23 results found
    1. Structural Biology and Molecular Biophysics

    Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

    Adithya N Ananth et al.
    Biomimetic nanopores reveal that the sequence-dependent spatial distribution of intrinsically disordered proteins plays a crucial role in establishing the selective permeability barrier of the nuclear pore complex.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Extensive cargo identification reveals distinct biological roles of the 12 importin pathways

    Makoto Kimura et al.
    Transport-based high-throughput identification of cargo proteins specific to all 12 human importin-β family nuclear import receptors revealed biological processes that the cargo cohorts of each receptor are involved in.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Investigating molecular crowding within nuclear pores using polarization-PALM

    Guo Fu et al.
    The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner

    Alan R Lowe et al.
    The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors

    Kasper R Andersen et al.
    Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.
  1. Nuclear pore assembly proceeds by an inside-out extrusion of the nuclear envelope

    Shotaro Otsuka et al.
    Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.
    1. Cell Biology

    Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9

    Juliana S Capitanio et al.
    Mechanistic insight into the role of intranuclear Nup98 in gene expression is revealed by functional interactions with the helicase DHX9.
    1. Cell Biology
    2. Chromosomes and Gene Expression

    Chromatin-prebound Crm1 recruits Nup98-HoxA9 fusion to induce aberrant expression of Hox cluster genes

    Masahiro Oka et al.
    Nup98-HoxA9 is recruited to Hox gene cluster regions together with the chromosomally pre-bound nuclear export factor Crm1, which induces aberrant expression of several Hox genes and affecting the differentiation of embryonic stem cells.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    The molecular mechanism of nuclear transport revealed by atomic-scale measurements

    Loren E Hough et al.
    NMR spectroscopy has been used to explain a central unresolved issue of nuclear transport, namely how it can be both fast and specific.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

    Hermann Broder Schmidt, Dirk Görlich
    How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.

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