ArticleMolecular and cellular biology2008
A compartmentalized phosphorylation/dephosphorylation system that regulates U snRNA export from the nucleus.
Article in Molecular and cellular biology, 2008. 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, 37 citations in OpenAlex.
- Review
- Assembly mechanism of the snRNA nuclear export complex.Nature structural & molecular biology · 2025Article
- Structural basis for the synergistic assembly of the snRNA export complex.Nature structural & molecular biology · 2025Article
- TRIM24 Cooperates with Ras Mutation to Drive Glioma Progression through snoRNA Recruitment of PHAX and DNA-PKcs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Phosphorylated Adapter RNA Export Protein Is Methylated at Lys 381 by an Methyltransferase-like 21C (METTL21C).International journal of molecular sciences · 2023Article
- The Nuclear Cap-Binding Complex, a multitasking binding partner of RNA polymerase II transcripts.Journal of biochemistry · 2023Review
- Cajal bodies: Evolutionarily conserved nuclear biomolecular condensates with properties unique to plants.The Plant cell · 2023Review
- TGS1 impacts snRNA 3'-end processing, ameliorates survival motor neuron-dependent neurological phenotypes in vivo and prevents neurodegeneration.Nucleic acids research · 2022Article
- SMN - A chaperone for nuclear RNP social occasions?RNA biology · 2017Review
- Towards an understanding of regulating Cajal body activity by protein modification.RNA biology · 2017Review
- Plant snRNP Biogenesis: A Perspective from the Nucleolus and Cajal Bodies.Frontiers in plant science · 2017Review
- Transcriptomic comparison of Drosophila snRNP biogenesis mutants reveals mutant-specific changes in pre-mRNA processing: implications for spinal muscular atrophy.RNA (New York, N.Y.) · 2016Article
- A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.eLife · 2015Article
- Quantitative phosphoproteomics of cytotoxic T cells to reveal protein kinase d 2 regulated networks.Molecular & cellular proteomics : MCP · 2014Article
- p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly.Nucleic acids research · 2014Article
- A day in the life of the spliceosome.Nature reviews. Molecular cell biology · 2014Review
- Cap-binding complex (CBC).The Biochemical journal · 2014Review
- Signals controlling Cajal body assembly and function.The international journal of biochemistry & cell biology · 2013Review
- 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
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PHAX (phosphorylated adaptor for RNA export) is the key regulator of U snRNA nuclear export in metazoa. Our previous work revealed that PHAX is phosphorylated in the nucleus and is exported as a component of the U snRNA export complex to the cytoplasm, where it is dephosphorylated (M. Ohno, A. Segref, A. Bachi, M. Wilm, and I. W. Mattaj, Cell 101:187-198, 2000). PHAX phosphorylation is essential for export complex assembly, whereas its dephosphorylation causes export complex disassembly. Thus, PHAX is subject to a compartmentalized phosphorylation/dephosphorylation cycle that contributes to transport directionality. However, neither essential PHAX phosphorylation sites nor the modifying enzymes that contribute to the compartmentalized system have been identified. Here, we identify PHAX phosphorylation sites that are necessary and sufficient for U snRNA export. Mutation of the phosphorylation sites inhibited U snRNA export in a dominant-negative way. We also show, by both biochemical and RNA interference knockdown experiments, that the nuclear kinase and the cytoplasmic phosphatase for PHAX are CK2 kinase and protein phosphatase 2A, respectively. Our results reveal the composition of the compartmentalized phosphorylation/dephosphorylation system that regulates U snRNA export. This finding was surprising in that such a specific system for U snRNA export regulation is composed of two such universal regulators, suggesting that this compartmentalized system is used more broadly for gene expression regulation.
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