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

Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.6K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

4.3K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
4.3K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.3K
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...
3.3K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

9.9K
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...
9.9K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.0K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.0K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

10.8K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
10.8K

You might also read

Related Articles

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

Sort by
Same author

Clearance and secretion of α-synuclein by RTN3L-mediated endoplasmic reticulum autophagy.

Molecular biology of the cell·2026
Same author

How Host Phylogeny, Diet, and Habitat Affect Gut Microbial Diversity in Wild Snakes.

Ecology and evolution·2026
Same author

Receptor-cargo coupling during ER-autophagy depends on coat proteins and ER membrane properties.

Autophagy·2026
Same author

Coupling of cargo to the autophagy receptor is a critical step in ER-phagy.

Science advances·2026
Same author

The Present and Future of THERANOSTICS.

Asia-Pacific journal of clinical oncology·2026
Same author

Characteristics and Prognostic Implications in Newly Diagnosed KMT2Ar AML: A Multicenter Study of the ECLA Group.

American journal of hematology·2026

Related Experiment Video

Updated: Mar 12, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

3.1K

TRAPPI tethers COPII vesicles by binding the coat subunit Sec23.

Huaqing Cai1, Sidney Yu, Shekar Menon

  • 1Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06519, USA.

Nature
|February 9, 2007
PubMed
Summary

The TRAPP I tethering complex binds to the COPII coat subunit Sec23, mediated by Bet3. This interaction targets TRAPP I to vesicles, facilitating their fusion with target membranes.

More Related Videos

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

14.5K
In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

15.1K

Related Experiment Videos

Last Updated: Mar 12, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

3.1K
Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

14.5K
In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

15.1K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Vesicle budding from the endoplasmic reticulum (ER) relies on the COPII coat complex.
  • Coat assembly involves Sar1-GTP, Sec23/24 adaptors, and the Sec13/31 polymerization complex.
  • Vesicle tethering to target membranes is mediated by specific tethering factors.

Purpose of the Study:

  • To investigate the interaction between vesicle tethering machinery and the COPII coat.
  • To identify the molecular components involved in targeting tethers to COPII vesicles.
  • To understand how tethering complexes are recruited to transport vesicles.

Main Methods:

  • Biochemical assays in yeast and mammalian cell extracts.
  • In vitro binding studies.
  • Analysis of protein-protein interactions between coat and tethering factors.

Main Results:

  • The TRAPP I tethering complex directly binds to the COPII coat subunit Sec23.
  • This interaction is dependent on the Bet3 subunit of TRAPP I.
  • In vitro studies confirm that Sec23-Bet3 interaction targets TRAPP I to COPII vesicles for tethering.

Conclusions:

  • TRAPP I is recruited to COPII vesicles via interaction with Sec23, mediated by Bet3.
  • This mechanism ensures proper tethering of vesicles to their target membranes.
  • The coat complex and its associated cargo play a role in determining vesicle destination.