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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Membrane Asymmetry Regulating Transporters

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
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Updated: Jun 28, 2025

Single-Molecule Imaging of Nuclear Transport
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Single-Molecule Imaging of Nuclear Transport

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Kinetic cooperativity resolves bidirectional clogging within the nuclear pore complex.

Tiantian Zheng1, Anton Zilman1

  • 1Department of Physics, University of Toronto, Toronto, ON, Canada.

Biophysical Journal
|April 19, 2024
PubMed
Summary
This summary is machine-generated.

Radial segregation does not improve nuclear pore complex (NPC) transport efficiency. Surprisingly, Nuclear Transport Receptor (NTR) crowding enhances NPC transport by self-regulating cargo density and flux, offering insights for artificial nanopore design.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Computational Biology

Background:

  • The nuclear pore complex (NPC) regulates nucleocytoplasmic transport, a critical process in eukaryotic cells.
  • Efficient bidirectional transport faces challenges due to competing import and export fluxes.
  • Radial segregation of fluxes has been proposed as a mechanism to enhance NPC transport efficiency.

Purpose of the Study:

  • To investigate the impact of radial segregation on bidirectional transport efficiency through the NPC.
  • To explore alternative mechanisms for efficient NPC transport.

Main Methods:

  • Utilized a coarse-grained computational model of the NPC.
  • Simulated bidirectional transport fluxes under varying conditions.

Main Results:

  • Found minimal evidence that radial segregation improves NPC transport efficiency.
  • Observed that Nuclear Transport Receptor (NTR) crowding unexpectedly enhances transport efficiency despite reduced pore space.
  • Identified self-regulation of cargo density and flux as a mechanism for crowding-induced transport cooperativity.

Conclusions:

  • Radial segregation is not the primary mechanism for efficient NPC transport.
  • NTR crowding promotes transport cooperativity, resolving challenges in bidirectional transport.
  • Findings offer insights for designing efficient artificial nanopores.