ArticleProtein science : a publication of the Protein Society2020
Nucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Molecular modelling and gene expression analysis to probe the GT-γ trihelix transcription factors in Solanum tuberosum under drought stress.Scientific reports · 2025Article
- Dynamics of nuclear export of pre-ribosomal subunits revealed by high-speed single-molecule microscopy in live cells.iScience · 2023Article
- Application of Super-resolution SPEED Microscopy in the Study of Cellular Dynamics.Chemical & biomedical imaging · 2023Review
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Obtaining 3D super-resolution images by utilizing rotationally symmetric structures and 2D-to-3D transformation.Computational and structural biotechnology journal · 2023Review
- Nuclear RNA binding regulates TDP-43 nuclear localization and passive nuclear export.Cell reports · 2022Article
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- Nuclear Import of Adeno-Associated Viruses Imaged by High-Speed Single-Molecule Microscopy.Viruses · 2021Review
- High-speed super-resolution imaging of rotationally symmetric structures using SPEED microscopy and 2D-to-3D transformation.Nature protocols · 2021Article
- The Paralogue of the Intrinsically Disordered Nuclear Protein 1 Has a Nuclear Localization Sequence that Binds to Human Importin α3.International journal of molecular sciences · 2020Article
- A Phosphorylation-Induced Switch in the Nuclear Localization Sequence of the Intrinsically Disordered NUPR1 Hampers Binding to Importin.Biomolecules · 2020Article
- Nucleocytoplasmic transport of intrinsically disordered proteins studied by high-speed super-resolution microscopy.Protein science : a publication of the Protein Society · 2020Article
- NovelFrontiers in genetics · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Both natively folded and intrinsically disordered proteins (IDPs) destined for the nucleus need to transport through the nuclear pore complexes (NPCs) in eukaryotic cells. NPCs allow for passive diffusion of small folded proteins while barricading large ones, unless they are facilitated by nuclear transport receptors. However, whether nucleocytoplasmic transport of IDPs would follow these rules remains unknown. By using a high-speed super-resolution fluorescence microscopy, we have measured transport kinetics and 3D spatial locations of transport routes through native NPCs for various IDPs. Our data revealed that the rules executed for folded proteins are not well followed by the IDPs. Instead, both large and small IDPs can passively diffuse through the NPCs. Furthermore, their diffusion efficiencies and routes are differentiated by their content ratio of charged (Ch) and hydrophobic (Hy) amino acids. A Ch/Hy-ratio mechanism was finally suggested for nucleocytoplasmic transport of IDPs.
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Registered trials
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