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Clathrin Coated Vesicles01:12

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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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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...
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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.
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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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Updated: Jan 23, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
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The AP2 adaptor enhances clathrin coat stiffness.

Michael Lherbette1, Lisa Redlingshöfer2, Frances M Brodsky2

  • 1Institute of Biological Chemistry, Biophysics and Bioengineering, School of Engineering and Physical Sciences, Heriot-Watt University, Edinburgh, UK.

The FEBS Journal
|June 15, 2019
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Summary

Clathrin coats, essential for endocytosis, are surprisingly flexible. The adaptor protein AP2 enhances clathrin coat stiffness, aiding cargo uptake during vesicle formation.

Keywords:
AFMclathrinmembrane biophysics

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Area of Science:

  • Cell biology
  • Biophysics
  • Molecular dynamics

Background:

  • Clathrin-mediated endocytosis involves forming clathrin-coated vesicles from the plasma membrane.
  • The roles of clathrin and adaptor proteins in membrane bending and curvature stabilization are debated.
  • Understanding the mechanics of clathrin coat assembly is crucial for elucidating endocytic mechanisms.

Purpose of the Study:

  • To investigate the contributions of clathrin and adaptor protein AP2 to clathrin coat stiffness.
  • To determine the mechanical properties of clathrin coats and their role in membrane deformation.
  • To clarify the interplay between clathrin coat mechanics and adaptor protein function in endocytosis.

Main Methods:

  • Utilized atomic force microscopy (AFM) to measure the stiffness of clathrin coats.
  • Compared the mechanical properties of native clathrin coats with those lacking light chain subunits.
  • Assessed the effect of adaptor protein AP2 on clathrin coat stiffness.

Main Results:

  • Clathrin coats exhibit a stiffness less than 10-fold that of the enclosed membrane, indicating a delicate balance for vesicle formation.
  • Adaptor protein AP2 increases the stiffness of native clathrin coats.
  • AP2 did not alter the stiffness of clathrin coats lacking light chain subunits.

Conclusions:

  • Clathrin light chains are critical for maintaining clathrin coat flexibility.
  • AP2 modulates clathrin coat stiffness, likely facilitating efficient cargo sequestration during vesicle formation.
  • The findings suggest a model where clathrin coat mechanics, influenced by AP2 and light chains, are finely tuned for endocytosis.