Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

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...

Vesicular Tubular Clusters

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...

ER Retrieval Pathway

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

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...

Clathrin Coated Vesicles

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...

Overview of Secretory Vesicles

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...

You might also read

Related Articles

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

Sort by

Same author

K48-ubiquitin-dependent proteases cut-up post-ER proteins.

Nature communications·2026

Same author

Insulated piggyBac and FRT vectors for engineering transgenic homozygous and heterozygous eHAP cells.

Biology open·2025

Same author

Loss of HD-PTP function results in lipodystrophy, defective cellular signaling and altered lipid homeostasis.

Journal of cell science·2024

Same author

Bro1 family proteins harmonize cargo sorting with vesicle formation.

BioEssays : news and reviews in molecular, cellular and developmental biology·2022

Same author

FoxM1 insufficiency hyperactivates Ect2-RhoA-mDia1 signaling to drive cancer.

Nature cancer·2021

Same author

ANTH domains within CALM, HIP1R, and Sla2 recognize ubiquitin internalization signals.

eLife·2021

Search research articles

Related Experiment Video

Updated: Jun 23, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting.

S Brookhart Shields¹, Andrea J Oestreich, Stanley Winistorfer

¹Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52240, USA.

The Journal of Cell Biology

|April 22, 2009

Summary

Researchers discovered a new ubiquitin-binding domain in ESCRT-I, revealing coordinated action of ubiquitin-binding domains in targeting proteins to multivesicular bodies (MVBs) for sorting.

More Related Videos

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

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

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

Published on: May 10, 2022

Related Experiment Videos

Last Updated: Jun 23, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

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

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

Published on: May 10, 2022

Area of Science:

Cell Biology
Molecular Biology
Protein Trafficking

Background:

Ubiquitin sorting receptors guide ubiquitinated proteins into multivesicular bodies (MVBs).
Ubiquitin-binding domains (UBDs) are known components of endosomal sorting complexes required for transport (ESCRT).

Purpose of the Study:

Investigate the role of multiple UBDs within ESCRT complexes in MVB cargo selection.
Identify novel UBDs and their contribution to the MVB sorting pathway.

Main Methods:

Analysis of available structural information of ESCRT complexes.
Functional investigation of UBDs in the context of MVB sorting.

Main Results:

A novel UBD was identified within ESCRT-I.
This novel UBD, along with previously known UBDs, actively participates in MVB sorting.
Evidence suggests coordinated function rather than sequential action of ESCRT UBDs.

Conclusions:

ESCRT UBDs exhibit coordinated activity in MVB cargo selection.
This collective recognition mechanism allows for handling a diverse range of ubiquitinated cargo.