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Related Concept Videos

Vesicular Tubular Clusters01:45

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...
COP Coated Vesicles00:59

COP Coated Vesicles

Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
ER Retrieval Pathway01:45

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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Related Experiment Video

Updated: Jun 20, 2026

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

A link between ER tethering and COP-I vesicle uncoating.

Sabrina Zink1, Dirk Wenzel, Christian A Wurm

  • 1Department Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, D37077, Germany.

Developmental Cell
|September 18, 2009
PubMed
Summary
This summary is machine-generated.

The Dsl1p vesicle tethering complex binds COP-I subunits, mediating Golgi-derived vesicle tethering and fusion. This interaction also aids COP-I uncoating, preventing aggregate formation.

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SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Related Experiment Videos

Last Updated: Jun 20, 2026

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Area of Science:

  • Cell biology
  • Molecular and cell biology

Background:

  • The Dsl1p complex (Dsl1p, Dsl3p, Tip20p) tethers Golgi-derived COP-I vesicles to the endoplasmic reticulum.
  • This complex associates with Q-SNAREs and interacts with COP-I subunits.

Purpose of the Study:

  • To investigate the interaction between the Dsl1p complex and COP-I subunits.
  • To elucidate the role of this interaction in vesicle tethering and COP-I coat dynamics.

Main Methods:

  • Analysis of binding sites between Dsl1p and COP-I subunits.
  • Observation of vesicle trafficking in yeast cells with defects in Dsl1p/SNARE complex function.

Main Results:

  • Dsl1p binds COP-I subunits at sites crucial for COP-I coat stabilization.
  • Defects in Dsl1p/SNARE complex function lead to massive accumulation of COP-I-coated vesicles.
  • COP-II coat proteins are recruited to these accumulated vesicles.

Conclusions:

  • The Dsl1p/SNARE complex binds the COP-I coat to mediate vesicle tethering.
  • This binding also facilitates COP-I uncoating by blocking domains that promote repolymerization.
  • This dual function prevents the formation of large COP-I aggregates.