ArticleThe Journal of cell biology1991
p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 202 citations in OpenAlex.
- From the Cytoplasm into the Nucleus-Hepatitis B Virus Travel and Genome Repair.Microorganisms · 2025Review
- Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field.Viruses · 2023Review
- Protoparvovirus Knocking at the Nuclear Door.Viruses · 2017Review
- Nuclear Import of Hepatitis B Virus Capsids and Genome.Viruses · 2017Review
- Article
- Regulating post-mitotic nuclear access: Cdk1-phosphorylation of NLSs.Cell cycle (Georgetown, Tex.) · 2015Article
- Article
- Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?Biochimica et biophysica acta · 2011Review
- Developmental downregulation of Xenopus cyclin E is phosphorylation and nuclear import dependent and is mediated by ubiquitination.Developmental biology · 2011Article
- Recognition of nuclear targeting signals by Karyopherin-β proteins.Current opinion in structural biology · 2010Review
- 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
- The beta subunit of voltage-gated Ca2+ channels interacts with and regulates the activity of a novel isoform of Pax6.The Journal of biological chemistry · 2010Article
- Sox9 inhibits Wnt signaling by promoting beta-catenin phosphorylation in the nucleus.The Journal of biological chemistry · 2009Article
- The Ty1 integrase protein can exploit the classical nuclear protein import machinery for entry into the nucleus.Nucleic acids research · 2008Article
- BK virus as a cofactor in the etiology of prostate cancer in its early stages.Journal of virology · 2008Article
- Clustering of phosphorylation site recognition motifs can be exploited to predict the targets of cyclin-dependent kinase.Genome biology · 2007Article
- Stability and function of JC virus large T antigen and T' proteins are altered by mutation of their phosphorylated threonine 125 residues.Journal of virology · 2006Article
- Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance.Molecular and cellular biology · 2006Article
- Phosphorylation of the varicella-zoster virus (VZV) major transcriptional regulatory protein IE62 by the VZV open reading frame 66 protein kinase.Journal of virology · 2006Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear import of transcription regulatory proteins appears to be used by the cell to trigger transitions in cell cycle, morphogenesis, and transformation. We have previously observed that the rate at which SV-40 T antigen fusion proteins containing a functional nuclear localization sequence (NLS; residues 126-132) are imported into the nucleus is enhanced in the presence of the casein kinase II (CK-II) site S111/112. In this study purified p34cdc2 kinase was used to phosphorylate T antigen proteins specifically at T124 and kinetic measurements at the single-cell level performed to assess its effect on nuclear protein import. T124 phosphorylation, which could be functionally simulated by a T-to-D124 substitution, was found to reduce the maximal extent of nuclear accumulation whilst negligibly affecting the import rate. The inhibition of nuclear import depended on the stoichiometry of phosphorylation. T124 and S111/112 could be phosphorylated independently of one another. Two alternative mechanisms were considered to explain the inhibition of nuclear import by T124 phosphorylation: inactivation of the NLS and cytoplasmic retention, respectively. Furthermore, we speculate that in vivo T124 phosphorylation may regulate the small but functionally significant amount of cytoplasmic SV-40 T antigen. A sequence comparison showed that many transcription regulatory proteins contain domains comprising potential CK-II-sites, cdc2-sites, and NLS. This raises the possibility that the three elements represent a functional unit regulating nuclear protein import.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.