ArticlePlant signaling & behavior2013
The distribution of different classes of nuclear localization signals (NLSs) in diverse organisms and the utilization of the minor NLS-binding site inplantnuclear import factor importin-α.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 14 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
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Insights into FourInternational journal of molecular sciences · 2022Article
- Nuclear import of LIKE HETEROCHROMATIN PROTEIN1 is redundantly mediated by importins α-1, α-2 and α-3.The Plant journal : for cell and molecular biology · 2020Article
- Article
- Plasmonic labeling of subcellular compartments in cancer cells: multiplexing with fine-tuned gold and silver nanoshells.Chemical science · 2017Article
- Analysis of origin and protein-protein interaction maps suggests distinct oncogenic role of nuclear EGFR during cancer evolution.Journal of Cancer · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The specific recognition between the import receptor importin-α and the nuclear localization signals (NLSs) is crucial to ensure the selective transport of cargoes into the nucleus. NLSs contain 1 or 2 clusters of positively charged amino acids, which usually bind to the major (monopartite NLSs) or both minor and major NLS-binding sites (bipartite NLSs). In our recent study, we determined the structure of importin-α1a from rice (Oryza sativa), and made 2 observations that suggest an increased utilization of the minor NLS-binding site in this protein. First, unlike the mammalian protein, both the major and minor NLS-binding sites are auto-inhibited in the unliganded rice protein. Second, we showed that NLSs of the "plant-specific" class preferentially bind to the minor NLS-binding site of rice importin-α. Here, we show that a distinct group of "minor site-specific" NLSs also bind to the minor site of the rice protein. We further show a greater enrichment of proteins containing these "plant-specific" and "minor site-specific" NLSs in the rice proteome. However, the analysis of the distribution of different classes of NLSs in diverse eukaryotes shows that in all organisms, the minor site-specific NLSs are much less prevalent than the classical monopartite and bipartite NLSs.
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