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

Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
The Proteasome01:13

The Proteasome

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 (ubiquitin...
The Proteasome02:18

The Proteasome

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...
The Proteasome02:18

The Proteasome

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...
The Proteasome Structure01:17

The Proteasome Structure

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...
Autophagic Cell Death01:18

Autophagic Cell Death

Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and pro-apoptotic...

You might also read

Related Articles

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

Sort by
Same author

R405W Desmin Knock-In Mice Highlight Alterations of Mitochondria, Protein Quality Control and Myofibrils in Myofibrillar Myopathy.

Journal of cachexia, sarcopenia and muscle·2025
Same author

Quantification of Exercise-Induced Sarcomeric Damage in R349P Desmin Knock-In Mice: A New Approach in Myofibrillar Myopathy Research.

Neuropathology and applied neurobiology·2025
Same author

Desmin Modulates Muscle Cell Adhesion and Migration.

Frontiers in cell and developmental biology·2022
Same author

Vimentin: Regulation and pathogenesis.

Biochimie·2022
Same author

Absence of Desmin Results in Impaired Adaptive Response to Mechanical Overloading of Skeletal Muscle.

Frontiers in cell and developmental biology·2021
Same author

Dual Functional States of R406W-Desmin Assembly Complexes Cause Cardiomyopathy With Severe Intercalated Disc Derangement in Humans and in Knock-In Mice.

Circulation·2020

Related Experiment Video

Updated: May 11, 2026

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

Relationship between the proteasomal system and autophagy.

Alain Lilienbaum1

  • 1Laboratory of Stress and Pathologies of the Cytoskeleton, Unit of Functional and Adaptive Biology (BFA) affiliated with CNRS (EAC4413), University Paris Diderot-Paris 7 75250 Paris Cedex 13, France.

International Journal of Biochemistry and Molecular Biology
|May 3, 2013
PubMed
Summary

The ubiquitin-proteasome system and autophagy are key cellular protein degradation pathways. Recent research reveals these distinct systems are intricately interconnected, impacting cellular homeostasis and disease.

Keywords:
Proteasomeautophagyhomeostasisubiquitin

More Related Videos

Cell-Based Drug Screening for Inhibitors of Autophagy Related 4B Cysteine Peptidase
09:51

Cell-Based Drug Screening for Inhibitors of Autophagy Related 4B Cysteine Peptidase

Published on: June 30, 2023

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
11:39

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Published on: July 21, 2017

Related Experiment Videos

Last Updated: May 11, 2026

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

Cell-Based Drug Screening for Inhibitors of Autophagy Related 4B Cysteine Peptidase
09:51

Cell-Based Drug Screening for Inhibitors of Autophagy Related 4B Cysteine Peptidase

Published on: June 30, 2023

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
11:39

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Published on: July 21, 2017

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic cells utilize two primary protein degradation pathways: the ubiquitin-proteasome system (UPS) and autophagy.
  • The UPS typically degrades most proteins, while autophagy handles long-lived or aggregated proteins and organelles.
  • Disruptions in these pathways are linked to various diseases and impact cellular homeostasis.

Purpose of the Study:

  • To review recent advances in understanding the interplay between the ubiquitin-proteasome system and autophagy.
  • To highlight the interfacing elements that orchestrate the activities of these two major degradation pathways.
  • To discuss the implications of this interplay for cellular homeostasis and disease pathology.

Main Methods:

  • Literature review of recent scientific publications.
  • Synthesis of findings on the interactions between UPS and autophagy.
  • Discussion of molecular mechanisms and cellular consequences.

Main Results:

  • The ubiquitin-proteasome system and autophagy, once thought distinct, are now understood to be closely coordinated.
  • Several interfacing elements have been identified that regulate the crosstalk between these degradation pathways.
  • This coordinated activity is crucial for maintaining cellular homeostasis.

Conclusions:

  • The ubiquitin-proteasome system and autophagy are not independent but rather form an integrated network for protein degradation.
  • Understanding these interconnections is vital for comprehending cellular health and disease.
  • Future research should focus on the regulatory mechanisms and therapeutic potential of this integrated system.