ArticleThe Plant cell2012
Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 71 citations in OpenAlex.
- Structures of Nicotiana benthamiana importin-α1 complexes reveal mechanisms for plant virus NLS recognition.The Plant journal : for cell and molecular biology · 2026Article
- The importin-alpha superfamily engages in ethylene signaling by shuttling ETHYLENE INSENSITIVE 2 from the endoplasmic reticulum to the nucleus.The FEBS journal · 2026Article
- Training bias and sequence alignments shape protein-peptide docking by AlphaFold and related methods.Protein science : a publication of the Protein Society · 2025Article
- Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus.Molecular plant pathology · 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
- Appropriate reduction of importin-α gene expression enhances yellow dwarf disease resistance in common wheat.Plant biotechnology journal · 2024Article
- Toxoplasma Gondii Importin α Shows Weak Auto-Inhibition.The protein journal · 2023Article
- Nuclear effectors of plant pathogens: Distinct strategies to be one step ahead.Molecular plant pathology · 2023Review
- BRXL4-LAZY1 interaction at the plasma membrane controls Arabidopsis branch angle and gravitropism.The Plant journal : for cell and molecular biology · 2023Article
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Article
- OsWRKY62 and OsWRKY76 Interact with Importin α1s for Negative Regulation of Defensive Responses in Rice Nucleus.Rice (New York, N.Y.) · 2022Article
- Importin-αs are required for the nuclear localization and function of the Plasmopara viticola effector PvAVH53.Horticulture research · 2021Article
- Article
- Coordination of NMCP1- and NMCP2-class proteins within the plant nucleoskeleton.Molecular biology of the cell · 2020Article
- TALE-carrying bacterial pathogens trap host nuclear import receptors for facilitation of infection of rice.Molecular plant pathology · 2019Article
- Nuclear Import ofFrontiers in plant science · 2018Article
- Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha.PloS one · 2017Article
- Distinctive Nuclear Localization Signals in the OomyceteFrontiers in microbiology · 2017Article
- Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the classical nucleocytoplasmic import pathway, nuclear localization signals (NLSs) in cargo proteins are recognized by the import receptor importin-α. Importin-α has two separate NLS binding sites (the major and the minor site), both of which recognize positively charged amino acid clusters in NLSs. Little is known about the molecular basis of the unique features of the classical nuclear import pathway in plants. We determined the crystal structure of rice (Oryza sativa) importin-α1a at 2-Å resolution. The structure reveals that the autoinhibitory mechanism mediated by the importin-β binding domain of importin-α operates in plants, with NLS-mimicking sequences binding to both minor and major NLS binding sites. Consistent with yeast and mammalian proteins, rice importin-α binds the prototypical NLS from simian virus 40 large T-antigen preferentially at the major NLS binding site. We show that two NLSs, previously described as plant specific, bind to and are functional with plant, mammalian, and yeast importin-α proteins but interact with rice importin-α more strongly. The crystal structures of their complexes with rice importin-α show that they bind to the minor NLS binding site. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin-α show preferential binding to the major NLS binding site. Our results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants.
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