ArticleThe Biochemical journal2003
Role of flanking sequences and phosphorylation in the recognition of the simian-virus-40 large T-antigen nuclear localization sequences by importin-alpha.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 110 citations in OpenAlex.
- Elucidation of the binding interaction interface between AAV serotype 11 capsid protein and host nuclear import proteins.Molecular therapy. Methods & clinical development · 2025Article
- Probing the extent of importin-α targeting of the TAF8 NLS by eliminating its cationic net-charge.Protein science : a publication of the Protein Society · 2025Article
- Karyopherins in the Remodeling of Extracellular Matrix: Implications in Tendon Injury.Journal of orthopaedics and sports medicine · 2023Article
- Review
- The isolated C-terminal nuclear localization sequence of the breast cancer metastasis suppressor 1 is disordered.Archives of biochemistry and biophysics · 2019Article
- New Therapeutic Approach for Targeting Hippo Signalling Pathway.Scientific reports · 2019Article
- Modulating CRISPR gene drive activity through nucleocytoplasmic localization of Cas9 inFungal biology and biotechnology · 2019Article
- Variations in nuclear localization strategies among pol X family enzymes.Traffic (Copenhagen, Denmark) · 2018Article
- Review
- Crystal structure of importin-α bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein.Protein science : a publication of the Protein Society · 2017Article
- Structural Basis for Importin-α Binding of the Human Immunodeficiency Virus Tat.Scientific reports · 2017Article
- Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha.PloS one · 2017Article
- Insights into a novel nuclear function for Fascin in the regulation of the amino-acid transporter SLC3A2.Scientific reports · 2016Article
- The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production.PLoS pathogens · 2016Article
- Importin α1 Mediates Yorkie Nuclear Import via an N-terminal Non-canonical Nuclear Localization Signal.The Journal of biological chemistry · 2016Article
- The Pseudorabies Virus DNA Polymerase Accessory Subunit UL42 Directs Nuclear Transport of the Holoenzyme.Frontiers in microbiology · 2016Article
- Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects.Acta crystallographica. Section D, Structural biology · 2016Article
- Phosphorylation of bovine papillomavirus E1 by the protein kinase CK2 near the nuclear localization signal does not influence subcellular distribution of the protein in dividing cells.Archives of virology · 2016Article
- Comprehensive analysis of the dynamic structure of nuclear localization signals.Biochemistry and biophysics reports · 2015Article
- Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
7 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear import of simian-virus-40 large T-antigen (tumour antigen) is enhanced via phosphorylation by the protein kinase CK2 at Ser112 in the vicinity of the NLS (nuclear localization sequence). To determine the structural basis of the effect of the sequences flanking the basic cluster KKKRK, and the effect of phosphorylation on the recognition of the NLS by the nuclear import factor importin-alpha (Impalpha), we co-crystallized non-autoinhibited Impalpha with peptides corresponding to the phosphorylated and non-phosphorylated forms of the NLS, and determined the crystal structures of the complexes. The structures show that the amino acids N-terminally flanking the basic cluster make specific contacts with the receptor that are distinct from the interactions between bipartite NLSs and Impalpha. We confirm the important role of flanking sequences using binding assays. Unexpectedly, the regions of the peptides containing the phosphorylation site do not make specific contacts with the receptor. Binding assays confirm that phosphorylation does not increase the affinity of the T-antigen NLS to Impalpha. We conclude that the sequences flanking the basic clusters in NLSs play a crucial role in nuclear import by modulating the recognition of the NLS by Impalpha, whereas phosphorylation of the T-antigen enhances nuclear import by a mechanism that does not involve a direct interaction of the phosphorylated residue with Impalpha.
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