ArticleMolecular and cellular biology2003
Sam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 106 citations in OpenAlex.
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- Role of Sam68 in Sunitinib induced renal cell carcinoma apoptosis.Cancer medicine · 2022Article
- Targeting protein tyrosine kinase 6 in cancer.Biochimica et biophysica acta. Reviews on cancer · 2020Review
- PSPC1-interchanged interactions with PTK6 and β-catenin synergize oncogenic subcellular translocations and tumor progression.Nature communications · 2019Article
- Understanding the binding specificities of mRNA targets by the mammalian Quaking protein.Nucleic acids research · 2019Article
- Apoptosis and Autophagy in Picornavirus Infection.Frontiers in microbiology · 2019Review
- A Rev-CBP80-eIF4AI complex drives Gag synthesis from the HIV-1 unspliced mRNA.Nucleic acids research · 2018Article
- Mechanism of mRNA-STAR domain interaction: Molecular dynamics simulations of Mammalian Quaking STAR protein.Scientific reports · 2017Article
- Nuclear Protein Sam68 Interacts with the Enterovirus 71 Internal Ribosome Entry Site and Positively Regulates Viral Protein Translation.Journal of virology · 2015Article
- PTK6 inhibition promotes apoptosis of Lapatinib-resistant Her2(+) breast cancer cells by inducing Bim.Breast cancer research : BCR · 2015Article
- Evolutionary conservation of a molecular machinery for export and expression of mRNAs with retained introns.RNA (New York, N.Y.) · 2015Article
- Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus.Frontiers in microbiology · 2015Review
- Gammaretroviral pol sequences act in cis to direct polysome loading and NXF1/NXT-dependent protein production by gag-encoded RNA.Retrovirology · 2014Article
- Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic function.Journal of cell science · 2014Article
- Feline immunodeficiency virus Gag is a nuclear shuttling protein.Journal of virology · 2012Article
- Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.PloS one · 2012Article
- A cell-based method for screening RNA-protein interactions: identification of constitutive transport element-interacting proteins.PloS one · 2012Article
- Sam68 marks the transcriptionally active stages of spermatogenesis and modulates alternative splicing in male germ cells.Nucleic acids research · 2011Article
- The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway.RNA (New York, N.Y.) · 2011Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Cells normally restrict the nuclear export and expression of intron-containing mRNA. In many cell lines, this restriction can be overcome by inclusion of cis-acting elements, such as the Mason-Pfizer monkey virus constitutive transport element (CTE), in the RNA. In contrast, we observed that CTE-mediated expression from human immunodeficiency virus Gag-Pol reporters was very inefficient in 293 and 293T cells. However, addition of Sam68 led to a dramatic increase in the amount of Gag-Pol proteins produced in these cells. Enhancement of CTE function was not seen when a Sam68 point mutant (G178E) that is defective for RNA binding was used. Additionally, the effect of Sam68 was inhibited in a dose-dependent manner by coexpression of an activated form of the nuclear kinase Sik/BRK that hyperphosphorylated Sam68. RNA analysis showed that cytoplasmic Gag-Pol-CTE RNA levels were only slightly enhanced by the addition of Sam68, compared to a 60- to 70-fold increase in the levels of Gag-Pol protein expression. Thus, in this system, Sam68 functioned to enhance the cytoplasmic utilization of RNA containing the CTE. These results suggest that Sam68 may interact with specific RNAs in the nucleus to provide a "mark" that affects their cytoplasmic fate. They also provide further evidence of links between signal transduction and RNA utilization.
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