ArticleMolecular and cellular biology2004
Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p.
Article in Molecular and cellular biology, 2004. 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.
- Substitutions in RNA-binding protein Hrp1 map a potential interaction surface with the yeast RNA polymerase II elongation complex.Genetics · 2026Article
- Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control inInternational journal of molecular sciences · 2024Review
- Article
- The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023Review
- Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018Article
- Multilayer regulatory mechanisms control cleavage factor I proteins in filamentous fungi.Nucleic acids research · 2015Article
- Monosome formation during translation initiation requires the serine/arginine-rich protein Npl3.Molecular and cellular biology · 2013Article
- Yeast hnRNP-related proteins contribute to the maintenance of telomeres.Biochemical and biophysical research communications · 2012Article
- Article
- Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin.The Journal of biological chemistry · 2011Article
- The Role of Protein Arginine Methylation in mRNP Dynamics.Molecular biology international · 2011Article
- Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF.Molecular and cellular biology · 2010Article
- Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.Nucleic acids research · 2010Article
- The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.Journal of molecular biology · 2009Article
- Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Nucleic acids research · 2009Article
- Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals.PLoS biology · 2008Article
- Autoregulation of Npl3, a yeast SR protein, requires a novel downstream region and serine phosphorylation.Molecular and cellular biology · 2008Article
- Snu56p is required for Mer1p-activated meiotic splicing.Molecular and cellular biology · 2008Article
- Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.Journal of molecular biology · 2008Article
- Protein arginine methyltransferases: from unicellular eukaryotes to humans.Eukaryotic cell · 2007Review
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2 authors.
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Abstract
Eukaryotic mRNA processing and export are mediated by a series of complexes composed of heterogeneous nuclear ribonucleoproteins (hnRNPs). Many of these hnRNPs are methylated at arginine residues within their RGG domains. Although cellular arginine methylation is required for the efficient nuclear export of several hnRNPs, its role in this process is unknown. To address this question, we replaced the methylated RGG tripeptides of two hnRNPs, Npl3p and Hrp1p, with KGG. We found that these substitutions specifically abolish their methylation but have different effects on their nuclear export activity. Although the efficient export of Hrp1p requires cellular methyltransferase activity, the modification of Hrp1p itself is dispensable. In contrast, we found that Npl3 arginine methylation not only facilitates its own export but also is required for Hrp1p to efficiently exit the nucleus. Consistent with this observation, we found that Npl3p and Hrp1p exist in a ribonucleoprotein complex. We provide the first evidence that the arginine methylation of a particular protein directly affects its activity. Efficient export does not require methylation per se, but unmethylated arginine residues lead to retention of hnRNPs. Thus, arginine methylation serves to mask the Npl3p RGG domain for efficient ribonucleoprotein export.
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