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

Amyloid Fibrils03:03

Amyloid Fibrils

9.5K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.5K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

3.8K
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
3.8K
The Proteasome01:13

The Proteasome

830
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
830
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Proteoglycans01:05

Proteoglycans

3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Protein Networks02:26

Protein Networks

3.9K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
3.9K

You might also read

Related Articles

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

Sort by
Same author

Molecular architecture of synaptic vesicles.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Mutant huntingtin impairs neurodevelopment in human brain organoids through CHCHD2-mediated neurometabolic failure.

Nature communications·2024
Same author

AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.

Molecular systems biology·2024
Same author

A proteomics analysis of 5xFAD mouse brain regions reveals the lysosome-associated protein Arl8b as a candidate biomarker for Alzheimer's disease.

Genome medicine·2023
Same author

The polyphenol EGCG directly targets intracellular amyloid-β aggregates and promotes their lysosomal degradation.

Journal of neurochemistry·2023
Same author

CellFIE: CRISPR- and Cell Fusion-based Two-hybrid Interaction Mapping of Endogenous Proteins.

Journal of molecular biology·2021

Related Experiment Video

Updated: Jun 28, 2025

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.0K

Polyglutamine disease proteins: Commonalities and differences in interaction profiles and pathological effects.

Megan Bonsor1, Orchid Ammar1, Sigrid Schnoegl1

  • 1Department of Neuroproteomics, Max Delbrück Center for Molecular Medicine, Berlin, Germany.

Proteomics
|April 14, 2024
PubMed
Summary

Nine polyglutamine (polyQ) expansion diseases stem from trinucleotide repeat mutations. This review explores commonalities and differences in polyQ protein structure, function, and disease pathology, using AlphaFold models and interaction networks.

Keywords:
interactomepolyQ diseasepolyQ expansionprotein networksprotein structure

More Related Videos

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

2.8K
Growth Assays to Assess Polyglutamine Toxicity in Yeast
09:06

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

13.6K

Related Experiment Videos

Last Updated: Jun 28, 2025

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.0K
Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

2.8K
Growth Assays to Assess Polyglutamine Toxicity in Yeast
09:06

Growth Assays to Assess Polyglutamine Toxicity in Yeast

Published on: March 5, 2012

13.6K

Area of Science:

  • Neuroscience
  • Genetics
  • Molecular Biology

Background:

  • Nine known polyglutamine (polyQ) expansion diseases, including spinocerebellar ataxias (SCA), spinal and bulbar muscular atrophy (SBMA), dentatorubral-pallidoluysian atrophy (DRPLA), and Huntington's disease (HD), are linked to trinucleotide repeat mutations.
  • These mutations result in proteins with elongated polyQ tracts, driving pathogenesis across diverse neurodegenerative conditions.

Purpose of the Study:

  • To review and compare the nine polyQ expansion diseases, focusing on the structure and function of causative polyQ proteins.
  • To analyze pathological features and explore shared molecular mechanisms underlying these diseases.
  • To integrate insights from AlphaFold structural predictions and protein-protein interaction networks.

Main Methods:

  • Literature review of polyglutamine expansion diseases.
  • Analysis of protein structures and functions, including insights from AlphaFold predictions.
  • Examination of protein-protein interaction networks associated with polyQ proteins.

Main Results:

  • Expanded polyQ domains are a common pathogenic driver, mediating protein complex formation involved in critical cellular processes.
  • PolyQ proteins exhibit both shared and distinct structural and functional characteristics.
  • Protein-protein interaction networks reveal common interaction partners and pathways relevant to disease development.

Conclusions:

  • Understanding the commonalities and differences in polyQ proteins and their interactions is crucial for deciphering disease mechanisms.
  • AlphaFold models and interaction network analysis provide valuable insights into polyQ protein biology and disease pathogenesis.
  • Further research into shared pathways may reveal therapeutic targets for multiple polyQ expansion diseases.