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Coat Assembly and GTPases

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 Vesicles

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...

Rab Proteins

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

Rab Cascades

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

COP Coated Vesicles

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...

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...

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Related Experiment Video

Updated: Jun 27, 2026

In Vitro Polymerization of F-actin on Early Endosomes

In Vitro Polymerization of F-actin on Early Endosomes

Published on: August 28, 2017

ArfGAP1 activity and COPI vesicle biogenesis.

Rainer Beck¹, Frank Adolf, Carolin Weimer

¹Heidelberg University Biochemistry Center, Heidelberg University, Im Neuenheimer Feld 328, Heidelberg, Germany.

Traffic (Copenhagen, Denmark)

|December 6, 2008

Summary

ADP-ribosylation factor GTPase-activating protein 1 (ArfGAP1) is not essential for coat protein I (COPI) vesicle formation. ArfGAP1 may play a novel role in membrane trafficking, distinct from COPI vesicle biogenesis.

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Area of Science:

Cell biology
Molecular and cell biology
Membrane trafficking

Background:

Coat protein I (COPI) vesicles are crucial for transport within the early secretory pathway.
COPI vesicle formation requires coatomer, ADP-ribosylation factor 1 (Arf1), and coat receptors like p24 proteins.
Conflicting reports exist regarding the involvement of ArfGAP1 in COPI vesicle biogenesis.

Purpose of the Study:

To clarify the role of ArfGAP1 in COPI vesicle formation.
To investigate the necessity of ArfGAP1 for COPI vesicle biogenesis in vitro.
To reconcile contradictory findings on ArfGAP1's function in membrane trafficking.

Main Methods:

Utilized a defined in vitro reconstitution assay to form and purify COPI vesicles.
Titrated ArfGAP1 into the assay to assess its impact on vesicle formation.
Quantified COPI vesicle yield and analyzed coat composition.

Main Results:

ArfGAP1 is not required for COPI vesicle formation, contrary to some literature.
Catalytic amounts of ArfGAP1 significantly decrease the yield of purified COPI vesicles.
Arf1, not ArfGAP1, is a stoichiometric component of the COPI coat.

Conclusions:

ArfGAP1's established role in COPI vesicle biogenesis is re-evaluated.
Findings suggest ArfGAP1 has a novel function in membrane trafficking.
Arf1 is confirmed as a stoichiometric component of the COPI coat, essential for vesicle formation.