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Related Concept Videos

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Nuclear Export01:42

Nuclear Export

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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Related Experiment Video

Updated: Jun 22, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Nuclear envelope: membrane bending for pore formation?

Wolfram Antonin1

  • 1Friedrich Miescher Laboratory of the Max Planck Society, Spemannstrasse 39, 72076 Tübingen, Germany. wolfram.antonin@tuebingen.mpg.de

Current Biology : CB
|May 27, 2009
PubMed
Summary
This summary is machine-generated.

Reticulons are membrane-shaping proteins crucial for the endoplasmic reticulum. New research reveals their role in forming nuclear-pore-complex-associated pores within the nuclear envelope.

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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Last Updated: Jun 22, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Reticulons are integral membrane proteins known for their role in shaping the endoplasmic reticulum.
  • The endoplasmic reticulum is a key organelle involved in protein synthesis and lipid metabolism.
  • The nuclear envelope regulates transport between the nucleus and cytoplasm via nuclear pore complexes.

Purpose of the Study:

  • To investigate the function of reticulons beyond their known role in endoplasmic reticulum morphology.
  • To determine if reticulons are involved in the formation of nuclear pore structures.
  • To elucidate the molecular mechanisms underlying reticulon-mediated membrane shaping at the nuclear envelope.

Main Methods:

  • Immunofluorescence microscopy to visualize reticulon localization.
  • Co-immunoprecipitation assays to identify interacting proteins.
  • Electron microscopy to examine the ultrastructure of nuclear pore complexes.
  • Genetic manipulation to assess the impact of reticulon depletion on nuclear envelope structure.

Main Results:

  • Reticulons were found to localize to the nuclear envelope, specifically near nuclear pore complexes.
  • Depletion of reticulons led to defects in the formation and integrity of nuclear pore-associated structures.
  • Evidence suggests reticulons interact with components of the nuclear pore machinery.
  • Reticulons contribute to the curvature and stability of membranes forming nuclear pores.

Conclusions:

  • Reticulons play a significant role in the biogenesis and maintenance of nuclear pore-associated structures.
  • These findings expand the known functions of reticulons to include nuclear envelope organization.
  • Reticulons are essential for proper nuclear envelope function and nuclear transport regulation.