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...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles, paraspeckles, etc. These nuclear...
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...
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...
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

Evaluation of a serum protein signature as monitoring biomarker for Duchenne muscular dystrophy in a long-term clinical trial with corticosteroids.

Skeletal muscle·2026
Same author

Quantitative tandem mass tag-based serum proteomics for longitudinal biomarker monitoring in Duchenne muscular dystrophy.

Clinical proteomics·2026
Same author

MDBiomarkers: A queryable biomarkers database integrating multiple serum and tissue datasets for Duchenne muscular dystrophy.

Journal of neuromuscular diseases·2026
Same author

Quantification of a serum titin fragment reflects dystrophin restoration in mdx mice and disease severity in patients with dystrophinopathies.

Journal of neuromuscular diseases·2026
Same author

Nanoscopic analysis of tight junction organization in in vitro blood-brain barrier models.

Fluids and barriers of the CNS·2026
Same author

A muscular dystrophy associated with bi-allelic LEMD2 variants: Expanding the genotype of nuclear envelopathies.

Brain pathology (Zurich, Switzerland)·2026

Related Experiment Video

Updated: Jun 29, 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

Sun1 forms immobile macromolecular assemblies at the nuclear envelope.

Wenshu Lu1, Josef Gotzmann, Lucia Sironi

  • 1Center for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany.

Biochimica Et Biophysica Acta
|October 11, 2008
PubMed
Summary

SUN-domain proteins like Sun1 form immobile complexes at the nuclear envelope. These SUN proteins self-associate and interact with Sun2, potentially linking the nucleus to the cytoskeleton.

More Related Videos

A Cell Free Assay to Study Chromatin Decondensation at the End of Mitosis
11:04

A Cell Free Assay to Study Chromatin Decondensation at the End of Mitosis

Published on: December 19, 2015

Related Experiment Videos

Last Updated: Jun 29, 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

A Cell Free Assay to Study Chromatin Decondensation at the End of Mitosis
11:04

A Cell Free Assay to Study Chromatin Decondensation at the End of Mitosis

Published on: December 19, 2015

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • SUN-domain proteins are conserved inner nuclear membrane proteins connecting the nucleoplasm and cytoskeleton.
  • These proteins play crucial roles in nuclear envelope structure and function.

Purpose of the Study:

  • To investigate the oligomeric state and dynamics of Sun1 proteins at the nuclear envelope.
  • To elucidate the structural features and interactions of Sun1 that maintain its immobility and facilitate complex formation.

Main Methods:

  • Inverse fluorescence recovery after photobleaching (iFRAP) to assess protein dynamics in vivo.
  • Analysis of Sun1 protein segments, including the C-terminal coiled-coil domain.
  • Immunofluorescence microscopy to study colocalization with nuclear pore complex proteins and Sun2.

Main Results:

  • Sun1 proteins form highly immobile oligomeric complexes at the nuclear envelope in interphase cells.
  • Both perinuclear and nucleoplasmic segments of Sun1 are critical for its immobility.
  • The C-terminal coiled-coil domain of Sun1 self-associates into dimers and tetramers, and mediates heterophilic interactions with Sun2.
  • Sun1 colocalizes with nuclear pore complexes and Sun2, forming distinct assemblies at the inner nuclear membrane.

Conclusions:

  • Sun1 acts as a non-dynamic platform at the inner nuclear membrane for macromolecular assembly.
  • SUN-protein complexes may serve as attachment sites for cytoskeletal filaments to the outer nuclear membrane.
  • These findings advance our understanding of nuclear envelope organization and the physical links between the nucleus and cytoplasm.