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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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...
COP Coated Vesicles00:59

COP Coated Vesicles

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 different...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
Transport Across the Golgi01:26

Transport Across the Golgi

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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Related Experiment Video

Updated: Jun 24, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

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

Published on: October 20, 2014

Cargo and dynamin regulate clathrin-coated pit maturation.

Dinah Loerke1, Marcel Mettlen, Defne Yarar

  • 1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA, USA.

Plos Biology
|March 20, 2009
PubMed
Summary
This summary is machine-generated.

Researchers used advanced microscopy to track clathrin-coated pits (CCPs) during endocytosis. They discovered distinct CCP types and identified cargo and dynamin as key regulators of vesicle formation.

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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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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
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Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

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Related Experiment Videos

Last Updated: Jun 24, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
12:40

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

Published on: October 20, 2014

In vivo and in vitro Studies of Adaptor-clathrin Interaction
17:14

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
08:02

Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells

Published on: October 17, 2025

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Clathrin-mediated endocytosis (CME) is crucial for cellular processes.
  • Total internal reflection fluorescence microscopy (TIR-FM) is a key technique for studying CME.
  • Previous analyses of clathrin-coated pits (CCPs) were limited by tracking difficulties.

Purpose of the Study:

  • To identify intermediates in clathrin-coated vesicle formation.
  • To uncover factors regulating CCP progression.
  • To establish an unbiased inventory of CCP dynamics.

Main Methods:

  • Utilized particle-tracking software and statistical analysis of TIR-FM data.
  • Categorized CCPs into distinct dynamic subpopulations.
  • Employed small interfering RNA (siRNA) to deplete dynamin-2 and reintroduced dynamin-1 variants.

Main Results:

  • Identified three dynamically distinct CCP subpopulations: two short-lived (aborted) and one longer-lived (productive).
  • Cargo concentration, modulated by AP2 adaptor complexes, enhances productive CCP maturation efficiency.
  • Dynamin regulates abortive intermediate turnover and CCP maturation rate.

Conclusions:

  • Infer the existence of a cargo-responsive, dynamin-regulated endocytic checkpoint.
  • Dynamin plays a critical role in controlling the fidelity and efficiency of endocytosis.
  • Cargo availability influences the maturation of productive CCPs.