes.
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