ArticleRNA (New York, N.Y.)2001
The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA export.
Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Structural basis for the synergistic assembly of the snRNA export complex.Nature structural & molecular biology · 2025Article
- The Nuclear Cap-Binding Complex, a multitasking binding partner of RNA polymerase II transcripts.Journal of biochemistry · 2023Review
- Review
- The nuclear cap-binding complex as choreographer of gene transcription and pre-mRNA processing.Genes & development · 2020Review
- mRNA export in the apicomplexan parasite Toxoplasma gondii: emerging divergent components of a crucial pathway.Parasites & vectors · 2018Review
- Structural basis for mutually exclusive co-transcriptional nuclear cap-binding complexes with either NELF-E or ARS2.Nature communications · 2017Article
- Plant snRNP Biogenesis: A Perspective from the Nucleolus and Cajal Bodies.Frontiers in plant science · 2017Review
- Spatial regulation of cytoplasmic snRNP assembly at the cellular level.Journal of experimental botany · 2015Article
- Review
- Allosteric control of the exportin CRM1 unraveled by crystal structure analysis.The FEBS journal · 2014Review
- p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly.Nucleic acids research · 2014Article
- Cap-binding complex (CBC).The Biochemical journal · 2014Review
- Nuclear export mediated regulation of microRNAs: potential target for drug intervention.Current drug targets · 2013Review
- Comparative genomics of proteins involved in RNA nucleocytoplasmic export.BMC evolutionary biology · 2011Article
- Cajal body surveillance of U snRNA export complex assembly.The Journal of cell biology · 2010Article
- Structure and RNA recognition by the snRNA and snoRNA transport factor PHAX.RNA (New York, N.Y.) · 2010Article
- The molecular basis for the regulation of the cap-binding complex by the importins.Nature structural & molecular biology · 2009Article
- The assembly of a spliceosomal small nuclear ribonucleoprotein particle.Nucleic acids research · 2008Review
- A compartmentalized phosphorylation/dephosphorylation system that regulates U snRNA export from the nucleus.Molecular and cellular biology · 2008Article
- Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In metazoa, a subset of spliceosomal U snRNAs are exported from the nucleus after transcription. This export occurs in a large complex containing a U snRNA, the nuclear cap binding complex (CBC), the leucine-rich nuclear export signal receptor CRM1/Xpo1, RanGTP, and the recently identified phosphoprotein PHAX (phosphorylated adaptor for RNA export). Previous results indicated that PHAX made direct contact with RNA, CBC, and Xpo1 in the U snRNA export complex. We have now performed a systematic characterization of the functional domains of PHAX. The most evolutionarily conserved region of PHAX is shown to be a novel RNA-binding domain that is essential for U snRNA export. In addition, PHAX contains two major nuclear localization signals (NLSs) that are required for its recycling to the nucleus after export. The interaction domain of PHAX with CBC is at least partly distinct from the RNA-binding domain and the NLSs. Thus, the different interaction domains of PHAX allow it to act as a scaffold for the assembly of U snRNA export complexes.
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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.