ArticleNature communications2018
Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Unveiling nuclear localization signals in human arginine deiminase proteins.Protein science : a publication of the Protein Society · 2026Article
- Structural and functional characterisation of ATF2 nuclear import reveals paralogue-selective importin-α recognition and a non-canonical NLS formed in trans.Life science alliance · 2026Article
- Structural Insights Into the Nuclear Import of Gallid Alphaherpesvirus 1 Large Tegument Protein.MicrobiologyOpen · 2026Article
- Structural Insights Into the Nuclear Import of Marek's Disease Virus Large Tegument Protein.Advances in virology · 2026Article
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Alpha-ketoglutarate mitigates insulin resistance and metabolic inflexibility in a mouse model of Ataxia-Telangiectasia.Nature communications · 2025Article
- Structural Insights into the Nuclear Import of Haliotid Herpesvirus 1 Large Tegument Protein Homologue.Viruses · 2025Article
- The intracellular virus-host interface of henipaviruses.Journal of virology · 2025Review
- Importin α3 Is Tolerant to Nuclear Localization Signal Chirality.International journal of molecular sciences · 2025Article
- A conserved motif in Henipavirus P/V/W proteins drives the fibrillation of the W protein from Hendra virus.Protein science : a publication of the Protein Society · 2025Article
- Cas9-mediated gene-editing frequency in microalgae is doubled by harnessing the interaction between importin α and phytopathogenic NLSs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dissecting Henipavirus W proteins conformational and fibrillation properties: contribution of their N- and C-terminal constituent domains.The FEBS journal · 2025Article
- Structural basis for nuclear import of adeno-associated virus serotype 6 capsid protein.Journal of virology · 2025Article
- Sequence specificity of an essential nuclear localization sequence in Mcm3.PLoS genetics · 2025Article
- Sequence specificity of an essential nuclear localization sequence in Mcm3.bioRxiv : the preprint server for biology · 2024Article
- Structural basis for nuclear import of bat adeno-associated virus capsid protein.The Journal of general virology · 2024Article
- Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.Viruses · 2023Article
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9 authors.
Funding
Abstract
Seven human isoforms of importin α mediate nuclear import of cargo in a tissue- and isoform-specific manner. How nuclear import adaptors differentially interact with cargo harbouring the same nuclear localisation signal (NLS) remains poorly understood, as the NLS recognition region is highly conserved. Here, we provide a structural basis for the nuclear import specificity of W proteins in Hendra and Nipah viruses. We determine the structural interfaces of these cargo bound to importin α1 and α3, identifying a 2.4-fold more extensive interface and > 50-fold higher binding affinity for importin α3. Through the design of importin α1 and α3 chimeric and mutant proteins, together with structures of cargo-free importin α1 and α3 isoforms, we establish that the molecular basis of specificity resides in the differential positioning of the armadillo repeats 7 and 8. Overall, our study provides mechanistic insights into a range of important nucleocytoplasmic transport processes reliant on isoform adaptor specificity.
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