ArticleThe EMBO journal1991
The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen.
Article in The EMBO journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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123 citing papers in PubMed, 355 citations in OpenAlex.
- Succinylation enables IDE to act as a hub of larval tissue destruction and adult tissue reconstruction during insect metamorphosis.Science advances · 2025Article
- Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field.Viruses · 2023Review
- Nuclear Transport of Respiratory Syncytial Virus Matrix Protein Is Regulated by Dual Phosphorylation Sites.International journal of molecular sciences · 2022Article
- Robust control of floral meristem determinacy by position-specific multifunctions of KNUCKLES.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- CK2-mediated phosphorylation of Che-1/AATF is required for its pro-proliferative activity.Journal of experimental & clinical cancer research : CR · 2021Article
- Human Papillomavirus 31 Tyrosine 102 Regulates Interaction with E2 Binding Partners and Episomal Maintenance.Journal of virology · 2020Article
- Development of a novel DsRed-NLS vector with a monopartite classical nuclear localization signal.3 Biotech · 2019Article
- Oocyte shuttle, a recombinant protein transporting donor DNA into theBiology open · 2017Article
- Regulation and function of phosphorylation on VP8, the major tegument protein of bovine herpesvirus 1.Journal of virology · 2015Article
- Acetylation of the RhoA GEF Net1A controls its subcellular localization and activity.Journal of cell science · 2015Article
- Enrichment techniques employed in phosphoproteomics.Amino acids · 2012Review
- Toward intracellular targeted delivery of cancer therapeutics: progress and clinical outlook for brain tumor therapy.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2012Article
- Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?Biochimica et biophysica acta · 2011Review
- Stimulation of CK2-dependent Grp94 phosphorylation by the nuclear localization signal peptide.Molecular and cellular biochemistry · 2011Article
- In-cell NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2011Review
- Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening.The Journal of biological chemistry · 2010Article
- Binding of p110 retinoblastoma protein inhibits nuclear import of simian virus SV40 large tumor antigen.The Journal of biological chemistry · 2010Article
- Molecular targeting of intracellular compartments specifically in cancer cells.Genes & cancer · 2010Article
- Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replication.Virology · 2010Article
- Viral oncolysis that targets Raf-1 signaling control of nuclear transport.Journal of virology · 2010Article
63 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously demonstrated [Rihs, H.-P. and Peters, R. (1989) EMBO J., 8, 1479-1484] that the nuclear transport of recombinant proteins in which short fragments of the SV40 T-antigen are fused to the amino terminus of Escherichia coli beta-galactosidase is dependent on both the nuclear localization sequence (NLS, T-antigen residues 126-132) and a phosphorylation-site-containing sequence (T-antigen residues 111-125). While the NLS determines the specificity, the rate of transport is controlled by the phosphorylation-site-containing sequence. The present study furthers this observation and examines the role of the various phosphorylation sites. Purified, fluorescently labeled recombinant proteins were injected into the cytoplasm of Vero or hepatoma (HTC) cells and the kinetics of nuclear transport measured by laser microfluorimetry. By replacing serine and threonine residues known to be phosphorylated in vivo, we identified the casein kinase II (CK-II) site S111/S112 to be the determining factor in the enhancement of the transport. Either of the residues 111 or 112 was sufficient to elicit the maximum transport enhancement. The other phosphorylation sites (S120, S123, T124) had no influence on the transport rate. Examination of the literature suggested that many proteins harboring a nuclear localization sequence also contain putative CK-II sites at a distance of approximately 10-30 amino acid residues from the NLS. CK-II has been previously implicated in the transmission of growth signals to the nucleus. Our results suggest that CK-II may exert this role by controlling the rate of nuclear protein transport.
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