Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors.

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Structure

• Publication date

  2007-08-14

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.STR.2007.06.011PMID 17698002
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Nanomechanical interactions of phenylalanine-glycine nucleoporins studied by single molecule force-volume spectroscopy.

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• Association of nuclear pore FG-repeat domains to NTF2 import and export complexes.

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• Karyopherin flexibility in nucleocytoplasmic transport.

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• Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport.

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• Dynamic nuclear pore complexes: life on the edge.

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• Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling

  2005cited by this paper
• Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p.

  2005cited by this paper
• Binding dynamics of isolated nucleoporin repeat regions to importin-beta.

  2005cited by this paper
• The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding.

  2005cited by this paper
• Modularity within the architecture of the nuclear pore complex.

  2005cited by this paper
• Scalable molecular dynamics with NAMD

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• Mechanisms of Receptor‐Mediated Nuclear Import and Nuclear Export

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• Translocation Through the Nuclear Pore Complex: Selectivity and Speed by Reduction‐of‐Dimensionality

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• Structural basis for the assembly of a nuclear export complex

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• Nuclear Pore Complex Structure and Dynamics Revealed by Cryoelectron Tomography

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• Nuclear export of RNA

  2004cited by this paper
• Minimal nuclear pore complexes define FG repeat domains essential for transport

  2004cited by this paper
• Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2.

  2004cited by this paper
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• Components of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture

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• Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats.

  2003cited by this paper
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• Binding Dynamics of Structural Nucleoporins Govern Nuclear Pore Complex Permeability and May Mediate Channel Gating

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• Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport.

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• Virtual gating and nuclear transport: the hole picture.

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• Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle.

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• Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded

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• Accelerating the Rate of Disassembly of Karyopherin·Cargo Complexes*

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• GLFG and FxFG Nucleoporins Bind to Overlapping Sites on Importin-β*

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• Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats

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• Functional Analysis of the Hydrophobic Patch on Nuclear Transport Factor 2 Involved in Interactions with the Nuclear Porein Vivo *

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• Dissecting the Interactions between NTF2, RanGDP, and the Nucleoporin XFXFG Repeats*

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• Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking.

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• Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex.

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• Selective Disruption of Nuclear Import by a Functional Mutant Nuclear Transport Carrier

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• Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP.

  1999cited by this paper
• Interactions between a Nuclear Transporter and a Subset of Nuclear Pore Complex Proteins Depend on Ran GTPase

  1999cited by this paper
• β-Subunit of Nuclear Pore-targeting Complex (Importin-β) Can Be Exported from the Nucleus in a Ran-independent Manner*

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• A Role for RanBP1 in the Release of CRM1 from the Nuclear Pore Complex in a Terminal Step of Nuclear Export

  1999cited by this paper
• The direction of transport through the nuclear pore can be inverted.

  1999cited by this paper
• Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2.

  1998cited by this paper
• Cse1p functions as the nuclear export receptor for importin alpha in yeast.

  1998cited by this paper
• Ran and Nuclear Transport*

  1998cited by this paper
• Cse1p Is Involved in Export of Yeast Importin α from the Nucleus

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• Cse1p Is Required for Export of Srp1p/Importin-α from the Nucleus in Saccharomyces cerevisiae *

  1998cited by this paper
• Cselp functions as the nuclear export receptor for importin α in yeast

  1998cited by this paper
• Major Binding Sites for the Nuclear Import Receptor Are the Internal Nucleoporin Nup153 and the Adjacent Nuclear Filament Protein Tpr

  1998cited by this paper
• Cse1p is involved in export of yeast importin alpha from the nucleus.

  1998cited by this paper
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  1995cited by this paper
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