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

The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

3.2K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
3.2K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

4.2K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
4.2K
Protein Complex Assembly02:41

Protein Complex Assembly

17.1K
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...
17.1K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.8K
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...
2.8K
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

6.0K
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
6.0K

You might also read

Related Articles

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

Sort by
Same author

IFI16 restricts SARS-CoV-2 replication by disrupting nucleocapsid-driven phase separation.

Communications biology·2026
Same author

Knockout of the LRRK2-counteracting RAB phosphatase PPM1H disrupts axonal autophagy and exacerbates alpha-synuclein aggregation.

Cell reports·2026
Same author

Direct interaction between TDP-43 and Tau promotes their co-condensation, while suppressing Tau fibril formation and seeding.

The EMBO journal·2025
Same author

Synthetic chaperone based on Hsp90-Tau interaction inhibits Tau aggregation and rescues physiological Tau-Microtubule interaction.

Nature communications·2025
Same author

A novel alpha-synuclein G14R missense variant is associated with atypical neuropathological features.

Molecular neurodegeneration·2025
Same author

A Novel α-Synuclein K58N Missense Variant in a Patient with Parkinson's Disease.

Movement disorders : official journal of the Movement Disorder Society·2025
Same journal

Turbulent flow in a vortex separator with a directed pipe inlet.

Scientific reports·2026
Same journal

Systematic characteristic evaluation of clay-based cementitious material derived from calcium carbide residue and waste tile powder.

Scientific reports·2026
Same journal

Retraction Note: Improvement of a rapid diagnostic application of monoclonal antibodies against avian influenza H7 subtype virus using Europium nanoparticles.

Scientific reports·2026
Same journal

Applying large language models to spam detection in the Kazakh low-resource language setting.

Scientific reports·2026
Same journal

An open-source 3D printing system enabling in-situ freeze-thaw processing of hydrogels.

Scientific reports·2026
Same journal

An enhanced EfficientNet framework for automated waste classification using cosine annealing and label smoothing.

Scientific reports·2026
See all related articles

Related Experiment Video

Updated: Apr 6, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K

Structures of intermediates during RES complex assembly.

Piotr Wysoczanski1, Stefan Becker1, Markus Zweckstetter2

  • 1Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Scientific Reports
|July 28, 2015
PubMed
Summary
This summary is machine-generated.

The spliceosome

More Related Videos

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe
08:07

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

1.1K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

20.6K

Related Experiment Videos

Last Updated: Apr 6, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

7.0K
Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe
08:07

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

1.1K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

20.6K

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • The spliceosome's function relies on the dynamic assembly and disassembly of its protein components.
  • The Retention and Splicing (RES) complex exhibits strong cooperativity, with over 100-fold affinity changes during assembly, impacting RNA binding.
  • The RES complex, comprising Snu17p, Pml1p, and Bud13p, is crucial for splicing regulation and pre-mRNA retention.

Purpose of the Study:

  • To elucidate the three-dimensional structure and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimeric complexes.
  • To understand the molecular basis of the cooperative assembly of the RES complex.

Main Methods:

  • Liquid state Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the structures and dynamics of the dimeric complexes.
  • Analysis of structural and dynamic changes during the assembly pathway of the RES trimer.

Main Results:

  • The study determined the 3D structures and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimers.
  • Localized and global structural changes were observed throughout the RES trimer assembly pathway.
  • Stepwise rigidification of Snu17p upon binding of Pml1p and Bud13p was identified.

Conclusions:

  • The observed stepwise rigidification of Snu17p provides a structural basis for the high cooperativity in RES complex assembly.
  • Understanding these dynamics is key to comprehending spliceosome regulation and function.