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

Overview of Exosomes01:36

Overview of Exosomes

3.4K
Exosomes are stable, lipid bilayer-enclosed vesicles capable of crossing biological barriers. They can carry a wide range of molecules required for intercellular communication. Once exosomes are released from the cell where they originated, they enter a recipient cell through various pathways such as fusion, receptor-mediated endocytosis, macropinocytosis, and phagocytosis.
Stahl et al. discovered exosomes in 1983, but the exosomes were initially considered waste products released from the...
3.4K
The Proteasome01:13

The Proteasome

1.5K
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...
1.5K
The Proteasome02:18

The Proteasome

9.9K
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...
9.9K
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

4.6K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
4.6K
Regulated Protein Degradation02:58

Regulated Protein Degradation

8.6K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.6K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.9K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
4.9K

You might also read

Related Articles

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

Sort by
Same author

The impact of endocrine disrupting chemicals diethylstilbestrol and ketoconazole on lipid storage in in vitro matured bovine cumulus-oocyte complexes.

Biology of reproduction·2026
Same author

Protocol for fibrin-based endothelial-cardiomyocyte co-culture in a microfluidic device.

STAR protocols·2026
Same author

Uptake of polystyrene nanoplastics by cumulus-oocyte complexes impairs oocyte and embryo development.

Reproductive toxicology (Elmsford, N.Y.)·2026
Same author

Bioorthogonal click chemistry to visualize an immunogenic HLA-A2-restricted hepatitis B virus epitope in human monocyte-derived dendritic cells.

Journal of immunology (Baltimore, Md. : 1950)·2025
Same author

Author Correction: Geometric deep learning improves generalizability of MHC-bound peptide predictions.

Communications biology·2025
Same author

HLA I immunopeptidome of synthetic long peptide pulsed human dendritic cells for therapeutic vaccine design.

NPJ vaccines·2025

Related Experiment Video

Updated: Jan 1, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

3.0K

Exosomes contain ubiquitinated proteins.

Sonja I Buschow1, Jolanda M P Liefhebber, Richard Wubbolts

  • 1Department of Biochemistry and Cell Biology, Faculty of Veterinary Medicine, and Institute of Biomembranes, University of Utrecht, PO Box 80176, Utrecht 3508 TD, The Netherlands.

Blood Cells, Molecules & Diseases
|October 6, 2005
PubMed
Summary

Exosomes, secreted vesicles originating from multivesicular bodies (MVBs), were found to contain polyubiquitinated proteins. This discovery suggests ubiquitinated proteins can be incorporated into the MVB pathway and serve as exosome markers.

More Related Videos

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.3K
Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 18, 2009

43.5K

Related Experiment Videos

Last Updated: Jan 1, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

3.0K
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.3K
Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 18, 2009

43.5K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Endosomal Sorting

Background:

  • Multivesicular bodies (MVBs) are endosomal compartments containing luminal vesicles formed by inward budding.
  • Protein sorting into luminal vesicles typically involves monoubiquitination, with tags removed before vesicle formation.
  • Exosomes are secreted vesicles derived from MVBs, implying a similar protein composition to luminal vesicles.

Purpose of the Study:

  • To investigate the ubiquitination status of proteins within exosomes.
  • To determine if polyubiquitinated proteins are present in exosomes.
  • To explore the potential of ubiquitinated proteins as exosome markers.

Main Methods:

  • Analysis of exosome protein composition.
  • Comparison of ubiquitinated protein enrichment in exosomes versus total cell lysates.

Main Results:

  • Exosomes were found to contain polyubiquitinated proteins.
  • Many of these polyubiquitinated proteins were not membrane-integrated.
  • Polyubiquitinated proteins were relatively enriched in exosomes compared to total cell lysates.

Conclusions:

  • A subset of polyubiquitinated cytoplasmic proteins is incorporated into the multivesicular body pathway.
  • Ubiquitinated proteins can serve as reliable markers for exosomes.
  • This finding has implications for understanding exosome biogenesis and function.