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

4.7K
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...
4.7K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.4K
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...
2.4K
Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
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...
10.6K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.6K
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...
3.6K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

7.7K
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...
7.7K
The Nucleolus02:55

The Nucleolus

8.9K
The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
8.9K

You might also read

Related Articles

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

Sort by
Same author

Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.

The Journal of cell biology·2025
Same author

Integrative Chemical Genetics Platform Identifies Condensate Modulators Linked to Neurological Disorders.

bioRxiv : the preprint server for biology·2025
Same author

Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities.

Nature cell biology·2022
Same author

The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis.

Nature cell biology·2022
Same author

p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells.

International journal of molecular sciences·2022
Same author

The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease.

Biomolecules·2020

Related Experiment Video

Updated: Jul 18, 2025

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

10.3K

Coordinating nucleoporin condensation and nuclear pore complex assembly.

E F Elsiena Kuiper1, Sarah M Prophet1, Christian Schlieker1,2

  • 1Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT, USA.

FEBS Letters
|August 24, 2023
PubMed
Summary

Understanding nuclear pore complex (NPC) assembly is crucial, as defects link to diseases like ALS. Controlled condensation of key proteins is vital to prevent harmful aggregation during NPC biogenesis.

Keywords:
condensationfusogenmembrane fusionmolecular chaperonesnuclear envelopenuclear pore complexphase separation

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

18.7K
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

7.4K

Related Experiment Videos

Last Updated: Jul 18, 2025

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

10.3K
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

18.7K
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

7.4K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The nuclear pore complex (NPC) is a large, intricate protein structure essential for eukaryotic cell function.
  • While assembly mechanisms for other large cellular machines are known, NPC assembly processes remain incompletely understood.
  • Dysfunctional NPC assembly and maintenance are implicated in severe human conditions, including neurodegenerative diseases and aging.

Purpose of the Study:

  • To review recent advancements in understanding the assembly of the nuclear pore complex.
  • To explore the connection between defects in NPC biogenesis and human disorders.
  • To propose critical regulatory steps in NPC assembly.

Main Methods:

  • Literature review of recent research on NPC assembly.
  • Analysis of genetic and molecular data linking NPC defects to human diseases.
  • Biochemical and biophysical modeling of nucleoporin condensation.

Main Results:

  • Recent studies have elucidated key steps and components involved in NPC assembly.
  • Human disorders such as dystonia and amyotrophic lateral sclerosis (ALS) provide insights into NPC biogenesis failures.
  • Aberrant condensation of phenylalanine-glycine (FG) repeat nucleoporins is a potential mechanism for NPC dysfunction.

Conclusions:

  • Controlled condensation of FG-repeat nucleoporins is essential for proper NPC assembly.
  • Preventing aberrant condensation, aggregation, or amyloid formation is critical for maintaining NPC homeostasis.
  • Further research into NPC assembly holds therapeutic potential for age-related and neurodegenerative diseases.