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Clathrin Coated Vesicles

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...

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...

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...

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...

Transport Across the Golgi

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...

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Related Experiment Video

Updated: May 28, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Published on: October 20, 2014

Clathrin is required for postmitotic Golgi reassembly.

Andreea E Radulescu¹, Dennis Shields

¹Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY, USA. aradulescu@ucsd.edu

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology

|October 4, 2011

Summary

Clathrin heavy chain (CHC) is essential for rebuilding the Golgi apparatus after cell division. This protein, found on spindle poles, acts as a template for Golgi reassembly, ensuring proper cell structure.

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Last Updated: May 28, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy

Published on: October 20, 2014

In vivo and in vitro Studies of Adaptor-clathrin Interaction

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Published on: January 26, 2011

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells

Published on: February 21, 2019

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The Golgi apparatus fragments during mitosis and must reassemble post-mitosis.
The mechanisms governing Golgi reassembly remain incompletely understood.

Purpose of the Study:

To identify novel factors and mechanisms involved in postmitotic Golgi reassembly.
To investigate the role of clathrin heavy chain (CHC) in Golgi reformation.

Main Methods:

siRNA-mediated CHC knockdown
Biochemical assays
Morphological analysis using microscopy

Main Results:

Identified membrane-bound clathrin pools associated with spindle poles, distinct from previously known spindle-associated clathrin.
Demonstrated that CHC is required for the reassembly and proper morphology of the Golgi apparatus post-mitosis.
Observed that Golgi fragmentation persists in the absence of CHC, leading to disordered cellular structure.

Conclusions:

Clathrin heavy chain (CHC) plays a critical, previously unrecognized role in postmitotic Golgi reassembly.
Spindle pole-associated clathrin may serve as a template for Golgi reformation and cisternal remodeling.
CHC is indispensable for restoring the characteristic perinuclear, lace-like Golgi morphology.