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

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...
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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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...

You might also read

Related Articles

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

Sort by
Same author

The Molecular Logic of Immunoglobulin Heavy Chain Class Switch Recombination.

Annual review of immunology·2026
Same author

Loss of <i>Sun2</i> ablates nuclear mechanosensing-driven extracellular matrix production and mitigates lung fibrosis.

bioRxiv : the preprint server for biology·2026
Same author

Components of an ESCRT-independent nuclear envelope assembly pathway.

bioRxiv : the preprint server for biology·2026
Same author

The LINC complex component Kms1 and CENP-B protein Cbp1 cooperate to enforce faithful homology-directed DNA repair at the nuclear periphery in <i>S. pombe</i>.

Genes & development·2025
Same author

The LINC complex component Kms1 and CENP-B protein Cbp1 cooperate to enforce faithful homology-directed DNA repair at the nuclear periphery in <i>S. pombe</i>.

bioRxiv : the preprint server for biology·2025
Same author

Nuclear mechanics as a determinant of nuclear pore complex plasticity.

Nature cell biology·2025

Related Experiment Video

Updated: Jun 4, 2026

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

Lumenal interactions in nuclear pore complex assembly and stability.

William T Yewdell1, Paolo Colombi, Taras Makhnevych

  • 1Howard Hughes Medical Institute, New York, NY 10065, USA.

Molecular Biology of the Cell
|February 25, 2011
PubMed
Summary

Nuclear pore complex assembly is clarified by studying Heh1p and Heh2p proteins. These LEM proteins interact with nucleoporins, suggesting a role in nuclear pore complex structure and stability.

Related Experiment Videos

Last Updated: Jun 4, 2026

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear pore complexes (NPCs) regulate macromolecule transport across the nuclear envelope (NE).
  • The precise mechanisms governing NPC assembly remain incompletely understood.
  • Integral inner nuclear membrane proteins, such as Heh1p and Heh2p, are implicated in nuclear envelope organization.

Purpose of the Study:

  • To investigate the role of Heh1p and Heh2p in NPC assembly and function.
  • To identify genetic and physical interactions between Heh1/Heh2p and NPC components.
  • To elucidate the contribution of specific protein domains to NPC formation.

Main Methods:

  • Analysis of nucleoporin distribution in yeast strains lacking Heh1p and Heh2p.
  • Genetic interaction studies between HEH1/HEH2 and NPC genes.
  • Protein interaction assays, including co-immunoprecipitation.
  • Functional analysis of Heh1p domains in rescue experiments.

Main Results:

  • Absence of Heh1p and Heh2p leads to defects in nucleoporin localization.
  • Specific genetic interactions link HEH1/HEH2 to membrane, inner, and outer ring nucleoporins.
  • A lumenal domain of Heh1p can rescue nucleoporin mislocalization and growth defects.
  • Physical interaction identified between Heh1p lumenal domain and Pom152p.

Conclusions:

  • Heh1p and Heh2p are crucial for proper nucleoporin distribution and NPC assembly.
  • Heh1p may contribute to NPC stability by forming a lumenal bridge with Pom152p.
  • These findings provide new insights into the molecular mechanisms of nuclear pore complex biogenesis.