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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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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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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...
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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...
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Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
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Related Experiment Video

Updated: Apr 30, 2026

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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Key interactions for clathrin coat stability.

Till Böcking1, François Aguet2, Iris Rapoport3

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Centre for Vascular Research, University of New South Wales, Sydney NSW 2052 Australia.

Structure (London, England : 1993)
|May 13, 2014
PubMed
Summary
This summary is machine-generated.

Histidine residues are key to clathrin coat assembly and stability in cells. Modifying these histidines makes the clathrin coat easier to disassemble, impacting vesicular transport.

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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Clathrin-coated vesicles mediate essential vesicular transport in eukaryotic cells.
  • The clathrin endocytic pathway involves coat assembly and disassembly.
  • Hsc70 chaperones play a critical role in clathrin coat disassembly.

Purpose of the Study:

  • To identify key residues determining clathrin coat assembly and stability.
  • To investigate the role of histidine residues in clathrin lattice structure.
  • To examine the impact of histidine mutations on Hsc70-mediated coat disassembly.

Main Methods:

  • Site-directed mutagenesis of histidine residues in clathrin heavy chains.
  • Analysis of pH-dependent clathrin coat stability.
  • Single-particle fluorescence imaging to monitor coat uncoating dynamics.
  • Modeling of Hsc70-mediated disassembly.

Main Results:

  • Histidine residues at the interface of clathrin heavy chain segments are crucial for lattice assembly and stability.
  • Mutating histidine to glutamine alters the pH sensitivity of coat stability.
  • Destabilized clathrin coats require less Hsc70 for disassembly initiation.
  • Experimental results align with models of Hsc70 trapping conformational distortions.

Conclusions:

  • Histidine residues are critical determinants of clathrin coat structure and function.
  • Targeting these histidine residues offers a way to modulate clathrin coat disassembly.
  • Understanding these mechanisms provides insights into vesicular trafficking regulation.