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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

9.0K
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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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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...
3.0K
Protein Folding01:22

Protein Folding

125.9K
Overview
125.9K
Protein Folding01:25

Protein Folding

11.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Protein Organization01:13

Protein Organization

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Related Experiment Video

Updated: Jan 10, 2026

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

9.9K

Protein organization in clathrin trimers

T Kirchhausen, S C Harrison

    Cell
    |March 1, 1981
    PubMed
    Summary

    Researchers isolated a stable clathrin complex from calf-brain coated vesicles. This 8.6S clathrin species, composed of heavy and light chains, can self-assemble into cages without other proteins.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Structural Biology

    Background:

    • Clathrin is a key protein involved in vesicle formation.
    • Coated vesicles are essential for intracellular trafficking.

    Purpose of the Study:

    • To characterize the composition and structure of a soluble clathrin species.
    • To investigate the self-assembly properties of this clathrin species.

    Main Methods:

    • Preparation of homogeneous 8.6S clathrin from calf-brain coated vesicles.
    • Crosslinking experiments to determine subunit composition.
    • Reassembly experiments to assess self-assembly capacity.

    Main Results:

    • A homogeneous, soluble 8.6S clathrin species was successfully prepared.

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

    Published on: October 20, 2014

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    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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    Related Experiment Videos

    Last Updated: Jan 10, 2026

    Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
    08:27

    Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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

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

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  • The 8.6S clathrin is composed of three heavy chains (180,000 MW) and three light chains (33,000 and 36,000 MW).
  • Each heavy chain interacts with one light chain; light chains do not interact with each other.
  • Intact 8.6S clathrin can reassemble into cages independently.

    • Conclusions:

    • The isolated 8.6S clathrin represents a functional, self-assembling unit.
    • This finding provides insights into the structural organization of clathrin molecules.
    • The study elucidates the basic building blocks required for clathrin cage formation.