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Related Concept Videos

Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

3.4K
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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Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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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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Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
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GTPases and their Regulation02:14

GTPases and their Regulation

8.6K
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Related Experiment Video

Updated: Sep 10, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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The small GTPase Ran defines nuclear pore complex asymmetry.

Jenny Sachweh1, Mandy Börmel2, Sven Klumpe3

  • 1Department of Molecular Sociology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Cell
|August 19, 2025
PubMed
Summary
This summary is machine-generated.

Nuclear pore complexes (NPCs) are key to nucleocytoplasmic exchange. This study reveals how NPCs achieve asymmetric structure from a symmetric scaffold, controlled by the Ran GTPase, suggesting a self-regulatory transport system.

Keywords:
Ran GTPaseasymmetrybiogenesiscryo-ETheterogeneityin situ structural biologynuclear envelopenuclear pore complexnucleoporins

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Related Experiment Videos

Last Updated: Sep 10, 2025

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Analyzing the Function of Small GTPases by Microinjection of Plasmids into Polarized Epithelial Cells
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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
  • NPCs exhibit asymmetric structures crucial for directional transport.
  • The assembly of these asymmetric structures onto a symmetric scaffold remained poorly understood.

Purpose of the Study:

  • To elucidate the mechanism of asymmetric nuclear pore complex assembly.
  • To investigate the role of the Ran GTPase in NPC structure and function.
  • To understand the self-regulatory nature of the nuclear transport system.

Main Methods:

  • Cryo-electron tomography
  • Subtomogram averaging
  • Template matching
  • Live imaging in budding yeast and Drosophila
  • Genetic induction of ectopic nuclear pores

Main Results:

  • Ectopic nuclear pores formed outside the nuclear envelope were found to be symmetric.
  • The peripheral structure of NPCs is influenced by the nucleotide state of the Ran GTPase.
  • Evidence suggests a unified mechanism controls both NPC transport and composition.

Conclusions:

  • The nuclear transport system is self-regulatory.
  • The same molecular mechanism governs both nucleocytoplasmic transport and the composition of the transport channel.
  • Ran GTPase plays a critical role in establishing NPC asymmetry.