ArticleThe Journal of biological chemistry2011
Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- The N-terminal extension of ribosomal protein Rps2 shapes its early fate through Chaperone-Importin competition and arginine methylation.The Journal of biological chemistry · 2026Article
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- Research progress on PRMTs involved in epigenetic modification and tumour signalling pathway regulation (Review).International journal of oncology · 2023Review
- Coordination of RNA Processing Regulation by Signal Transduction Pathways.Biomolecules · 2021Review
- Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation.Frontiers in molecular biosciences · 2021Article
- Transportin-1: A Nuclear Import Receptor with Moonlighting Functions.Frontiers in molecular biosciences · 2021Review
- Nonclassical nuclear localization signals mediate nuclear import of CIRBP.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Non-Histone Arginine Methylation by Protein Arginine Methyltransferases.Current protein & peptide science · 2020Review
- Antiviral activity of a purine synthesis enzyme reveals a key role of deamidation in regulating protein nuclear import.Science advances · 2019Article
- Proteomic analysis reveals that wildtype and alanine-expanded nuclear poly(A)-binding protein exhibit differential interactions in skeletal muscle.The Journal of biological chemistry · 2019Article
- Friend or foe-Post-translational modifications as regulators of phase separation and RNP granule dynamics.The Journal of biological chemistry · 2019Review
- PABPN1 suppresses TDP-43 toxicity in ALS disease models.Human molecular genetics · 2015Article
- pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral Replication.Journal of virology · 2015Article
- Arginine methylation of DRBD18 differentially impacts its opposing effects on the trypanosome transcriptome.Nucleic acids research · 2015Article
- Interactions affected by arginine methylation in the yeast protein-protein interaction network.Molecular & cellular proteomics : MCP · 2013Article
- PABPN1: molecular function and muscle disease.The FEBS journal · 2013Review
- Signaling pathways that control mRNA turnover.Cellular signalling · 2013Review
- Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.The EMBO journal · 2012Article
- Advances in understanding the molecular basis of frontotemporal dementia.Nature reviews. Neurology · 2012Review
- Beyond the Poly(A) Tail: The Expanding Functional Landscape of PABPN1 and Its Dysregulation in OPMD and Cancer.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear poly(A) binding protein, PABPN1, promotes mRNA polyadenylation in the cell nucleus by increasing the processivity of poly(A) polymerase and contributing to poly(A) tail length control. In its C-terminal domain, the protein carries 13 arginine residues that are all asymmetrically dimethylated. The function of this modification in PABPN1 has been unknown. Part of the methylated domain serves as nuclear localization signal, binding the import receptor transportin. Here we report that arginine methylation weakens the affinity of PABPN1 for transportin. Recombinant, unmethylated PABPN1 binds more strongly to transportin than its methylated counterpart from mammalian tissue, and in vitro methylation reduces the affinity. Transportin and RNA compete for binding to PABPN1. Methylation favors RNA binding. Transportin also inhibits in vitro methylation of the protein. Finally, a peptide corresponding to the nuclear localization signal of PABPN1 competes with transportin-dependent nuclear import of the protein in a permeabilized cell assay and does so less efficiently when it is methylated. We hypothesize that transportin binding might delay methylation of PABPN1 until after nuclear import. In the nucleus, arginine methylation may favor the transition of PABPN1 to the competing ligand RNA and serve to reduce the risk of the protein being reexported to the cytoplasm by transportin.
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