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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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...
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COP Coated Vesicles00:59

COP Coated Vesicles

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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...
13.7K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.8K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.7K
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: Oct 22, 2025

In vivo and in vitro Studies of Adaptor-clathrin Interaction
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In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

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Clathrin: the molecular shape shifter.

Katherine M Wood1, Corinne J Smith2

  • 1Warwick Medical School, University of Warwick, Coventry, U.K.

The Biochemical Journal
|August 26, 2021
PubMed
Summary
This summary is machine-generated.

Clathrin protein assembles into diverse lattice structures, enabling its crucial roles beyond endocytosis in cellular functions like vesicle recycling and migration. Its

Keywords:
clathrincryo-electron microscopyendocytosis

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
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Related Experiment Videos

Last Updated: Oct 22, 2025

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Clathrin is primarily known for clathrin-mediated endocytosis.
  • It also plays roles in various other cellular processes.

Purpose of the Study:

  • To review clathrin structure, vesicle formation, and diverse cellular functions.
  • To explore how clathrin's lattice-forming ability contributes to its multifaceted roles.

Main Methods:

  • Literature review of clathrin structure and function.
  • Analysis of clathrin's involvement in cellular processes.

Main Results:

  • Clathrin self-assembles into various polyhedral lattices (e.g., curved, flat, tubular).
  • These structures are utilized in synaptic vesicle recycling, hormone desensitization, spermiogenesis, cell migration, and mitosis.

Conclusions:

  • Clathrin's structural adaptability ('shapeshifting') is key to its diverse cellular functions.
  • Understanding these lattices provides insight into fundamental cellular mechanisms.