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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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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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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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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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Solution Formation02:16

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There is no one solvent that can dissolve every type of solute. Some substances that readily dissolve in a certain solvent might be insoluble in a different solvent. A simple way to predict which substances dissolve in which solvent is the phrase "like dissolves like". This means that polar substances, such as salt and sugar, dissolve in a polar substance like water. In contrast, non-polar substances are more soluble in non-polar solvents such as carbon tetrachloride.
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Related Experiment Video

Updated: Feb 6, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Measuring Clathrin-Coated Vesicle Formation with Single-Molecule Resolution.

François Aguet1, Emanuele Cocucci2

  • 1The Broad Institute of MIT and Harvard, Cambridge, MA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|August 22, 2018
PubMed
Summary

This study details a quantitative fluorescence microscopy method to analyze molecular assembly, specifically clathrin-coated vesicles. The protocol offers insights into molecular stoichiometry and kinetics for broader biological applications.

Keywords:
Clathrin-coated vesiclesImagingSingle moleculeTIRF

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Area of Science:

  • Biophysics
  • Cell Biology
  • Molecular Imaging

Background:

  • High-resolution fluorescence microscopy is crucial for understanding molecular mechanisms.
  • Quantitative imaging provides insights into molecular assembly stoichiometry and kinetics.
  • Clathrin-coated vesicles play vital roles in cellular transport.

Purpose of the Study:

  • To describe a method for studying clathrin-coated vesicle assembly using single-molecule resolution.
  • To enable quantitative analysis of molecular processes with fluorescence microscopy.
  • To provide a broadly applicable protocol for characterizing molecular assemblies.

Main Methods:

  • Utilizing total internal reflection fluorescence microscopy (TIRFm).
  • Employing single-molecule intensity analysis for quantitative measurements.
  • Detailing experimental and analytical steps for vesicle assembly studies.

Main Results:

  • Demonstrated the ability to achieve single-molecule resolution in imaging molecular assembly.
  • Provided quantitative data on the stoichiometry and kinetics of clathrin-coated vesicle formation.
  • Validated the applicability of the method for studying complex molecular processes.

Conclusions:

  • The described protocol enables quantitative, single-molecule resolution studies of molecular assembly.
  • This method offers valuable insights into the dynamics of clathrin-coated vesicles.
  • The protocol's components are adaptable for characterizing diverse molecular systems.