ArticleNature communications2017
Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 49 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
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- 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
- Isothermal Titration Calorimetry for Investigating Thermodynamics of Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Understanding the role of GhRCC1.61 in flowering time in upland cotton through integrated analyses of gene family, RNA-seq, VIGS and allelic variation.Plant cell reports · 2025Article
- CanFrontiers in cellular and infection microbiology · 2025Article
- Structural basis for nuclear import of bat adeno-associated virus capsid protein.The Journal of general virology · 2024Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core.Science advances · 2024Article
- Nuclear localization signal-tagged systems: relevant nuclear import principles in the context of current therapeutic design.Chemical Society reviews · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Toxoplasma Gondii Importin α Shows Weak Auto-Inhibition.The protein journal · 2023Article
- Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Recognition of the TDP-43 nuclear localization signal by importin α1/β.Cell reports · 2022Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- MERS-CoV ORF4b employs an unusual binding mechanism to target IMPα and block innate immunity.Nature communications · 2022Article
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- Structural characterization of human importin alpha 7 in its cargo-free form at 2.5 Å resolution.Scientific reports · 2022Article
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- Types of nuclear localization signals and mechanisms of protein import into the nucleus.Cell communication and signaling : CCS · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Active nuclear import of Ran exchange factor RCC1 is mediated by importin α3. This pathway is essential to generate a gradient of RanGTP on chromatin that directs nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. Here we identify the mechanisms of importin α3 selectivity for RCC1. We find this isoform binds RCC1 with one order of magnitude higher affinity than the generic importin α1, although the two isoforms share an identical NLS-binding groove. Importin α3 uses its greater conformational flexibility to wedge the RCC1 β-propeller flanking the NLS against its lateral surface, preventing steric clashes with its Armadillo-core. Removing the β-propeller, or inserting a linker between NLS and β-propeller, disrupts specificity for importin α3, demonstrating the structural context rather than NLS sequence determines selectivity for isoform 3. We propose importin α3 evolved to recognize topologically complex NLSs that lie next to bulky domains or are masked by quaternary structures.Importin α3 facilitates the nuclear transport of the Ran guanine nucleotide exchange factor RCC1. Here the authors reveal the molecular basis for the selectivity of RCC1 for importin α3 vs the generic importin α1 and discuss the evolution of importin α isoforms.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.