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Related Concept Videos

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...
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...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Overview of Secretory Vesicles01:33

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...
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...
Clathrin Coated Vesicles01:12

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...

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Related Experiment Video

Updated: May 11, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

Published on: June 28, 2019

COPII - a flexible vesicle formation system.

Elizabeth A Miller1, Randy Schekman

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027, USA. em2282@columbia.edu

Current Opinion in Cell Biology
|May 25, 2013
PubMed
Summary
This summary is machine-generated.

The COPII coat system facilitates endoplasmic reticulum (ER) export of large cargo proteins, not just small vesicles. Research now focuses on how coat structure adapts to cargo geometry for efficient ER export.

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Last Updated: May 11, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

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Published on: June 28, 2019

Lipid Bilayer Vesicle Generation Using Microfluidic Jetting
08:35

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Formation of Biomembrane Microarrays with a Squeegee-based Assembly Method
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • The COPII (coat complex II) system is essential for protein transport from the endoplasmic reticulum (ER).
  • Traditionally known for generating small transport vesicles, its role in exporting larger cargo is increasingly recognized.

Purpose of the Study:

  • To understand how the COPII coat adapts its structure to accommodate diverse and large cargo proteins during ER export.
  • To explore the roles of individual COPII paralogs in mammalian physiology and cargo handling.

Main Methods:

  • Utilizing high-resolution structural data, including crystal structures and cryo-electron microscopy (cryo-EM).
  • Analyzing the molecular architecture of the COPII coat and its interaction with cargo.

Main Results:

  • Atomic-level structural insights reveal COPII coat architecture.
  • The coat demonstrates adaptability to varying cargo geometries, enabling export of proteins beyond canonical vesicle size limits.

Conclusions:

  • The COPII coat possesses both structural rigidity and geometric flexibility.
  • Coat assembly and post-translational modifications are key to handling diverse ER export cargoes efficiently.