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 Proteasome02:18

The Proteasome

10.4K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.4K
The Proteasome01:13

The Proteasome

1.9K
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...
1.9K
The Proteasome02:18

The Proteasome

5.0K
5.0K
The Proteasome Structure01:17

The Proteasome Structure

2.1K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
2.1K

You might also read

Related Articles

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

Sort by
Same author

Acid ceramidase modulates the lipid profile and exacerbates sensitivity to ferroptosis in WI-38 replicative senescent cells.

Cell death & disease·2026
Same author

Sustained dysregulation of iron and glutathione homeostasis induces chronoferroptosis, a persistent ferroptotic adaptation in neuronal cells.

Cell death discovery·2026
Same author

Glomerular hyperfiltration and enhanced sensitivity to kidney ischemia reperfusion with a blunted KIM-1 response in young male aging-accelerated SAMP8 mice.

American journal of physiology. Renal physiology·2026
Same author

Neuroprotective and anti-inflammatory activity of <i>Wyethia</i> species: therapeutic potential for neurodegenerative diseases.

Frontiers in pharmacology·2026
Same author

Acid ceramidase modulates the lipid profile and exacerbates sensitivity to ferroptosis in senescent cells.

Research square·2025
Same author

Ferroptosis-related stress during aging and its relevance to disease.

GeroScience·2025

Related Experiment Video

Updated: Mar 17, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

15.1K

Proteasome Assay in Cell Lysates.

Pamela Maher1

  • 1Cellular Neurobiology, Salk Institute for Biological Studies, La Jolla, USA.

Bio-Protocol
|July 22, 2016
PubMed
Summary
This summary is machine-generated.

The ubiquitin-proteasome system (UPS) degrades proteins, crucial for cellular health. This study presents a new assay to measure proteasome activity, aiding research into neurological disorders and aging.

More Related Videos

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

7.3K
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

Related Experiment Videos

Last Updated: Mar 17, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

15.1K
Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

7.3K
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

Area of Science:

  • Cell Biology
  • Biochemistry
  • Neuroscience

Background:

  • The ubiquitin-proteasome system (UPS) is vital for protein degradation in mammalian cells, regulating critical processes like cell death and inflammation.
  • Reduced proteasome activity is linked to neurological disorders (Parkinson's, Alzheimer's, ALS, stroke) and aging, potentially causing abnormal protein accumulation.

Purpose of the Study:

  • To describe a novel assay for measuring the protein degradation activity of the proteasome.
  • To provide a tool for investigating the role of proteasome dysfunction in disease and aging.

Main Methods:

  • The assay utilizes fluorogenic substrates designed for the three main proteasome activities: chymotrypsin-like, trypsin-like, and caspase-like.
  • Proteasome-mediated cleavage of these substrates releases a fluorophore, generating a detectable signal.

Main Results:

  • The assay allows for the quantification of proteasome's degradation function.
  • Fluorescence intensity correlates with proteasome activity, enabling sensitive detection.

Conclusions:

  • This assay offers a reliable method to assess proteasome activity.
  • It can be a valuable tool for studying proteasome function in various physiological and pathological conditions, including neurodegeneration.