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Related Concept Videos

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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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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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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Transport Across the Golgi01:26

Transport Across the Golgi

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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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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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Related Experiment Video

Updated: Apr 8, 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

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Cargo regulates clathrin-coated pit dynamics.

Manojkumar A Puthenveedu1, Mark von Zastrow

  • 1Department of Psychiatry, University of California at San Francisco, 600 16th Street, San Francisco, CA 94158, USA.

Cell
|October 5, 2006
PubMed
Summary
This summary is machine-generated.

Regulated endocytosis of G protein-coupled receptors (GPCRs) uses a specific subset of clathrin-coated pits (CCPs). This cargo-specific regulation of CCPs allows for functional specialization in the endocytic pathway.

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

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Clathrin-coated pits (CCPs) are key endocytic machines.
  • CCPs are typically viewed as a uniform population handling diverse membrane cargo.
  • The specific mechanisms governing cargo segregation and CCP dynamics remain incompletely understood.

Purpose of the Study:

  • To investigate whether specific cargo, like G protein-coupled receptors (GPCRs), utilize distinct CCP subsets for endocytosis.
  • To determine if GPCR-containing CCPs exhibit unique functional properties.
  • To elucidate the regulatory mechanisms controlling CCP dynamics based on cargo content.

Main Methods:

  • Live-cell imaging to observe CCP dynamics and cargo trafficking.
  • Biochemical assays to analyze protein-protein interactions, including PDZ-domain mediated linkages.
  • Perturbation studies to assess the impact of cargo on CCP assembly and disassembly.

Main Results:

  • Regulated endocytosis of GPCRs preferentially occurs via a specialized subset of CCPs.
  • GPCR-containing CCPs exhibit prolonged surface residence times, regulated by cargo-actin cytoskeleton interactions.
  • These specialized CCPs show delayed dynamin recruitment and can experience abortive events, uncoupling coat disassembly from cargo internalization.

Conclusions:

  • Endocytic cargo, such as GPCRs, can segregate into distinct CCP subsets.
  • Cargo-dependent regulation of CCP dynamics provides a kinetic mechanism for functional specialization.
  • This specialization optimizes the early endocytic pathway and mitigates competition among different cargo types.