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Related Concept Videos

Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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...
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...
Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...

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Related Experiment Video

Updated: May 30, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

COPI budding within the Golgi stack.

Vincent Popoff1, Frank Adolf, Britta Brügger

  • 1Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany.

Cold Spring Harbor Perspectives in Biology
|August 17, 2011
PubMed
Summary
This summary is machine-generated.

Coatomer protein complexes mediate intracellular transport via COPI-coated vesicles. These vesicles bud from the Golgi apparatus, sorting lipids and cargo proteins for secretion.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Golgi apparatus is a central organelle for intracellular membrane traffic in eukaryotic cells.
  • Transport within the early secretory pathway relies on COPI-coated vesicles, distinct from clathrin-coated vesicles.
  • The small GTPase Arf1 and the coatomer complex are key regulators of COPI vesicle formation.

Purpose of the Study:

  • To elucidate the mechanisms of COPI-coated vesicle formation and cargo sorting.
  • To understand the role of Arf1 and coatomer in membrane trafficking.
  • To investigate the lipid sorting during COPI vesicle budding.

Main Methods:

  • The study likely involves biochemical assays to analyze protein-coat interactions.
  • Lipid-protein binding studies to understand cargo recognition.
  • Cellular imaging techniques to observe vesicle formation and budding.

Main Results:

  • Coatomer, a heptameric complex, is recruited by activated Arf1 to the Golgi membrane.
  • Coatomer possesses distinct binding sites for membrane proteins and cargo.
  • Lipid sorting during budding results in a liquid-disordered phase composition within COPI vesicles.
  • Cooperation between coatomer and Arf1 facilitates membrane scission for vesicle release.

Conclusions:

  • COPI vesicles play a crucial role in early secretory pathway transport.
  • Arf1 and coatomer orchestrate vesicle formation through specific protein-lipid interactions.
  • The lipid composition of COPI vesicles is actively sorted during budding.