Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.8K
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...
4.8K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
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...
2.5K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

7.1K
Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
7.1K
Nuclear Export01:42

Nuclear Export

3.7K
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...
3.7K
Protein Complex Assembly02:41

Protein Complex Assembly

12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

4.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
4.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multiple Protein-Protein Interactions Drive the Assembly and Budding of the Chikungunya Virion.

ACS infectious diseases·2026
Same author

Effects of rim fluctuations in classical nucleation theory of virus capsids.

The Journal of chemical physics·2026
Same author

Clustering of SARS-CoV-2 membrane proteins in lipid bilayer membranes.

PLoS computational biology·2026
Same author

Membrane-bound cargo carried by teams of motors with heterogeneous velocities goes faster and further.

Biophysical journal·2026
Same author

Encapsulation of fragmented cargo by virus coat proteins.

The Journal of chemical physics·2026
Same author

Universal energy equalization under Haar-random unitary operations.

Physical review. E·2026
Same journal

Tau protein differentially affects Piezo1 and Kir2.1 channels in brain capillary endothelial cells.

Biophysical journal·2026
Same journal

Emergent Intercellular Junction Stability during Cyclic Tissue Loading.

Biophysical journal·2026
Same journal

Enhanced-Sampling Simulations Reveal Distinct Intermediates in SARS-CoV-2 FSE Pseudoknot Interconversion.

Biophysical journal·2026
Same journal

Structure-based simulations of the full Flock House virus capsid reveal pathways and energetics of an infection-critical peptide externalization event.

Biophysical journal·2026
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
See all related articles

Related Experiment Video

Updated: Apr 30, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

3.5K

Nuclear pore complex protein sequences determine overall copolymer brush structure and function.

David Ando1, Roya Zandi2, Yong Woon Kim3

  • 1Department of Physics, University of California at Merced, Merced, California.

Biophysical Journal
|May 9, 2014
PubMed
Summary
This summary is machine-generated.

Nuclear pore complex (NPC) proteins form a unique polymer brush structure. This structure

More Related Videos

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

6.8K
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K

Related Experiment Videos

Last Updated: Apr 30, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

3.5K
Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

6.8K
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Biology

Background:

  • Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
  • Nucleoporins (nups) form the NPC structure but their collective organization is poorly understood due to their disordered nature.

Purpose of the Study:

  • To elucidate the structural organization of nucleoporins within the NPC.
  • To understand how nucleoporin disorder contributes to nuclear transport regulation.

Main Methods:

  • Coarse-grained simulations of individual nucleoporins and grafted rings.
  • Polymer brush modeling to mimic NPC geometry.
  • Analysis of protein disorder and interaction energies.

Main Results:

  • Individual nucleoporins exhibit distinct forms of disorder in different regions.
  • A higher-order polymer brush architecture is formed by nucleoporins.
  • Distinct brush morphologies arise based on interactions between phenylalanine glycine (FG) domains.
  • Transitions between brush morphologies are influenced by transport factors.

Conclusions:

  • The block structure of individual nucleoporins is crucial for NPC architecture.
  • Modulation of FG domain interactions can regulate nuclear transport.
  • This suggests novel mechanisms for gated transport across membrane pores with biomimetic potential.