ArticleThe Journal of biological chemistry2010
Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Multiple types of nuclear localization signals inBiochemistry and biophysics reports · 2024Article
- Molecular Coevolution of Nuclear and Nucleolar Localization Signals inside the Basic Domain of HIV-1 Tat.Journal of virology · 2022Article
- Structural characterization of human importin alpha 7 in its cargo-free form at 2.5 Å resolution.Scientific reports · 2022Article
- Nuclear Localization Signals for Optimization of Genetically Encoded Tools in Neurons.Frontiers in cell and developmental biology · 2022Article
- The structure of importin α and the nuclear localization peptide of ChREBP, and small compound inhibitors of ChREBP-importin α interactions.The Biochemical journal · 2020Article
- Acetylation accumulates PFKFB3 in cytoplasm to promote glycolysis and protects cells from cisplatin-induced apoptosis.Nature communications · 2018Article
- Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha.PloS one · 2017Article
- Article
- Diversification of importin-α isoforms in cellular trafficking and disease states.The Biochemical journal · 2015Review
- Respiratory virus modulation of host nucleocytoplasmic transport; target for therapeutic intervention?Frontiers in microbiology · 2015Review
- Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.PloS one · 2015Article
- Global Characteristics of CSIG-Associated Gene Expression Changes in Human HEK293 Cells and the Implications for CSIG Regulating Cell Proliferation and Senescence.Frontiers in endocrinology · 2015Article
- Regulating post-mitotic nuclear access: Cdk1-phosphorylation of NLSs.Cell cycle (Georgetown, Tex.) · 2015Article
- The p53-induced factor Ei24 inhibits nuclear import through an importin β-binding-like domain.The Journal of cell biology · 2014Article
- Design rules for selective binding of nuclear localization signals to minor site of importin α.PloS one · 2014Article
- Identification of cargo proteins specific for importin-β with importin-α applying a stable isotope labeling by amino acids in cell culture (SILAC)-based in vitro transport system.The Journal of biological chemistry · 2013Article
- Serotype-specific differences in dengue virus non-structural protein 5 nuclear localization.The Journal of biological chemistry · 2013Article
- Identification of cargo proteins specific for the nucleocytoplasmic transport carrier transportin by combination of an in vitro transport system and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics.Molecular & cellular proteomics : MCP · 2013Article
- Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals.The Plant cell · 2012Article
- Somatic mutations in the Notch, NF-KB, PIK3CA, and Hedgehog pathways in human breast cancers.Genes, chromosomes & cancer · 2012Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Importin-alpha is the nuclear import receptor that recognizes the classic monopartite and bipartite nuclear localization sequences (cNLSs), which contain one or two clusters of basic amino acids, respectively. Different importin-alpha paralogs in a single organism are specific for distinct repertoires of cargos. Structural studies revealed that monopartite cNLSs and the C-terminal basic clusters of the bipartite cNLSs bind to the same site on importin-alpha, termed the major cNLS-binding site. We used an oriented peptide library approach with five degenerate positions to probe the specificity of the major cNLS-binding site in importin-alpha. We identified the sequences KKKRR, KKKRK, and KKRKK as the optimal sequences for binding to this site for mouse importin-alpha2, human importin-alpha1, and human importin-alpha5, respectively. The crystal structure of mouse importin-alpha2 with its optimal peptide confirmed the expected binding mode resembling the binding of simian virus 40 large tumor-antigen cNLS. Binding assays confirmed that the peptides containing these sequences bound to the corresponding proteins with low nanomolar affinities. Nuclear import assays showed that the sequences acted as functional cNLSs, with specificity for particular importin-alphas. This is the first time that structural information has been linked to an oriented peptide library screening approach for importin-alpha; the results will contribute to understanding of the sequence determinants of cNLSs, and may help identify as yet unidentified cNLSs in novel proteins.
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